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Conserved domains on  [gi|1715121658|dbj|GBN59503|]
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putative ATP-dependent RNA helicase DDX46 [Araneus ventricosus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
72-492 1.53e-161

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.53e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleadDGPLAIIMTPTREL 151
Cdd:COG0513     8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDM 231
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 232 GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKLLELLGYYQ 311
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 312 DQgSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCP 391
Cdd:COG0513   241 PE-RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 392 NHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQEMEGKKVKSSSGFSGKG 471
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRG 399
                         410       420
                  ....*....|....*....|.
gi 1715121658 472 FKFDEAEAQLANEKKKFQKAA 492
Cdd:COG0513   400 GRPGPKGERKARRGKRRRRKR 420
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
617-719 3.24e-64

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


:

Pssm-ID: 411901  Cd Length: 103  Bit Score: 208.32  E-value: 3.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 617 TFRKYEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNELAVSKARAEFIR 696
Cdd:cd22473     1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                          90       100
                  ....*....|....*....|...
gi 1715121658 697 LIKEELVKLQHSYQPINRGRYKV 719
Cdd:cd22473    81 LIKEELLRLQASYQPINKGRYKV 103
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
545-598 7.56e-03

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


The actual alignment was detected with superfamily member cd07067:

Pssm-ID: 472174 [Multi-domain]  Cd Length: 153  Bit Score: 37.69  E-value: 7.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 545 ELAKKLASRIS---------LQRnigaeAQQTAEAVLKGHLGTPVISAKTLAEQRAEKLHAKL 598
Cdd:cd07067    36 ALGKRLKELGIkfdriysspLKR-----AIQTAEIILEELPGLPVEVDPRLREARVLPALEEL 93
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
72-492 1.53e-161

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.53e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleadDGPLAIIMTPTREL 151
Cdd:COG0513     8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDM 231
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 232 GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKLLELLGYYQ 311
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 312 DQgSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCP 391
Cdd:COG0513   241 PE-RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 392 NHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQEMEGKKVKSSSGFSGKG 471
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRG 399
                         410       420
                  ....*....|....*....|.
gi 1715121658 472 FKFDEAEAQLANEKKKFQKAA 492
Cdd:COG0513   400 GRPGPKGERKARRGKRRRRKR 420
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
55-276 1.75e-161

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: 464.54  E-value: 1.75e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  55 KVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAL 134
Cdd:cd17953     1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 135 EADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNL 214
Cdd:cd17953    81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715121658 215 RRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17953   161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
10-455 2.97e-159

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 471.18  E-value: 2.97e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  10 KKLLTVTKEDVTYQPFRKNFYVEVPELARMTSEEVEALRTDLEGIKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKP 89
Cdd:PTZ00110   74 KRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLR 169
Cdd:PTZ00110  154 TPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIR 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQ 249
Cdd:PTZ00110  234 NTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQ 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 250 TVLFSATFPRQMEALARRILT-KPIEVQVGGRSV-VCKDVEQHVVVIEEDGKFLKLLELLG-YYQDQGSALVFVDKQENA 326
Cdd:PTZ00110  311 TLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQrIMRDGDKILIFVETKKGA 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 327 DLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGR 406
Cdd:PTZ00110  391 DFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1715121658 407 AGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQE 455
Cdd:PTZ00110  471 AGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTE 519
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
617-719 3.24e-64

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411901  Cd Length: 103  Bit Score: 208.32  E-value: 3.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 617 TFRKYEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNELAVSKARAEFIR 696
Cdd:cd22473     1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                          90       100
                  ....*....|....*....|...
gi 1715121658 697 LIKEELVKLQHSYQPINRGRYKV 719
Cdd:cd22473    81 LIKEELLRLQASYQPINKGRYKV 103
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
90-264 3.45e-63

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: 207.87  E-value: 3.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQpaleaDDGPLAIIMTPTRELAMQITKECKKFTKALSLR 169
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL-----DNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAansgRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQ 249
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                         170
                  ....*....|....*
gi 1715121658 250 TVLFSATFPRQMEAL 264
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
81-290 5.47e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 190.01  E-value: 5.47e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658   81 LKKQNYEKPTPIQAQAIPCIMSG-KDLIGIAKTGSGKTLAFLLPMFRHILDQPaleaddGPLAIIMTPTRELAMQITKEC 159
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK------GGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  160 KKFTKALSLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVM 238
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1715121658  239 RIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRsvVCKDVEQH 290
Cdd:smart00487 152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQF 201
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
545-598 7.56e-03

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 37.69  E-value: 7.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 545 ELAKKLASRIS---------LQRnigaeAQQTAEAVLKGHLGTPVISAKTLAEQRAEKLHAKL 598
Cdd:cd07067    36 ALGKRLKELGIkfdriysspLKR-----AIQTAEIILEELPGLPVEVDPRLREARVLPALEEL 93
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
72-492 1.53e-161

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 472.32  E-value: 1.53e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleadDGPLAIIMTPTREL 151
Cdd:COG0513     8 GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDM 231
Cdd:COG0513    84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLI--ERGAL-DLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 232 GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKLLELLGYYQ 311
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 312 DQgSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCP 391
Cdd:COG0513   241 PE-RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 392 NHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQEMEGKKVKSSSGFSGKG 471
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRG 399
                         410       420
                  ....*....|....*....|.
gi 1715121658 472 FKFDEAEAQLANEKKKFQKAA 492
Cdd:COG0513   400 GRPGPKGERKARRGKRRRRKR 420
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
55-276 1.75e-161

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: 464.54  E-value: 1.75e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  55 KVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAL 134
Cdd:cd17953     1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 135 EADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNL 214
Cdd:cd17953    81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715121658 215 RRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17953   161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
PTZ00110 PTZ00110
helicase; Provisional
10-455 2.97e-159

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 471.18  E-value: 2.97e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  10 KKLLTVTKEDVTYQPFRKNFYVEVPELARMTSEEVEALRTDLEGIKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKP 89
Cdd:PTZ00110   74 KRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLR 169
Cdd:PTZ00110  154 TPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIR 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQ 249
Cdd:PTZ00110  234 NTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQ 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 250 TVLFSATFPRQMEALARRILT-KPIEVQVGGRSV-VCKDVEQHVVVIEEDGKFLKLLELLG-YYQDQGSALVFVDKQENA 326
Cdd:PTZ00110  311 TLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLLQrIMRDGDKILIFVETKKGA 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 327 DLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGR 406
Cdd:PTZ00110  391 DFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1715121658 407 AGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQE 455
Cdd:PTZ00110  471 AGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTE 519
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
77-275 7.72e-101

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: 307.80  E-value: 7.72e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQIT 156
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQ 236
Cdd:cd17952    81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKA---TNLQRVTYLVLDEADRMFDMGFEYQ 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1715121658 237 VMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17952   158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
78-462 8.55e-101

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 317.51  E-value: 8.55e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  78 LDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHI-LDQPALEAddgplaIIMTPTRELAMQIT 156
Cdd:PRK11776   16 LANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdVKRFRVQA------LVLCPTRELADQVA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKAL-SLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEP 235
Cdd:PRK11776   90 KEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGT---LDLDALNTLVLDEADRMLDMGFQD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 236 QVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKdVEQHVVVIEEDGKFLKLLELLGYYQDQgS 315
Cdd:PRK11776  167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLLHHQPE-S 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 316 ALVFVD-KQENADLLlKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHI 394
Cdd:PRK11776  245 CVVFCNtKKECQEVA-DALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDP 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 395 EDYVHRCGRTGRAGNKGYAYTFVTQEQGRYAGDIIKALEQGSNPVPEDLQKLWDEYKLKQEME------GKKVK 462
Cdd:PRK11776  324 EVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVtlcidgGKKDK 397
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
77-276 4.57e-98

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: 300.44  E-value: 4.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQIT 156
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQ 236
Cdd:cd17966    81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGK---TNLRRVTYLVLDEADRMLDMGFEPQ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1715121658 237 VMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17966   158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
77-276 3.37e-97

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: 298.20  E-value: 3.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAlEADDGPLAIIMTPTRELAMQIT 156
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDMGFEPQ 236
Cdd:cd00268    80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLI--ERGKL-DLSNVKYLVLDEADRMLDMGFEED 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1715121658 237 VMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd00268   157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
17-278 2.81e-93

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: 291.14  E-value: 2.81e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  17 KEDVTYQP-FRKNFYVEVPELARMTSEEVEALRTDLEgIKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQ 95
Cdd:cd18050    13 KWDLSELPkFEKNFYVEHPEVARMTQYDVEELRRKKE-ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  96 AIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYG 175
Cdd:cd18050    92 GFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 176 GTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQTVLFSA 255
Cdd:cd18050   172 GAPKGPQIRDLERGVEICIATPGRLIDFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSA 248
                         250       260
                  ....*....|....*....|...
gi 1715121658 256 TFPRQMEALARRILTKPIEVQVG 278
Cdd:cd18050   249 TWPKEVRQLAEDFLRDYVQINIG 271
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
72-434 9.09e-89

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 285.93  E-value: 9.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPL-AIIMTPTRE 150
Cdd:PRK10590    7 GLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 151 LAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFD 230
Cdd:PRK10590   87 LAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNA---VKLDQVEILVLDEADRMLD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 231 MGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKflklLELLGYY 310
Cdd:PRK10590  164 MGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRK----RELLSQM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 311 QDQGS---ALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVN 387
Cdd:PRK10590  240 IGKGNwqqVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1715121658 388 YDCPNHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGRYAGDIIKALEQ 434
Cdd:PRK10590  320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
42-279 1.41e-87

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: 274.96  E-value: 1.41e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  42 EEVEALRTDLEgIKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFL 121
Cdd:cd18049     1 QEVEQYRRSKE-ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 122 LPMFRHILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMI 201
Cdd:cd18049    80 LPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1715121658 202 DMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGG 279
Cdd:cd18049   160 DFLEAGK---TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
29-443 1.79e-84

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 276.28  E-value: 1.79e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  29 FYVEVPEL-ARMTSEEVEALRTDLEgIKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLI 107
Cdd:PLN00206   84 FYVRDPGStSGLSSSQAELLRRKLE-IHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 108 GIAKTGSGKTLAFLLPMFRH--ILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAE 185
Cdd:PLN00206  163 VSADTGSGKTASFLVPIISRccTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYR 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 186 LKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTrPDRQTVLFSATFPRQMEALA 265
Cdd:PLN00206  243 IQQGVELIVGTPGRLIDLLSKHD---IELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFA 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 266 RRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKLLELLGYYQD-QGSALVFVDKQENADLLLKDLIKAS-YNCMAL 343
Cdd:PLN00206  319 SSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHfKPPAVVFVSSRLGADLLANAITVVTgLKALSI 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 344 HGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGR 423
Cdd:PLN00206  399 HGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRN 478
                         410       420
                  ....*....|....*....|
gi 1715121658 424 YAGDIIKALEQGSNPVPEDL 443
Cdd:PLN00206  479 LFPELVALLKSSGAAIPREL 498
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
77-278 4.39e-83

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: 262.42  E-value: 4.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDG-----PLAIIMTPTREL 151
Cdd:cd17967    11 LLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSALILAPTREL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDM 231
Cdd:cd17967    91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI--ERGRI-SLSSIKFLVLDEADRMLDM 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1715121658 232 GFEPQVMRIVDG-TRP---DRQTVLFSATFPRQMEALARRILTKPIEVQVG 278
Cdd:cd17967   168 GFEPQIRKIVEHpDMPpkgERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
66-491 2.67e-80

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 262.57  E-value: 2.67e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  66 KNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleADDGPLAI-I 144
Cdd:PRK11192    1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR--RKSGPPRIlI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 145 MTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDE 224
Cdd:PRK11192   79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN---FDCRAVETLILDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 225 ADRMFDMGFEPQVMRIVDGTRPDRQTVLFSATFP-RQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKL 303
Cdd:PRK11192  156 ADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 304 LELLGYYQDQGSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLI 383
Cdd:PRK11192  236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 384 LVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFV-------TQEQGRYAGDIIKAleqgsnPVPEDLqklwdEYKLKQEM 456
Cdd:PRK11192  316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVeahdhllLGKIERYIEEPLKA------RVIDEL-----RPKTKAPS 384
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1715121658 457 EGKKVKSSSGFSGKGFKFDEAEAQLANEKKKFQKA 491
Cdd:PRK11192  385 EKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRHRDT 419
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
68-423 1.67e-79

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 266.33  E-value: 1.67e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  68 WAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIldQPALEAddgPLAIIMTP 147
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELKA---PQILVLAP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 148 TRELAMQITKECKKFTKAL-SLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRvtyLVLDEAD 226
Cdd:PRK11634   83 TRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSG---LVLDEAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 227 RMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQH---VVVIEEDGKFLKL 303
Cdd:PRK11634  160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSywtVWGMRKNEALVRF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 304 LELlgyyQDQGSALVFVdKQENADLLLKD-LIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHL 382
Cdd:PRK11634  240 LEA----EDFDAAIIFV-RTKNATLEVAEaLERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1715121658 383 ILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFVTQEQGR 423
Cdd:PRK11634  315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR 355
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
77-275 6.29e-79

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: 251.47  E-value: 6.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEA---DDGPLAIIMTPTRELAM 153
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEetkDDGPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 154 QITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaanSGRVTNLRRVTYLVLDEADRMFDMGF 233
Cdd:cd17945    81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCL---ERRLLVLNQCTYVVLDEADRMIDMGF 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1715121658 234 EPQVMRIVD--------------------GTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17945   158 EPQVTKILDampvsnkkpdteeaeklaasGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
77-275 1.93e-75

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: 241.60  E-value: 1.93e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAL-EADDGPLAIIMTPTRELAMQI 155
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 156 TKECKKFTKAlSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYLVLDEADRMFDMGFEP 235
Cdd:cd17958    81 EAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNN---VINLKSITYLVLDEADRMLDMGFEP 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1715121658 236 QVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17958   157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
54-269 7.12e-75

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: 242.57  E-value: 7.12e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  54 IKVKGKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLP----MFRHIL 129
Cdd:cd18052    31 VEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltgMMKEGL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 130 DQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSG 209
Cdd:cd18052   111 TASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI--GRG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 210 RVtNLRRVTYLVLDEADRMFDMGFEPQVMRIVD----GTRPDRQTVLFSATFPRQMEALARRIL 269
Cdd:cd18052   189 KI-SLSKLKYLILDEADRMLDMGFGPEIRKLVSepgmPSKEDRQTLMFSATFPEEIQRLAAEFL 251
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
90-432 2.86e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 247.90  E-value: 2.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEAD--DGPLAIIMTPTRELAMQITKECKKFTKALS 167
Cdd:PRK01297  111 TPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERymGEPRALIIAPTRELVVQIAKDAAALTKYTG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 168 LRVVCVYGGTGISEQIAELK-RGAEIIVCTPGRMIDMlaaNSGRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRP 246
Cdd:PRK01297  191 LNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDF---NQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPR 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 247 --DRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFlKLLELLGYYQDQGSALVFVDKQE 324
Cdd:PRK01297  268 keERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKY-KLLYNLVTQNPWERVMVFANRKD 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 325 NADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRT 404
Cdd:PRK01297  347 EVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRT 426
                         330       340
                  ....*....|....*....|....*...
gi 1715121658 405 GRAGNKGYAYTFVTQEQGRYAGDIIKAL 432
Cdd:PRK01297  427 GRAGASGVSISFAGEDDAFQLPEIEELL 454
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
81-443 1.92e-71

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 243.32  E-value: 1.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALeAD---DGPLAIIMTPTRELAMQITK 157
Cdd:PRK04537   24 LESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAL-ADrkpEDPRALILAPTRELAIQIHK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 158 ECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgRVTNLRRVTYLVLDEADRMFDMGFEPQV 237
Cdd:PRK04537  103 DAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH--KVVSLHACEICVLDEADRMFDLGFIKDI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 238 MRIVD--GTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIEEDGKFLKLLELLGyyQDQGS 315
Cdd:PRK04537  181 RFLLRrmPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLGLLS--RSEGA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 316 -ALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHI 394
Cdd:PRK04537  259 rTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDA 338
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 395 EDYVHRCGRTGRAGNKGYAYTFVTQeqgRYA---GDIIKALEQG--SNPVPEDL 443
Cdd:PRK04537  339 EDYVHRIGRTARLGEEGDAISFACE---RYAmslPDIEAYIEQKipVEPVTAEL 389
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
52-278 2.82e-70

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: 229.93  E-value: 2.82e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  52 EGIKVK--GKGCPKPIKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIL 129
Cdd:cd18051     5 EDIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 130 DQ---PALEADDG--------PLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPG 198
Cdd:cd18051    85 EQgpgESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 199 RMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDMGFEPQVMRIVD-GTRP---DRQTVLFSATFPRQMEALARRILTKPIE 274
Cdd:cd18051   165 RLVDML--ERGKI-GLDYCKYLVLDEADRMLDMGFEPQIRRIVEqDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIF 241

                  ....
gi 1715121658 275 VQVG 278
Cdd:cd18051   242 LAVG 245
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
66-425 2.87e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 235.64  E-value: 2.87e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  66 KNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEA--DDGPLAI 143
Cdd:PRK04837    8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkVNQPRAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 144 IMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANsgrVTNLRRVTYLVLD 223
Cdd:PRK04837   88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN---HINLGAIQVVVLD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 224 EADRMFDMGFepqvmrIVDgTR------PD---RQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVI 294
Cdd:PRK04837  165 EADRMFDLGF------IKD-IRwlfrrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 295 EEDGKFLKLLELLGY-YQDQgsALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVA 373
Cdd:PRK04837  238 SNEEKMRLLQTLIEEeWPDR--AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1715121658 374 ARGL---DVKHlilVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFVTQEqgrYA 425
Cdd:PRK04837  316 ARGLhipAVTH---VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE---YA 364
KH-I_DDX46 cd22473
type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar ...
617-719 3.24e-64

type I K homology (KH) RNA-binding domain found in DEAD box protein 46 (DDX46) and similar proteins; DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411901  Cd Length: 103  Bit Score: 208.32  E-value: 3.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 617 TFRKYEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNELAVSKARAEFIR 696
Cdd:cd22473     1 TFKRYEEELEINDFPQTARWKVTSKEALAQISEYSEAGITVRGTYFPPGKEPKEGERKLYLAIEAASERAVQKAKAEITR 80
                          90       100
                  ....*....|....*....|...
gi 1715121658 697 LIKEELVKLQHSYQPINRGRYKV 719
Cdd:cd22473    81 LIKEELLRLQASYQPINKGRYKV 103
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
72-276 2.21e-63

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: 209.85  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQpalEADDGPLAIIMTPTREL 151
Cdd:cd17959     7 GLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH---SPTVGARALILSPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDM 231
Cdd:cd17959    84 ALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN---LKLSSVEYVVFDEADRLFEM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1715121658 232 GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
77-275 2.58e-63

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: 209.50  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQP---ALEADDGPLAIIMTPTRELAM 153
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 154 QITKECKKFTKALS------LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAAnsgRVTNLRRVTYLVLDEADR 227
Cdd:cd17951    81 QTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNK---KKINLDICRYLCLDEADR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1715121658 228 MFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17951   158 MIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
90-264 3.45e-63

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: 207.87  E-value: 3.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQpaleaDDGPLAIIMTPTRELAMQITKECKKFTKALSLR 169
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL-----DNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCVYGGTGISEQIAELKrGAEIIVCTPGRMIDMLAansgRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQ 249
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQ 150
                         170
                  ....*....|....*
gi 1715121658 250 TVLFSATFPRQMEAL 264
Cdd:pfam00270 151 ILLLSATLPRNLEDL 165
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
77-278 6.29e-62

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: 205.52  E-value: 6.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQpalEADDGPLAIIMTPTRELAMQIT 156
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVYGGT-GISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEP 235
Cdd:cd17957    78 RELLKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP---IDLSSVEYLVLDEADKLFEPGFRE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1715121658 236 QVMRIVDG-TRPDRQTVLFSATFPRQMEALARRILTKPIEVQVG 278
Cdd:cd17957   155 QTDEILAAcTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
PTZ00424 PTZ00424
helicase 45; Provisional
86-420 6.90e-62

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 212.76  E-value: 6.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  86 YEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIldQPALEADDgplAIIMTPTRELAMQITKECKKFTKA 165
Cdd:PTZ00424   48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--DYDLNACQ---ALILAPTRELAQQIQKVVLALGDY 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 166 LSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYLVLDEADRMFDMGFEPQVMRIVDGTR 245
Cdd:PTZ00424  123 LKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLK---LFILDEADEMLSRGFKGQIYDVFKKLP 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 246 PDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRSVVCKDVEQHVVVIE-EDGKFLKLLEL---LGYYQdqgsALVFVD 321
Cdd:PTZ00424  200 PDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEkEEWKFDTLCDLyetLTITQ----AIIYCN 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 322 KQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRC 401
Cdd:PTZ00424  276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRI 355
                         330
                  ....*....|....*....
gi 1715121658 402 GRTGRAGNKGYAYTFVTQE 420
Cdd:PTZ00424  356 GRSGRFGRKGVAINFVTPD 374
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
73-271 5.57e-60

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: 200.89  E-value: 5.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  73 VSKKVLDILKKQNYEKPTPIQAQAI-PCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTREL 151
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKAL-SLRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLAANSGRVTnLRRVTYLVLDEADRMF 229
Cdd:cd17964    81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKA-FTDLDYLVLDEADRLL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1715121658 230 DMGFEPQVMRIVDGTRP----DRQTVLFSATFPRQMEALARRILTK 271
Cdd:cd17964   160 DMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
68-276 4.45e-59

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: 198.31  E-value: 4.45e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  68 WAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleaddgPL-AIIMT 146
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ------RFfALVLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 147 PTRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGrvTNLRRVTYLVLDEAD 226
Cdd:cd17954    76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKG--FSLKSLKFLVMDEAD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1715121658 227 RMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17954   154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEXDc smart00487
DEAD-like helicases superfamily;
81-290 5.47e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 190.01  E-value: 5.47e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658   81 LKKQNYEKPTPIQAQAIPCIMSG-KDLIGIAKTGSGKTLAFLLPMFRHILDQPaleaddGPLAIIMTPTRELAMQITKEC 159
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK------GGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  160 KKFTKALSLRVVCVYGGTGISEQIAELKRG-AEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVM 238
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK---LSLSNVDLVILDEAHRLLDGGFGDQLE 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1715121658  239 RIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQVGGRsvVCKDVEQH 290
Cdd:smart00487 152 KLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQF 201
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
77-275 1.98e-55

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: 188.17  E-value: 1.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDGPLAIIMTPTRELAMQIT 156
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALS--LRVVCVYGGTGISEQIAELKR-GAEIIVCTPGRMIDMLAANSGRVtNLRRVTYLVLDEADRMFDMGF 233
Cdd:cd17960    81 EVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKV-KVKSLEVLVLDEADRLLDLGF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1715121658 234 EPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17960   160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
77-276 3.34e-55

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: 187.46  E-value: 3.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEAddGPLAIIMTPTRELAMQIT 156
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKA--ATRVLVLVPTRELAMQCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaANSGRVTnLRRVTYLVLDEADRMFDMGFEPQ 236
Cdd:cd17947    79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHL-RNSPSFD-LDSIEILVLDEADRMLEEGFADE 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1715121658 237 VMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17947   157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
287-417 1.79e-54

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: 183.09  E-value: 1.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 287 VEQHVVVIEEDGKFLKLLELLGYYQDQGSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSV 366
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1715121658 367 LIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFV 417
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
72-276 1.65e-53

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: 183.19  E-value: 1.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPmfrhILDQpaLEADD-GPLAIIMTPTRE 150
Cdd:cd17955     5 GLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP----ILQR--LSEDPyGIFALVLTPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 151 LAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYLVLDEADRMFD 230
Cdd:cd17955    79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVLSRVKFLVLDEADRLLT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1715121658 231 MGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17955   159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
77-257 8.80e-52

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: 179.74  E-value: 8.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIP-CIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQ----PALEADDGPLAIIMTPTREL 151
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYLVLDEADRMFDM 231
Cdd:cd17946    81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEK 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1715121658 232 G-FEpQVMRIVD-------GTRPDRQTVLFSATF 257
Cdd:cd17946   161 GhFA-ELEKILEllnkdraGKKRKRQTFVFSATL 193
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
81-275 6.60e-51

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: 175.81  E-value: 6.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHildqpALEADDGPLAIIMTPTRELAMQITKECK 160
Cdd:cd17962     5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR-----CLTEHRNPSALILTPTRELAVQIEDQAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 161 KFTKAL-SLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMFDMGFEPQVMR 239
Cdd:cd17962    80 ELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSS---VELDNIKIVVVDEADTMLKMGFQQQVLD 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1715121658 240 IVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17962   157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
85-275 8.04e-51

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: 175.95  E-value: 8.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  85 NYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHI-LDQPALEAddgplaIIMTPTRELAMQITKECKKFT 163
Cdd:cd17940    18 GFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQA------LILVPTRELALQTSQVCKELG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 164 KALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaanSGRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDG 243
Cdd:cd17940    92 KHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLA---KKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNF 168
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1715121658 244 TRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17940   169 LPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
81-277 5.27e-50

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: 173.24  E-value: 5.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHiLDQPALEADDGPLAIIMTPTRELAMQITKECK 160
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEK-LYRERWTPEDGLGALIISPTRELAMQIFEVLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 161 KFTKALSLRVVCVYGGTGISEqiaELKRGAE--IIVCTPGRMIDMLAANSGRVTNLRRVtyLVLDEADRMFDMGFEPQVM 238
Cdd:cd17941    84 KVGKYHSFSAGLIIGGKDVKE---EKERINRmnILVCTPGRLLQHMDETPGFDTSNLQM--LVLDEADRILDMGFKETLD 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1715121658 239 RIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQV 277
Cdd:cd17941   159 AIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
77-273 1.53e-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: 172.77  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIL-DQPALEADDGPLAIIMTPTRELAMQI 155
Cdd:cd17949     2 VSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 156 TKECKKFTKALSLRVVC-VYGGTGISEQIAELKRGAEIIVCTPGRMIDML-AANSGRVTNLRrvtYLVLDEADRMFDMGF 233
Cdd:cd17949    82 YEVLEKLLKPFHWIVPGyLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLR---WLVLDEADRLLDMGF 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 234 EPQVMRIV----DGTR---------PDRQTVLFSATFPRQMEALARRILTKPI 273
Cdd:cd17949   159 EKDITKILelldDKRSkaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
81-275 1.10e-45

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: 161.37  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFrHILDQPALEADDGPLAIIMTPTRELAMQITKECK 160
Cdd:cd17942     5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-ELLYKLKFKPRNGTGVIIISPTRELALQIYGVAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 161 KFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVT-NLRrvtYLVLDEADRMFDMGFEPQVMR 239
Cdd:cd17942    84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYkNLQ---CLIIDEADRILEIGFEEEMRQ 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1715121658 240 IVDGTRPDRQTVLFSATFPRQMEALARRIL-TKPIEV 275
Cdd:cd17942   161 IIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
81-273 9.27e-43

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: 153.89  E-value: 9.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEA-DDGPLAIIMTPTRELAMQITKEC 159
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGeEQGTRALILVPTRELAQQVSKVL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 160 KKFTKALS--LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYLVLDEADRMFDMGFEPQV 237
Cdd:cd17961    89 EQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHL--ESGSLLLLSTLKYLVIDEADLVLSYGYEEDL 166
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1715121658 238 MRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPI 273
Cdd:cd17961   167 KSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
77-275 6.31e-41

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: 148.11  E-value: 6.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSG--KDLIGIAKTGSGKTLAFLLPMFRHIldQPALEAddgPLAIIMTPTRELAMQ 154
Cdd:cd17963     5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKS---PQALCLAPTRELARQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 155 ITKECKKFTKALSLRVVC------VYGGTGISEQIaelkrgaeiIVCTPGRMIDMLAAnsgRVTNLRRVTYLVLDEADRM 228
Cdd:cd17963    80 IGEVVEKMGKFTGVKVALavpgndVPRGKKITAQI---------VIGTPGTVLDWLKK---RQLDLKKIKILVLDEADVM 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1715121658 229 FDM-GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17963   148 LDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
86-275 1.83e-40

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: 147.09  E-value: 1.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  86 YEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHI-LDQPALEAddgplaIIMTPTRELAMQITKECKKFTK 164
Cdd:cd17939    17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQA------LVLAPTRELAQQIQKVVKALGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 165 ALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYLVLDEADRMFDMGFEPQVMRIVDGT 244
Cdd:cd17939    91 YMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIK---MFVLDEADEMLSRGFKDQIYDIFQFL 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1715121658 245 RPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd17939   168 PPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
77-268 4.84e-39

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: 144.05  E-value: 4.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEAD--DGPLAIIMTPTRELAMQ 154
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 155 ITKECKKFTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRmidMLAANSGRVTNLRRVTYLVLDEADRMFDMGFE 234
Cdd:cd17948    81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGA---LSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1715121658 235 PQVMRIV-------------DGTRPDRQTVLFSATFPRQMEALARRI 268
Cdd:cd17948   158 EKLSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGVGEVLSKV 204
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
77-276 1.97e-38

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: 141.25  E-value: 1.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMfrhiLDQPALEAdDGPLAIIMTPTRELAMQIT 156
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIA----LESLDLER-RHPQVLILAPTREIAVQIH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFTKALSLRVVCVY-GGTGISEQIAELKRgAEIIVCTPGRMIDMLAANSGRVTNLRrvtYLVLDEADRMFDMGFEP 235
Cdd:cd17943    76 DVFKKIGKKLEGLKCEVFiGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVR---LFVLDEADKLMEGSFQK 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1715121658 236 QVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQ 276
Cdd:cd17943   152 DVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
KH-I_AtRH42_like cd22475
type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent ...
621-719 3.66e-38

type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins; RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411903  Cd Length: 102  Bit Score: 137.14  E-value: 3.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 621 YEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNELAVSKARAEfIRLIKE 700
Cdd:cd22475     5 FEEELEINDFPQHARWKVTHKDTLGQISELTGAAITTRGQYYPPGRIPGPGERKLYLLIEGPSEASVKEAKAE-IKRILE 83
                          90
                  ....*....|....*....
gi 1715121658 701 ELVKLQHSYQPINRGRYKV 719
Cdd:cd22475    84 EATEKASRPGGQQPGRYSV 102
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
91-274 8.28e-38

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: 139.60  E-value: 8.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  91 PIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHI-LDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKALSlr 169
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqEDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKLS-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVtylVLDEADRMFDMGFEPQVMRIVD-----GT 244
Cdd:cd17944    93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHV---VLDEVDQMLDMGFAEQVEEILSvsykkDS 169
                         170       180       190
                  ....*....|....*....|....*....|
gi 1715121658 245 RPDRQTVLFSATFPRQMEALARRILTKPIE 274
Cdd:cd17944   170 EDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
86-256 1.15e-37

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: 139.38  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  86 YEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIldqpaleaddgpLAIIMTPTRELAMQiTKEC----KK 161
Cdd:cd17938    19 WLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV------------VALILEPSRELAEQ-TYNCienfKK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 162 FTKALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVtNLRRVTYLVLDEADRMFDMGFEPQVMRI- 240
Cdd:cd17938    86 YLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLI--KTGKL-DLSSVRFFVLDEADRLLSQGNLETINRIy 162
                         170       180
                  ....*....|....*....|...
gi 1715121658 241 -------VDGTRpdRQTVLFSAT 256
Cdd:cd17938   163 nripkitSDGKR--LQVIVCSAT 183
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
86-277 7.69e-36

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: 134.39  E-value: 7.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  86 YEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPmfrhILDQpaLEADDGPL-AIIMTPTRELAMQITKECKKFTK 164
Cdd:cd17950    22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLS----TLQQ--LEPVDGQVsVLVICHTRELAFQISNEYERFSK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 165 AL-SLRVVCVYGGTGISEQIAELKRGA-EIIVCTPGRMIDMLAANSgrvTNLRRVTYLVLDEADRMF-DMGFEPQVMRIV 241
Cdd:cd17950    96 YMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKK---LKLSHVKHFVLDECDKMLeQLDMRRDVQEIF 172
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1715121658 242 DGTRPDRQTVLFSATFPRQMEALARRILTKPIEVQV 277
Cdd:cd17950   173 RATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
77-272 4.82e-34

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: 130.06  E-value: 4.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  77 VLDILKKQNYEKPTPIQAQAIPCIMSG---------KDLIGIAKTGSGKTLAFLLPMFRHILDQPALEAddgpLAIIMTP 147
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRL----RALIVVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 148 TRELAMQITKECKKFTKALSLRVVCVYGGTGISEQIAELKRG--------AEIIVCTPGRMIDMLAANSGrvTNLRRVTY 219
Cdd:cd17956    77 TKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPG--FTLKHLRF 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 220 LVLDEADRMFDMGFE---PQVMRIVDGTRPDR-----------------QTVLFSATFPRQMEALARRILTKP 272
Cdd:cd17956   155 LVIDEADRLLNQSFQdwlETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
620-698 3.39e-33

type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); The DDX46 family includes DEAD box protein 46 (DDX46), fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5, Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins. DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this family contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411815  Cd Length: 82  Bit Score: 122.39  E-value: 3.39e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1715121658 620 KYEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNELAVSKARAEFIRLI 698
Cdd:cd22387     4 NFVEEFEINDYPQIARLKVTSKEVLNSIMEETGATITIKGQYYPPGKKPKPGERKLYLLIEGATEESVQSARNEIKRVL 82
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
86-275 1.14e-32

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: 125.25  E-value: 1.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  86 YEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHIldQPALEAddgPLAIIMTPTRELAMQITKECKKFTKA 165
Cdd:cd18046    19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKA---TQALVLAPTRELAQQIQKVVMALGDY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 166 LSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYLVLDEADRMFDMGFEPQVMRIVDGTR 245
Cdd:cd18046    94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIK---MFVLDEADEMLSRGFKDQIYDIFQKLP 170
                         170       180       190
                  ....*....|....*....|....*....|
gi 1715121658 246 PDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd18046   171 PDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
85-275 1.22e-31

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: 122.19  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  85 NYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRhILDQPALEaddgPLAIIMTPTRELAMQITKECKKFTK 164
Cdd:cd18045    18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDIQVRE----TQALILSPTRELAVQIQKVLLALGD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 165 ALSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRrvtYLVLDEADRMFDMGFEPQVMRIVDGT 244
Cdd:cd18045    93 YMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIK---MLVLDEADEMLNKGFKEQIYDVYRYL 169
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1715121658 245 RPDRQTVLFSATFPRQMEALARRILTKPIEV 275
Cdd:cd18045   170 PPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
298-408 1.60e-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: 107.30  E-value: 1.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 298 GKFLKLLELLgYYQDQGSALVFVDKQENADL-LLkdLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARG 376
Cdd:pfam00271   1 EKLEALLELL-KKERGGKVLIFSQTKKTLEAeLL--LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1715121658 377 LDVKHLILVVNYDCPNHIEDYVHRCGRTGRAG 408
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
KH-I_PRP5_like cd22474
type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent ...
619-703 1.83e-23

type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5 and similar proteins; PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411902  Cd Length: 89  Bit Score: 94.70  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 619 RKYEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKE--GDRKLYLAIESTNELAVSKARAEFIR 696
Cdd:cd22474     3 TAYHAKVEINDLPQKARWEATNNTSLSKIIEETGCSITNKGNFYPPGKEPQPnnDEPKLYLLIEGTTEKAVRLAIELLRR 82

                  ....*..
gi 1715121658 697 LIKEELV 703
Cdd:cd22474    83 KLVEGVV 89
HELICc smart00490
helicase superfamily c-terminal domain;
327-408 2.93e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.82  E-value: 2.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  327 DLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGR 406
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1715121658  407 AG 408
Cdd:smart00490  81 AG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
73-267 6.06e-23

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: 98.60  E-value: 6.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  73 VSKKVLDILKKQNYE-----KPTPIQAQAIPcIMSGKDLIGI-----------------AKTGSGKTLAFLLPMFRHILD 130
Cdd:cd17965    10 VREAIIKEILKGSNKtdeeiKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 131 Q-----------PALEADDG-PLAIIMTPTRELAMQITKECKKFTKALSLRVVCVYGGTGIS-EQIAEL-KRGAEIIVCT 196
Cdd:cd17965    89 QeqepfeeaeeeYESAKDTGrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSyQRLQLAfKGRIDILVTT 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1715121658 197 PGRmIDMLAANSGRVtnLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARR 267
Cdd:cd17965   169 PGK-LASLAKSRPKI--LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK 236
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
65-272 8.99e-19

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: 85.84  E-value: 8.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  65 IKNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSG--KDLIGIAKTGSGKTLAFLLPMFRHIldqPALEAddGPLA 142
Cdd:cd18048    17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV---DALKL--YPQC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 143 IIMTPTRELAMQ---ITKECKKFTKALSLRVVCVYGGTGISEQIAelkrgAEIIVCTPGRMIDMlaANSGRVTNLRRVTY 219
Cdd:cd18048    92 LCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE-----AQIVIGTPGTVLDW--CFKLRLIDVTNISV 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 220 LVLDEADRMFDM-GFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKP 272
Cdd:cd18048   165 FVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
73-414 1.49e-18

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 89.57  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  73 VSKKVLDILKKQNYEKPTPIQAQAIP-CIMSGKDLIGIAKTGSGKTLAFLLPMFRHILdqpaleadDGPLAIIMTPTREL 151
Cdd:COG1204     7 PLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALL--------NGGKALYIVPLRAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AMQITKECKKFTKALSLRVVCVYGgtGISEQIAELKRgAEIIVCTPGRMIDMLAANSGrvtNLRRVTYLVLDEAdRMFDm 231
Cdd:COG1204    79 ASEKYREFKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPS---WLRDVDLVVVDEA-HLID- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 232 gfepqvmrivDGTR---------------PDRQTVLFSATFPrQMEALAR---RILTK----PIEVQVG---GRSVVCKD 286
Cdd:COG1204   151 ----------DESRgptlevllarlrrlnPEAQIVALSATIG-NAEEIAEwldAELVKsdwrPVPLNEGvlyDGVLRFDD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 287 VEQhvvviEEDGKFLKL-LELLgyyQDQGSALVFV-----------------------DKQENADLLLKDLIKAS----- 337
Cdd:COG1204   220 GSR-----RSKDPTLALaLDLL---EEGGQVLVFVssrrdaeslakkladelkrrltpEEREELEELAEELLEVSeetht 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 338 ----YNCMAL-----HGGIDQFDRDsTICD-FKAGKVSVLIATSVAARG--LDVKHLILVVNYDCPNH---IEDYVHRCG 402
Cdd:COG1204   292 neklADCLEKgvafhHAGLPSELRR-LVEDaFREGLIKVLVATPTLAAGvnLPARRVIIRDTKRGGMVpipVLEFKQMAG 370
                         410
                  ....*....|....
gi 1715121658 403 RTGRAG--NKGYAY 414
Cdd:COG1204   371 RAGRPGydPYGEAI 384
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
103-256 8.18e-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: 80.53  E-value: 8.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 103 GKDLIGIAKTGSGKTLAFLLPMFRHILDQpaleaddGPLAIIMTPTRELAMQITKECKKFTKaLSLRVVCVYGGTGISEQ 182
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEER 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1715121658 183 IAELKRGAEIIVCTPGRMIDMLAANSGRVtnLRRVTYLVLDEADRMFDMGFEPQVMRIVDGT--RPDRQTVLFSAT 256
Cdd:cd00046    73 EKNKLGDADIIIATPDMLLNLLLREDRLF--LKDLKLIIVDEAHALLIDSRGALILDLAVRKagLKNAQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
72-415 8.59e-18

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 87.97  E-value: 8.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  72 GVSKKVLDILKKQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDqpaleaDDGPLAIIMTPTREL 151
Cdd:COG1205    40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DPGATALYLYPTKAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 152 AM-QItKECKKFTKALSLRV-VCVY-GGTGISEQiAELKRGAEIIVCTPgrmiDM-----LAANSGRVTNLRRVTYLVLD 223
Cdd:COG1205   114 ARdQL-RRLRELAEALGLGVrVATYdGDTPPEER-RWIREHPDIVLTNP----DMlhyglLPHHTRWARFFRNLRYVVID 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 224 EA---------------DRMfdmgfepqvMRIVD--GTRPdrQTVLFSATF--PrqmEALARRiLTkpievqvgGRSVVC 284
Cdd:COG1205   188 EAhtyrgvfgshvanvlRRL---------RRICRhyGSDP--QFILASATIgnP---AEHAER-LT--------GRPVTV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 285 KDV------EQHVVVIE----EDGKFLKLL----ELLGYYQDQG-SALVFVDKQENADLLLKDLIK-----------ASY 338
Cdd:COG1205   245 VDEdgsprgERTFVLWNpplvDDGIRRSALaeaaRLLADLVREGlRTLVFTRSRRGAELLARYARRalrepdladrvAAY 324
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1715121658 339 ncmalHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYT 415
Cdd:COG1205   325 -----RAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
90-268 1.37e-16

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: 78.07  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  90 TPIQAQAIPCIM-SGKDLIGIAKTGSGKTLAFLLPMFRHILDQpaleaddGPLAIIMTPTRELAMQITKECKKFTKALSL 168
Cdd:cd17921     3 NPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 169 RVVCVYGGTGISeqiAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTR--- 245
Cdd:cd17921    76 NVGLLTGDPSVN---KLLLAEADILVATPEKLDLLL--RNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrin 150
                         170       180
                  ....*....|....*....|...
gi 1715121658 246 PDRQTVLFSATFPrQMEALARRI 268
Cdd:cd17921   151 KNARFVGLSATLP-NAEDLAEWL 172
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
109-382 4.68e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 81.99  E-value: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 109 IAKTGSGKTLAFLLPMFRHILDQPALeaddgplaiIMTPTRELAMQITKECKKFtkalsLRVVCVYGGtgiseqiaELKR 188
Cdd:COG1061   106 VAPTGTGKTVLALALAAELLRGKRVL---------VLVPRRELLEQWAEELRRF-----LGDPLAGGG--------KKDS 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 189 GAEIIVCTpgrmIDMLAANSGRVTNLRRVTYLVLDEADRMFDMGFEpQVMRIVD--------GT--RPDRQTVLFSA--- 255
Cdd:COG1061   164 DAPITVAT----YQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYR-RILEAFPaayrlgltATpfRSDGREILLFLfdg 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 256 ---TFPRQmEALARRILTKP--IEVQVGGRS-----VVCKDVEQHVVVIEEDGKFLKLLELLGYYQDQGSALVFVDKQEN 325
Cdd:COG1061   239 ivyEYSLK-EAIEDGYLAPPeyYGIRVDLTDeraeyDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVDH 317
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1715121658 326 ADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHL 382
Cdd:COG1061   318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
93-268 1.43e-15

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: 75.31  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  93 QAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPaleaddGPLAIIMTPTRELAMQITKECKKFTKALSLRVVC 172
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 173 -VYGG-TGISEQIAELKRGAEIIVCTPgrmiDMLAA-----NSGRVTNLRRVTYLVLDEAdRMFDMGFEPQV-------M 238
Cdd:cd17923    79 aTYDGdTPREERRAIIRNPPRILLTNP----DMLHYallphHDRWARFLRNLRYVVLDEA-HTYRGVFGSHValllrrlR 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 1715121658 239 RIVDGTRPDRQTVLFSATFpRQMEALARRI 268
Cdd:cd17923   154 RLCRRYGADPQFILTSATI-GNPAEHARTL 182
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
66-272 8.35e-15

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: 73.60  E-value: 8.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  66 KNWAQCGVSKKVLDILKKQNYEKPTPIQAQAIPCIMSG--KDLIGIAKTGSGKTLAFLLPMFRHIldQPALEADDgplAI 143
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQ---CL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 144 IMTPTRELAMQITKECKKFTKALSlRVVCVYGGTGiseqiAELKRGA----EIIVCTPGRMIDMLAanSGRVTNLRRVTY 219
Cdd:cd18047    76 CLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRG-----NKLERGQkiseQIVIGTPGTVLDWCS--KLKFIDPKKIKV 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 220 LVLDEADRMF-DMGFEPQVMRIVDGTRPDRQTVLFSATFPRQMEALARRILTKP 272
Cdd:cd18047   148 FVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
299-413 1.05e-12

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: 66.08  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 299 KFLKLLELL-GYYQDQGS--ALVFVdKQENADLLLKDLIK------ASYNCMAL--HGGIDQFDRD--------STICDF 359
Cdd:cd18802     8 KLQKLIEILrEYFPKTPDfrGIIFV-ERRATAVVLSRLLKehpstlAFIRCGFLigRGNSSQRKRSlmtqrkqkETLDKF 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 360 KAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRtGRAGNKGYA 413
Cdd:cd18802    87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYI 139
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
621-700 1.25e-11

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411813  Cd Length: 84  Bit Score: 61.07  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 621 YEEELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPG--KEPKEGDRKLYLAIESTNELAVSKAraefIRLI 698
Cdd:cd22385     5 YVAEIEINDLPNTCRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEekATFNPGERPLYLHVQAPTKEAVDRA----VNKI 80

                  ..
gi 1715121658 699 KE 700
Cdd:cd22385    81 NE 82
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
293-416 5.30e-10

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: 57.99  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 293 VIEEDGKFLKLLELLGY--YQDQGSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIAT 370
Cdd:cd18794     8 VRPKDKKDEKLDLLKRIkvEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1715121658 371 SVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTF 416
Cdd:cd18794    88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
299-410 1.27e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 61.67  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 299 KFLKLLELLGYY---QDQGSALVFVDKQENADLLLKDLIKASYNCMALHG--------GIDQFDRDSTICDFKAGKVSVL 367
Cdd:COG1111   336 KLSKLREILKEQlgtNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVL 415
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1715121658 368 IATSVAARGLDVKHLILVVNYD-CPNHIEdYVHRCGRTGRAGNK 410
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKREG 458
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
365-418 2.22e-09

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: 54.25  E-value: 2.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 365 SVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFVT 418
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
KH-I_RIK_like_rpt1 cd22471
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
624-698 8.89e-09

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and similar proteins; RIK, also called rough sheath 2-interacting KH domain protein, or RS2-interacting KH domain protein, is a RNA binding protein that acts together with RS2/AS1 in the recruitment of HIRA. RIK contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411899  Cd Length: 91  Bit Score: 53.24  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 624 ELEINDFPQQARWKVTSKEALAQISEYSEAGITVRGTYYPPGKEPKEGDRKLYLAIESTNEL---------AVSKARAEF 694
Cdd:cd22471     8 EIVINDAPPSVRHHLTKRSTQDEIQSKTGVVVVTRGRYYPPGTPPPDNEKPLYLHITAGAQLppddaerqkAVDAAAADI 87

                  ....
gi 1715121658 695 IRLI 698
Cdd:cd22471    88 QAML 91
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
78-276 5.80e-08

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 53.69  E-value: 5.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  78 LDILKKQ-NYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLpmfrhildqPALEADdgPLAIIMTPTRELaM--Q 154
Cdd:cd17920     1 EQILKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQL---------PALLLD--GVTLVVSPLISL-MqdQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 155 ITKeckkfTKALSLRVVCVYGGTGISEQ---IAELKRG-AEIIVCTP-----GRMIDMLAansgRVTNLRRVTYLVLDEA 225
Cdd:cd17920    69 VDR-----LQQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPerllsPDFLELLQ----RLPERKRLALIVVDEA 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 226 --------DrmfdmgFEPQVMRIVDGTR--PDRQTVLFSATFPRQMEALARRIL--TKPIEVQ 276
Cdd:cd17920   140 hcvsqwghD------FRPDYLRLGRLRRalPGVPILALTATATPEVREDILKRLglRNPVIFR 196
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
88-227 7.24e-08

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: 53.21  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  88 KPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEaddGPLAIIMTPTRELAMQITKECKKFTKALS 167
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGR---KGKVVFLANKVPLVEQQKEVFRKHFERPG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 168 LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYLVLDEADR 227
Cdd:cd17927    79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDL--KSGTIVSLSDFSLLVFDECHN 136
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
103-224 7.40e-08

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: 52.59  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 103 GKDLIGIAKTGSGKTLAFLLPMFRHILDQPAleadDGPLAIIMTPTRELAMQITKECKKFTKALSL--RVVCVYGGTGIS 180
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE----KGVQVLYISPLKALINDQERRLEEPLDEIDLeiPVAVRHGDTSQS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1715121658 181 EQIAELKRGAEIIVCTPGRMIDMLAANSGRVTnLRRVTYLVLDE 224
Cdd:cd17922    77 EKAKQLKNPPGILITTPESLELLLVNKKLREL-FAGLRYVVVDE 119
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
112-225 3.91e-07

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: 51.11  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 112 TGSGKTL-AFLLpmFRHILDQPALEADDGPLAIIMTPTRELAMQITKECKKFTKalsLRVVCVYGGTGISEQIA----EL 186
Cdd:cd18034    25 TGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTD---LKVGEYSGEMGVDKWTKerwkEE 99
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1715121658 187 KRGAEIIVCTPGRMIDMLaaNSGRVTnLRRVTYLVLDEA 225
Cdd:cd18034   100 LEKYDVLVMTAQILLDAL--RHGFLS-LSDINLLIFDEC 135
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
82-450 8.46e-07

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 52.39  E-value: 8.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  82 KKQNYEKPTPIQAQAIPCIMSGKDLIG-----IAKTGSGKTLAFLLPMFRHildqpaLEADDGPLAIIMTPTRELAMQIT 156
Cdd:COG1203   121 KSKPRTPINPLQNEALELALEAAEEEPglfilTAPTGGGKTEAALLFALRL------AAKHGGRRIIYALPFTSIINQTY 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 157 KECKKFtkaLSLRVVCVYGGTGISEQIAE------------LKRG--AEIIVCTPGRMIDMLAANSG----RVTNLRRvT 218
Cdd:COG1203   195 DRLRDL---FGEDVLLHHSLADLDLLEEEeeyesearwlklLKELwdAPVVVTTIDQLFESLFSNRKgqerRLHNLAN-S 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 219 YLVLDEADrMFDMGFEPQVMRIVD-----GTRpdrqTVLFSATFPrqmeALARRILTKPIEV---QVGGRSVVCKDVEQH 290
Cdd:COG1203   271 VIILDEVQ-AYPPYMLALLLRLLEwlknlGGS----VILMTATLP----PLLREELLEAYELipdEPEELPEYFRAFVRK 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 291 VVVIEEDGKFLKLL--ELLGYYQDQGSALVFV----DKQENADLLLKDLIKasYNCMALHGGIDQFDR---DSTICD-FK 360
Cdd:COG1203   342 RVELKEGPLSDEELaeLILEALHKGKSVLVIVntvkDAQELYEALKEKLPD--EEVYLLHSRFCPADRseiEKEIKErLE 419
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 361 AGKVSVLIATSVAARGLDVkhlilvvnyDCpnhieDYVH--------------RCGRTGRAGNKG--YAYTFVTQEQGRY 424
Cdd:COG1203   420 RGKPCILVSTQVVEAGVDI---------DF-----DVVIrdlapldsliqragRCNRHGRKEEEGnvYVFDPEDEGGGYV 485
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1715121658 425 AGDII-----KALEQGSNPVPEDLQKLWDEY 450
Cdd:COG1203   486 YDKPLlertrELLREHDEILPEDKRELIEEY 516
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
83-142 1.13e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 52.03  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1715121658  83 KQNYEKPTPIQAQAIPCIMSGKD-LIgIAKTGSGKTLAFLLPmfrhILDQPALEADDGPLA 142
Cdd:COG1201    19 AARFGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLP----ALDELARRPRPGELP 74
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
346-414 1.61e-06

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: 48.12  E-value: 1.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 346 GIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDC-PNHIEdYVHRCGRTGRaGNKGYAY 414
Cdd:cd18801    73 GMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDAsPSPIR-MIQRMGRTGR-KRQGRVV 140
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
88-224 3.49e-06

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: 48.24  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  88 KPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPalEADDGPLAIIMTPTRELA-MQITKECKKFTKAl 166
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRR--SAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKG- 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1715121658 167 sLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRV---TYLVLDE 224
Cdd:cd18036    79 -YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNL--LSGREEERVYLsdfSLLIFDE 136
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
92-224 4.03e-06

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: 48.12  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  92 IQAQAIP-CIMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPALEADDgPLAIIMTPTRELAMQITKECKKFTKALSLRV 170
Cdd:cd18023     5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKEKFGPLGLSC 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1715121658 171 VCVYGGTGI--SEQIaelkRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYLVLDE 224
Cdd:cd18023    84 AELTGDTEMddTFEI----QDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDE 135
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
91-274 4.44e-06

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: 47.71  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  91 PIQAQAIPC-IMSGKDLIGIAKTGSGKTLAFLLPMFRHILdqpaleadDGPLAIIMTPTRELAMQITKECKKFTKaLSLR 169
Cdd:cd18028     4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALASEKYEEFKKLEE-IGLK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 170 VVCvygGTGISEQIAELKRGAEIIVCTPGRmIDMLAANsgRVTNLRRVTYLVLDEADRMFDMGFEPQVMRIVDGTR---P 246
Cdd:cd18028    75 VGI---STGDYDEDDEWLGDYDIIVATYEK-FDSLLRH--SPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnP 148
                         170       180
                  ....*....|....*....|....*...
gi 1715121658 247 DRQTVLFSATFPrQMEALARRILTKPIE 274
Cdd:cd18028   149 NTQIIGLSATIG-NPDELAEWLNAELVE 175
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
295-419 1.90e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 47.91  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 295 EEDGKFLKLLELLGYYQDQG-SALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAG---KVsVLIAT 370
Cdd:COG0553   530 GRSAKLEALLELLEELLAEGeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeaPV-FLISL 608
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 371 SVAARGLDvkhliL-----VVNYDC---PNHIE---DYVHRCGRTgragNKGYAYTFVTQ 419
Cdd:COG0553   609 KAGGEGLN-----LtaadhVIHYDLwwnPAVEEqaiDRAHRIGQT----RDVQVYKLVAE 659
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
105-456 4.92e-05

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 46.27  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 105 DLIGIAKTGSGKTLAFLLPMFRHILDQpalEADDGplaIIMTPTRELAmqitkeckkftKALSLRVVCVYGGTGISEQIA 184
Cdd:cd09639     1 LLVIEAPTGYGKTEAALLWALHSLKSQ---KADRV---IIALPTRATI-----------NAMYRRAKEAFGETGLYHSSI 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 185 ELKRGAEII-------------------------VCTPGR-MIDMLAANSGRVTNLRRVTY--LVLDEADRM--FDMGFE 234
Cdd:cd09639    64 LSSRIKEMGdseefehlfplyihsndtlfldpitVCTIDQvLKSVFGEFGHYEFTLASIANslLIFDEVHFYdeYTLALI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 235 PQVMRIVdgTRPDRQTVLFSATFPRQMEALARRILTkPIEVQvggrSVVCKDVEQHVVVIEED---GKFLKLLELLGYYQ 311
Cdd:cd09639   144 LAVLEVL--KDNDVPILLMSATLPKFLKEYAEKIGY-VEENE----PLDLKPNERAPFIKIESdkvGEISSLERLLEFIK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 312 DQGSALVFVDKQENAD---LLLKDLIKaSYNCMALHGGIDQFDR----DSTICDFKAGKVSVLIATSVAARGLDVKHLIL 384
Cdd:cd09639   217 KGGSVAIIVNTVDRAQefyQQLKEKGP-EEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDISVDVM 295
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 385 VVNYdCPnhIEDYVHRCGRTGRAGNKgyaytfvtqeqgrYAGD--IIKALEQGSNPVPEDLQKLWDEYKLKQEM 456
Cdd:cd09639   296 ITEL-AP--IDSLIQRLGRLHRYGEK-------------NGEEvyIITDAPDGKGQKPYPYDLVERTIELLEEG 353
PRK00254 PRK00254
ski2-like helicase; Provisional
73-224 5.49e-05

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 46.73  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  73 VSKKVLDILKKQNYEKPTPIQAQAIPC-IMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQpaleaddGPLAIIMTPTREL 151
Cdd:PRK00254    8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLRE-------GGKAVYLVPLKAL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 152 AMQITKECKKFTKaLSLRVVCVyggTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVtnlRRVTYLVLDE 224
Cdd:PRK00254   81 AEEKYREFKDWEK-LGLRVAMT---TGDYDSTDEWLGKYDIIIATAEKFDSLLRHGSSWI---KDVKLVVADE 146
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
74-123 5.61e-05

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 45.05  E-value: 5.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1715121658  74 SKKVLDILKKQ-NYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLP 123
Cdd:cd18015     3 SGKVKDTLKNVfKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
78-458 5.91e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 46.29  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  78 LDILKKQ-NYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPmfrhildqpALeADDGpLAIIMTP--------T 148
Cdd:COG0514     6 LEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLP---------AL-LLPG-LTLVVSPlialmkdqV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 149 RELamqitkeckkftKALSLRVVCVYGGTGISEQ---IAELKRGA-EIIVCTP-----GRMIDMLAAnsgrvtnlRRVTY 219
Cdd:COG0514    75 DAL------------RAAGIRAAFLNSSLSAEERrevLRALRAGElKLLYVAPerllnPRFLELLRR--------LKISL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 220 LVLDEA--------DrmfdmgFEPQVMRIVDGTR--PDRQTVLFSATF-PRQMEALARRI-LTKPiEVQVGG-------- 279
Cdd:COG0514   135 FAIDEAhcisqwghD------FRPDYRRLGELRErlPNVPVLALTATAtPRVRADIAEQLgLEDP-RVFVGSfdrpnlrl 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 280 RsvvckdveqhVVVIEEDGKFLKLLELLGYYQDqGSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDF 359
Cdd:COG0514   208 E----------VVPKPPDDKLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRF 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 360 KAGKVSVLIATSvaARGL-----DVKhliLVVNYDCPNHIEDYVHRCGRTGRAGNKGYAYTFVTQEqgryagDIIKA--- 431
Cdd:COG0514   277 LRDEVDVIVATI--AFGMgidkpDVR---FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE------DVAIQrff 345
                         410       420
                  ....*....|....*....|....*..
gi 1715121658 432 LEQGSnpvPEDLQKLWDEYKLkQEMEG 458
Cdd:COG0514   346 IEQSP---PDEERKRVERAKL-DAMLA 368
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
297-402 6.08e-05

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: 43.23  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 297 DGKFLKLLELLGYYQDQGS-ALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVS--VLIATSVA 373
Cdd:cd18793    10 SGKLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAG 89
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1715121658 374 ARGLDvkhLI---LVVNYDC---PNHIE---DYVHRCG 402
Cdd:cd18793    90 GVGLN---LTaanRVILYDPwwnPAVEEqaiDRAHRIG 124
PRK13766 PRK13766
Hef nuclease; Provisional
299-419 7.05e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 46.41  E-value: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 299 KFLKLLEL----LGYYQDQgSALVFVDKQENADLLLKDLIKASYNCMALHGgidQFDRDS-----------TICDFKAGK 363
Cdd:PRK13766  348 KLEKLREIvkeqLGKNPDS-RIIVFTQYRDTAEKIVDLLEKEGIKAVRFVG---QASKDGdkgmsqkeqieILDKFRAGE 423
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1715121658 364 VSVLIATSVAARGLDVKHLILVVNYD-CPNHIEdYVHRCGRTGRaGNKGYAYTFVTQ 419
Cdd:PRK13766  424 FNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAK 478
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
88-265 7.73e-05

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 43.94  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  88 KPTPIQAQAIPCIMSG------KDLIGIAKTGSGKTLAFLLPMFrhildqpaLEADDGPLAIIMTPTRELAMQITKECKK 161
Cdd:cd17918    15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAAL--------LAYKNGKQVAILVPTEILAHQHYEEARK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 162 FTKalSLRVVCVYGGTgiSEQIAElkrGAEIIVCTPGrmidMLAANSgrvtNLRRVTYLVLDEADRmfdMGFEpQVMRIV 241
Cdd:cd17918    87 FLP--FINVELVTGGT--KAQILS---GISLLVGTHA----LLHLDV----KFKNLDLVIVDEQHR---FGVA-QREALY 147
                         170       180
                  ....*....|....*....|....*
gi 1715121658 242 DGTRPDrqTVLFSAT-FPRQMeALA 265
Cdd:cd17918   148 NLGATH--FLEATATpIPRTL-ALA 169
PRK13767 PRK13767
ATP-dependent helicase; Provisional
74-224 9.18e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 46.03  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  74 SKKVLDILK-------KQNYEKPTPIQAQAIPCIMSGKDLIGIAKTGSGKTLAfllpMFRHILDQPALEADDGPL----- 141
Cdd:PRK13767   11 DEEILDLLRpyvrewfKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLA----AFLAIIDELFRLGREGELedkvy 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 142 AIIMTPTRELA-----------MQITKECKKFTKALS-LRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSG 209
Cdd:PRK13767   87 CLYVSPLRALNndihrnleeplTEIREIAKERGEELPeIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNSPKF 166
                         170
                  ....*....|....*
gi 1715121658 210 RvTNLRRVTYLVLDE 224
Cdd:PRK13767  167 R-EKLRTVKWVIVDE 180
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
288-418 9.84e-05

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 43.31  E-value: 9.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 288 EQHVVVIEEDGKFLKLLELLGYYQDQ------------GSALVFVDKQENADLLLKDLIKASYncmaLHGGIDQFDRDsT 355
Cdd:cd18795     6 EEYVLGFNGLGIKLRVDVMNKFDSDIivllkietvsegKPVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRE-L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 356 ICD-FKAGKVSVLIATSVAARGldvkhlilvVN-------------YDCPNHIE----DYVHRCGRTGRAG--NKGYAYT 415
Cdd:cd18795    81 VEElFREGLIKVLVATSTLAAG---------VNlpartviikgtqrYDGKGYRElsplEYLQMIGRAGRPGfdTRGEAII 151

                  ...
gi 1715121658 416 FVT 418
Cdd:cd18795   152 MTK 154
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
317-413 1.22e-04

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 42.63  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 317 LVFVDKQENADLLLKDL-------IKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYD 389
Cdd:cd18797    39 IVFCRSRKLAELLLRYLkarlveeGPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
                          90       100
                  ....*....|....*....|....
gi 1715121658 390 CPNHIEDYVHRCGRTGRAGNKGYA 413
Cdd:cd18797   119 YPGSLASLWQQAGRAGRRGKDSLV 142
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
330-434 1.24e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 330 LKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNYDCPNHIEDYVHRC-GRTGRAG 408
Cdd:cd18811    54 LKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGD 133
                          90       100
                  ....*....|....*....|....*.
gi 1715121658 409 NKGYAYTFVTQEQGRYAGDIIKALEQ 434
Cdd:cd18811   134 HQSYCLLVYKDPLTETAKQRLRVMTE 159
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
91-224 1.90e-04

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 43.13  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  91 PIQAQAIPCIMSGKD--LIGiAKTGSGKTLAFLLPMFRHILDQPaleaddGPLAIIMTPTRELAMQITKECKK-FTKALS 167
Cdd:cd18022     4 PIQTQVFHTLYHTDNnvLLG-APTGSGKTIAAELAMFRAFNKYP------GSKVVYIAPLKALVRERVDDWKKrFEEKLG 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1715121658 168 LRVVCVYGGTgiSEQIAELkRGAEIIVCTPGRMiDMLAANSGRVTNLRRVTYLVLDE 224
Cdd:cd18022    77 KKVVELTGDV--TPDMKAL-ADADIIITTPEKW-DGISRSWQTREYVQQVSLIIIDE 129
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
85-224 4.05e-04

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 42.36  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  85 NYEKPTPIQAQAIPCIMSGKD-LIGIAKTGSGKTLAFLLPMFR----HILDQPALEADDGPLAIImTPTRELAMQITKEC 159
Cdd:cd18019    14 GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILReigkHRNPDGTINLDAFKIVYI-APMKALVQEMVGNF 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1715121658 160 KKFTKALSLRVVCVYGGTGIS-EQIAElkrgAEIIVCTPGRMiDMLAANSGRVTNLRRVTYLVLDE 224
Cdd:cd18019    93 SKRLAPYGITVAELTGDQQLTkEQISE----TQIIVTTPEKW-DIITRKSGDRTYTQLVRLIIIDE 153
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
315-409 7.83e-04

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: 40.33  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 315 SALVFVDKQENADLL---LKDLIKASY---NCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARGLDVKHLILVVNY 388
Cdd:cd18796    40 STLVFTNTRSQAERLaqrLRELCPDRVppdFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI 119
                          90       100
                  ....*....|....*....|.
gi 1715121658 389 DCPNHIEDYVHRCGRTGRAGN 409
Cdd:cd18796   120 GSPKSVARLLQRLGRSGHRPG 140
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
91-242 1.49e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 40.32  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  91 PIQAQAIPCIMSGKDLIGIAKTGSGKTLAFLLPMFrhildqpaLEADDGP-LAIIMTPTRELaM--QItkeckkftKAL- 166
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--------LLRRRGPgLTLVVSPLIAL-MkdQV--------DALp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 167 -SLRVVCVYGGTGISEQIAELK--RGAE--IIVCTPGRmidmLAANSGR--VTNLRRVTYLVLDEADRMFDMG--FEPQV 237
Cdd:cd18018    78 rAIKAAALNSSLTREERRRILEklRAGEvkILYVSPER----LVNESFRelLRQTPPISLLVVDEAHCISEWShnFRPDY 153

                  ....*
gi 1715121658 238 MRIVD 242
Cdd:cd18018   154 LRLCR 158
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
91-225 1.70e-03

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 40.32  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  91 PIQAQAIPCIMSGKD--LIGiAKTGSGKTLAFLLPMFRHILDQPaleaddGPLAIIMTPTRELAMQITKE-CKKFTKALS 167
Cdd:cd18021     6 PIQTQVFNSLYNTDDnvFVG-APTGSGKTVCAELALLRHWRQNP------KGRAVYIAPMQELVDARYKDwRAKFGPLLG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 168 LRVVCVYGgtgisEQIAELK--RGAEIIVCTPGRMiDMLAANSGRVTNLRRVTYLVLDEA 225
Cdd:cd18021    79 KKVVKLTG-----ETSTDLKllAKSDVILATPEQW-DVLSRRWKQRKNVQSVELFIADEL 132
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
298-418 2.25e-03

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 39.60  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 298 GKFLKLLELLGyyqDQGsaLVFVDK---QENADLLLKDLIKASYNC-MALHGGIDQFDrdsticDFKAGKVSVLIATS-- 371
Cdd:cd18798    14 EKLLELVKKLG---DGG--LIFVSIdygKEYAEELKEFLERHGIKAeLALSSTEKNLE------KFEEGEIDVLIGVAsy 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 372 --VAARGLDVKHLI-LVVNYDCPnhIEDYVHRCGRTGR--AGN--KGYAYTFVT 418
Cdd:cd18798    83 ygVLVRGIDLPERIkYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVD 134
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
81-224 4.00e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 39.03  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658  81 LKKQNYEKPTPIQAqaipciMSGKDLIGIAKTGSGKTLAFLLPMFRHILDQPalEADDGPLAIIMTPTRELAMQITKECK 160
Cdd:cd18073     1 FKPRNYQLELALPA------MKGKNTIICAPTGCGKTFVSLLICEHHLKKFP--QGQKGKVVFFATKVPVYEQQKSVFSK 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1715121658 161 KFTKaLSLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLaaNSGRVTNLRRVTYLVLDE 224
Cdd:cd18073    73 YFER-HGYRVTGISGATAENVPVEQIIENNDIIILTPQILVNNL--KKGTIPSLSIFTLMIFDE 133
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
299-408 4.07e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.47  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1715121658 299 KFLKLLELLGYYQDQ--GSALVFVDKQENADLLLKDLIKASYNCMALHGGIDQFDRDSTICDFKAGKVSVLIATSVAARG 376
Cdd:PRK11057  220 KFKPLDQLMRYVQEQrgKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1715121658 377 LDVKHLILVVNYDCPNHIEDYVHRCGRTGRAG 408
Cdd:PRK11057  300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
545-598 7.56e-03

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 37.69  E-value: 7.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1715121658 545 ELAKKLASRIS---------LQRnigaeAQQTAEAVLKGHLGTPVISAKTLAEQRAEKLHAKL 598
Cdd:cd07067    36 ALGKRLKELGIkfdriysspLKR-----AIQTAEIILEELPGLPVEVDPRLREARVLPALEEL 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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