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Conserved domains on  [gi|1371977166|ref|NP_001348572|]
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ATP-dependent RNA helicase DDX42 isoform d [Mus musculus]

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];
4-414 1.73e-155

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 454.99  E-value: 1.73e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVCPTRELCQQIHAECK 83
Cdd:COG0513    17 LAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTRELALQVAEELR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:COG0513    93 KLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRRLVEFTSSGSVLLFV 241
Cdd:COG0513   173 LPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRRLLRDEDPERAIVFC 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 242 TKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHR 321
Cdd:COG0513   249 NTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 322 IGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERP 400
Cdd:COG0513   329 IGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGP 404

                         410
                  ....*....|....
gi 1371977166 401 GlGSENSDRGNNNN 414
Cdd:COG0513   405 K-GERKARRGKRRR 417
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 380-625 1.66e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21118:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 380 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSnyeAYKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 459
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGC---TNPPPSGSHE---------------------SFSNSGGS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 460 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 539
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 540 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 619
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358


                  ....*.
gi 1371977166 620 GFNREN 625
Cdd:cd21118   359 PFNFDT 364
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
4-414 1.73e-155

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 454.99  E-value: 1.73e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVCPTRELCQQIHAECK 83
Cdd:COG0513    17 LAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTRELALQVAEELR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:COG0513    93 KLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRRLVEFTSSGSVLLFV 241
Cdd:COG0513   173 LPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRRLLRDEDPERAIVFC 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 242 TKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHR 321
Cdd:COG0513   249 NTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 322 IGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERP 400
Cdd:COG0513   329 IGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGP 404

                         410
                  ....*....|....
gi 1371977166 401 GlGSENSDRGNNNN 414
Cdd:COG0513   405 K-GERKARRGKRRR 417
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 1-196 1.49e-142

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: 413.35  E-value: 1.49e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17952     2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17952    82 EAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSI 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17952   162 VGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
PTZ00110 PTZ00110
helicase; Provisional
 4-388 1.79e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 395.30  E-value: 1.79e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:PTZ00110  145 LKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCN 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:PTZ00110  225 KFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLL 239
Cdd:PTZ00110  305 IRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILI 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 240 FVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHT 319
Cdd:PTZ00110  383 FVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYV 462

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371977166 320 HRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 388
Cdd:PTZ00110  463 HRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 13-184 1.53e-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: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  13 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 92
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  93 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 172
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153

                         170
                  ....*....|..
gi 1371977166 173 FSATFRKKIEKL 184
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
4-210 1.04e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 1.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166    4 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 82
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   83 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 161
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1371977166  162 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 210
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 33-331 5.75e-11

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 64.78  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  33 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 111
Cdd:TIGR01587   6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 112 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 163
Cdd:TIGR01587  76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 243
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 244 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 316
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308

                         330
                  ....*....|....*
gi 1371977166 317 THTHRIGRTGRAGEK 331
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 380-625 1.66e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 380 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSnyeAYKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 459
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGC---TNPPPSGSHE---------------------SFSNSGGS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 460 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 539
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 540 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 619
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358


                  ....*.
gi 1371977166 620 GFNREN 625
Cdd:cd21118   359 PFNFDT 364
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
4-414 1.73e-155

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 454.99  E-value: 1.73e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVCPTRELCQQIHAECK 83
Cdd:COG0513    17 LAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAPTRELALQVAEELR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:COG0513    93 KLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRRLVEFTSSGSVLLFV 241
Cdd:COG0513   173 LPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRRLLRDEDPERAIVFC 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 242 TKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHR 321
Cdd:COG0513   249 NTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 322 IGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKKLNIGGGGLGYRERP 400
Cdd:COG0513   329 IGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGP 404

                         410
                  ....*....|....
gi 1371977166 401 GlGSENSDRGNNNN 414
Cdd:COG0513   405 K-GERKARRGKRRR 417
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 1-196 1.49e-142

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: 413.35  E-value: 1.49e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17952     2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17952    82 EAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSI 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17952   162 VGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
PTZ00110 PTZ00110
helicase; Provisional
 4-388 1.79e-130

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 395.30  E-value: 1.79e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:PTZ00110  145 LKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCN 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:PTZ00110  225 KFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQ 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLL 239
Cdd:PTZ00110  305 IRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILI 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 240 FVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHT 319
Cdd:PTZ00110  383 FVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYV 462

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371977166 320 HRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 388
Cdd:PTZ00110  463 HRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 9-349 3.87e-107

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 332.15  E-value: 3.87e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKELepgdGPIAVIVCPTRELCQQIHAECKRFGKA 88
Cdd:PRK11776   24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAKEIRRLARF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 -YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 167
Cdd:PRK11776   99 iPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDPIRVvqgdIGEANEDVTQI----VEILHSGpsKWNWLTRRLVEFTSSgSVLLFVTK 243
Cdd:PRK11776  179 RQTLLFSATYPEGIAAISQRFQRDPVEV----KVESTHDLPAIeqrfYEVSPDE--RLPALQRLLLHHQPE-SCVVFCNT 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 244 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 323
Cdd:PRK11776  252 KKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIG 331

                         330       340
                  ....*....|....*....|....*.
gi 1371977166 324 RTGRAGEKGVAYTLLTPKDSNFAGDL 349
Cdd:PRK11776  332 RTGRAGSKGLALSLVAPEEMQRANAI 357
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 4-195 3.38e-98

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: 300.45  E-value: 3.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17953    27 IKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIGLIMAPTRELALQIYVECK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV---KKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17953   107 KFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKI 186

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17953   187 VNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 1-196 1.42e-97

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: 297.74  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17966     2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17966    82 EANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKI 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17966   162 VDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 4-195 2.99e-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: 297.05  E-value: 2.99e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd00268     5 LKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIAEVAR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:cd00268    84 KLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSA 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd00268   164 LPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 4-337 6.12e-91

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 289.15  E-value: 6.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK 83
Cdd:PRK11192   16 LQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTPTRELAMQVADQAR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:PRK11192   95 ELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 VRPDRQTLLFSATFR-KKIEKLARDILIDPIRVvqgdigEAN------EDVTQIVEILHSGPSKWNWLTRRLVEFTSSGS 236
Cdd:PRK11192  175 TRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKTALLCHLLKQPEVTRS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 237 VLlFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDID 316
Cdd:PRK11192  249 IV-FVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSAD 327

                         330       340
                  ....*....|....*....|.
gi 1371977166 317 THTHRIGRTGRAGEKGVAYTL 337
Cdd:PRK11192  328 TYLHRIGRTGRAGRKGTAISL 348
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 9-414 7.14e-80

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 260.90  E-value: 7.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPI-AVIVCPTRELCQQIHAECKRFGK 87
Cdd:PRK10590   21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQIGENVRDYSK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  88 AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 167
Cdd:PRK10590  101 YLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKLPAK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIV---------EILHSGPSKWNWltrrlveftssGSVL 238
Cdd:PRK10590  181 RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVhfvdkkrkrELLSQMIGKGNW-----------QQVL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 239 LFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTH 318
Cdd:PRK10590  250 VFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDY 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 319 THRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEganqhvsKELLDLAM--------------QNAwfRKSRFKGGKG 384
Cdd:PRK10590  330 VHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK-------KEIPRIAIpgyepdpsikaepiQNG--RQQRGGGGRG 400

                         410       420       430
                  ....*....|....*....|....*....|
gi 1371977166 385 KKLNIGGGGLGYRERPGLGSENSDRGNNNN 414
Cdd:PRK10590  401 QGGGRGQQQGQPRRGEGGAKSASAKPAEKP 430
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 1-201 1.89e-77

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: 246.24  E-value: 1.89e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDG-----PIAVIVCPTRELC 75
Cdd:cd17967    12 LENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPSALILAPTRELA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  76 QQIHAECKRFgkAYN--LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 153
Cdd:cd17967    92 IQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGF 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371977166 154 EYQVRSIASH----VRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 201
Cdd:cd17967   170 EPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 1-343 3.95e-75

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 249.06  E-value: 3.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAF---IWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQ 77
Cdd:PRK01297   99 MHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMGE-PRALIIAPTRELVVQ 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  78 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 156
Cdd:PRK01297  178 IAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQ 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 157 VRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILhSGPSKWNwLTRRLVEFTSS 234
Cdd:PRK01297  258 VRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AGSDKYK-LLYNLVTQNPW 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 235 GSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARD 314
Cdd:PRK01297  336 ERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPED 415

                         330       340
                  ....*....|....*....|....*....
gi 1371977166 315 IDTHTHRIGRTGRAGEKGVAYTLLTPKDS 343
Cdd:PRK01297  416 PDDYVHRIGRTGRAGASGVSISFAGEDDA 444
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 1-195 7.72e-74

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: 237.60  E-value: 7.72e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd18049    36 MDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQ 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd18049   116 VAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKI 195

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd18049   196 VDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 13-337 2.89e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 242.57  E-value: 2.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  13 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQIHAECKRFGKAYN 90
Cdd:PRK04837   32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvNQPRALIMAPTRELAVQIHADAEPLAQATG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  91 LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqVRSIASHVR--PD- 167
Cdd:PRK04837  112 LKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGF---IKDIRWLFRrmPPa 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 168 --RQTLLFSATFRKKIEKLARDILIDPIRVVqgdIGEANEDVTQIVEILH--SGPSKWNwLTRRLVEFTSSGSVLLFVTK 243
Cdd:PRK04837  189 nqRLNMLFSATLSYRVRELAFEHMNNPEYVE---VEPEQKTGHRIKEELFypSNEEKMR-LLQTLIEEEWPDRAIIFANT 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 244 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 323
Cdd:PRK04837  265 KHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIG 344

                         330
                  ....*....|....
gi 1371977166 324 RTGRAGEKGVAYTL 337
Cdd:PRK04837  345 RTGRAGASGHSISL 358
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 4-195 5.26e-73

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: 234.91  E-value: 5.26e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMD---QKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQQIEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17945    85 ETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKI 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371977166 161 ASHV-----RPD---------------RQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17945   165 LDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 1-198 1.52e-72

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: 235.29  E-value: 1.52e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd18050    74 MDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQ 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd18050   154 VADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKI 233

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 198
Cdd:cd18050   234 VDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 9-354 2.19e-72

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 245.91  E-value: 2.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEpgdGPIAVIVCPTRELCQQIHAECKRFGK- 87
Cdd:PRK11634   26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVLAPTRELAVQVAEAMTDFSKh 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  88 AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 167
Cdd:PRK11634  101 MRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDPIRV-VQGDIgEANEDVTQIVEILHsGPSKWNWLTRRLvEFTSSGSVLLFVTKKAN 246
Cdd:PRK11634  181 HQTALFSATMPEAIRRITRRFMKEPQEVrIQSSV-TTRPDISQSYWTVW-GMRKNEALVRFL-EAEDFDAAIIFVRTKNA 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 247 AEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTG 326
Cdd:PRK11634  258 TLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTG 337

                         330       340
                  ....*....|....*....|....*...
gi 1371977166 327 RAGEKGVAYTLLTPKDSNfagdLVRNLE 354
Cdd:PRK11634  338 RAGRAGRALLFVENRERR----LLRNIE 361
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 9-334 1.80e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 239.47  E-value: 1.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL---EPGDgPIAVIVCPTRELCQQIHAECKRF 85
Cdd:PRK04537   29 FTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRALILAPTRELAIQIHKDAVKF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  86 GKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHV 164
Cdd:PRK04537  108 GADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEADRMFDLGFIKDIRFLLRRM 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 165 --RPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVLLFVT 242
Cdd:PRK04537  188 peRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ--RIYFPADEEKQTLLLGLLSRSEGARTMVFVN 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 243 KKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 322
Cdd:PRK04537  266 TKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRI 345

                         330
                  ....*....|..
gi 1371977166 323 GRTGRAGEKGVA 334
Cdd:PRK04537  346 GRTARLGEEGDA 357
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 11-195 6.78e-70

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: 226.07  E-value: 6.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  11 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE---LEPGDGPIAVIVCPTRELCQQIHAECKRFGK 87
Cdd:cd17951    12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEGPYGLIVCPSRELARQTHEVIEYYCK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  88 AYN------LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 161
Cdd:cd17951    92 ALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIF 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1371977166 162 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17951   172 SYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 1-196 1.74e-69

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: 224.65  E-value: 1.74e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL-EPGDGPIAVIVCPTRELCQQIH 79
Cdd:cd17958     2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  80 AECKRFgKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 159
Cdd:cd17958    82 AECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371977166 160 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 1-366 4.69e-68

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 231.60  E-value: 4.69e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD--GPIAVIVCPTRELCQQI 78
Cdd:PLN00206  133 LLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQV 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  79 HAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 158
Cdd:PLN00206  213 EDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVM 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 159 SIASHVrPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKwnwltRRLVEFTSSGS-- 236
Cdd:PLN00206  293 QIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhf 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 237 ---VLLFVTKKANAEELASNL-KQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVA 312
Cdd:PLN00206  367 kppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP 446

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371977166 313 RDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLD 366
Cdd:PLN00206  447 NTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 1-201 1.88e-66

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: 219.07  E-value: 1.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-------DQKELEPgdgPIAVIVCPTRE 73
Cdd:cd18052    55 LKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQE---PQALIVAPTRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  74 LCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 153
Cdd:cd18052   132 LANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGF 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371977166 154 EYQVRSIASHV----RPDRQTLLFSATFRKKIEKLARDIL-IDPIRVVQGDIG 201
Cdd:cd18052   212 GPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 1-198 4.18e-65

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: 213.22  E-value: 4.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17957     2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---KKGLRALILAPTRELASQIYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVygGGSMWEQAKALQE---GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQV 157
Cdd:cd17957    79 ELLKLSKGTGLRIVLL--SKSLEAKAKDGPKsitKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1371977166 158 RSI-ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 198
Cdd:cd17957   157 DEIlAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 13-184 1.53e-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: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  13 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 92
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  93 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 172
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153

                         170
                  ....*....|..
gi 1371977166 173 FSATFRKKIEKL 184
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 9-195 2.84e-63

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: 208.32  E-value: 2.84e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgdGPIAVIVCPTRELCQQIHAECKRFGKA 88
Cdd:cd17954    20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLAPTRELAQQISEQFEALGSS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 167
Cdd:cd17954    95 IGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIPRE 174

                         170       180
                  ....*....|....*....|....*...
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17954   175 RTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 4-195 6.06e-61

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: 202.15  E-value: 6.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdqKELEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17959    16 IKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALILSPTRELALQTLKVTK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:cd17959    93 ELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSR 172

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17959   173 LPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEXDc smart00487
DEAD-like helicases superfamily;
4-210 1.04e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 1.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166    4 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 82
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   83 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 161
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1371977166  162 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 210
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
PTZ00424 PTZ00424
helicase 45; Provisional
 9-342 7.20e-57

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 198.13  E-value: 7.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKA 88
Cdd:PTZ00424   48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQ----ALILAPTRELAQQIQKVVLALGDY 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDR 168
Cdd:PTZ00424  123 LKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 169 QTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRrLVEFTSSGSVLLFVTKKANAE 248
Cdd:PTZ00424  203 QVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD-LYETLTITQAIIYCNTRRKVD 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 249 ELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRA 328
Cdd:PTZ00424  282 YLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRF 361

                         330
                  ....*....|....
gi 1371977166 329 GEKGVAYTLLTPKD 342
Cdd:PTZ00424  362 GRKGVAINFVTPDD 375
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 1-201 2.17e-56

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: 191.79  E-value: 2.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQ---KELEPGDG--------PIAVIVC 69
Cdd:cd18051    33 RNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESLPSESGyygrrkqyPLALVLA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  70 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 149
Cdd:cd18051   113 PTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRML 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371977166 150 DMGFEYQVRSIASH-VRP---DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 201
Cdd:cd18051   193 DMGFEPQIRRIVEQdTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 3-192 4.91e-55

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: 186.66  E-value: 4.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   3 QIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKELEPGDGPIAVIVCPTRELCQQIHAEC 82
Cdd:cd17955    13 QCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTPTRELAYQIAEQF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  83 KRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVK---KKATNLQRVSYLVFDEADRMFDMGFEYQVRS 159
Cdd:cd17955    88 RALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSFEDDLAT 167

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371977166 160 IASHVRPDRQTLLFSATFRKKIEKLARDILIDP 192
Cdd:cd17955   168 ILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 8-195 5.04e-54

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: 183.61  E-value: 5.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   8 EYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmlihIMDQKELEPGDGPI--AVIVCPTRELCQQIHAECKRF 85
Cdd:cd17947     9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQCFSVLQQL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  86 GKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEYQVRSIASHV 164
Cdd:cd17947    85 AQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEILRLC 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1371977166 165 RPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17947   165 PRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 207-338 3.97e-53

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: 178.47  E-value: 3.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 207 VTQIVEILHSGpSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIP 286
Cdd:cd18787     1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371977166 287 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 338
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 2-195 2.06e-52

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: 178.90  E-value: 2.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   2 HQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAE 81
Cdd:cd17962     3 SNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIEDQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  82 CKRFGKAY-NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSI 160
Cdd:cd17962    78 AKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371977166 161 ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17962   158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 4-195 3.72e-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: 3.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEgAEIVVCTPGRLIDHVKKK----ATNLQrvsYLVFDEADRMFDMGFEYQVRS 159
Cdd:cd17941    84 KVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpgfdTSNLQ---MLVLDEADRILDMGFKETLDA 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371977166 160 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17941   160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 6-196 1.80e-48

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: 168.92  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   6 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKR 84
Cdd:cd17949     8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  85 FGK-AYNLRSVAVYGGgsmwEQAKA----LQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVR 158
Cdd:cd17949    88 LLKpFHWIVPGYLIGG----EKRKSekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371977166 159 SIASHVR-------------PDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17949   164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 4-189 5.33e-48

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: 167.76  E-value: 5.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAEC 82
Cdd:cd17964     9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQIAAEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  83 KR---FGKAYNLRSvaVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVK--KKATNLQRVSYLVFDEADRMFDMGFEYQ 156
Cdd:cd17964    89 KKllqGLRKLRVQS--AVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMGFRPD 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371977166 157 VRSIASHVRP----DRQTLLFSATFRKKIEKLARDIL 189
Cdd:cd17964   167 LEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 4-196 4.03e-47

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 165.06  E-value: 4.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAY--NLRSVAVYGGGSMWEQ-AKALQEGAEIVVCTPGRLIDHVKKKAT--NLQRVSYLVFDEADRMFDMGFEYQVR 158
Cdd:cd17960    85 SFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLN 164

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371977166 159 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17960   165 RILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 4-193 6.87e-46

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: 161.60  E-value: 6.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD-GPIAVIVCPTRELCQQIHAE- 81
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQVSKVl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  82 ------CKRFgkaynLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFE 154
Cdd:cd17961    89 eqltayCRKD-----VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYE 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1371977166 155 YQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 193
Cdd:cd17961   164 EDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 1-177 1.81e-45

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: 161.64  E-value: 1.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE----LEPGDGPIAVIVCPTRELC 75
Cdd:cd17946     2 LRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTRELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  76 QQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKK---ATNLQRVSYLVFDEADRMFDMG 152
Cdd:cd17946    82 VQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKG 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371977166 153 -FEyQVRSIASHV-------RPDRQTLLFSATF 177
Cdd:cd17946   162 hFA-ELEKILELLnkdragkKRKRQTFVFSATL 193
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 1-186 2.36e-44

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: 157.14  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   1 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 80
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  81 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKA----TNLQrvsYLVFDEADRMFDMGFEYQ 156
Cdd:cd17942    81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1371977166 157 VRSIASHVRPDRQTLLFSATFRKKIEKLAR 186
Cdd:cd17942   158 MRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 4-195 7.94e-44

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: 155.92  E-value: 7.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKElepgDGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17940    14 IFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKK----DVIQALILVPTRELALQTSQVCK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:cd17940    89 ELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNF 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17940   169 LPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 9-193 2.00e-37

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: 138.09  E-value: 2.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFG 86
Cdd:cd17963    14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQ----ALCLAPTRELARQIGEVVEKMG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  87 K------AYNLRSVAVYGGGSMWEQakalqegaeIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDM-GFEYQVRS 159
Cdd:cd17963    89 KftgvkvALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIR 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1371977166 160 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 193
Cdd:cd17963   160 IKRMLPRNCQILLFSATFPDSVRKFAEKIAPNAN 193
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 9-195 2.54e-36

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


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 135.14  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHI-MDQKELEpgdgpiAVIVCPTRELCQQIHAECKRFGK 87
Cdd:cd17939    17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRELAQQIQKVVKALGD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  88 AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 167
Cdd:cd17939    91 YMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPE 170

                         170       180
                  ....*....|....*....|....*...
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17939   171 TQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 4-195 1.82e-34

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: 130.16  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIAVIV-CPTRELCQQIHAEC 82
Cdd:cd17950    17 IVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVLViCHTRELAFQISNEY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  83 KRFGKaY--NLRSVAVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF-DMGFEYQVR 158
Cdd:cd17950    91 ERFSK-YmpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQ 169

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1371977166 159 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 195
Cdd:cd17950   170 EIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 2-199 5.33e-33

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: 126.71  E-value: 5.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   2 HQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQIH 79
Cdd:cd17948     3 EILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  80 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 159
Cdd:cd17948    83 SVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSH 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371977166 160 IASH-----VRPDR--------QTLLFSATFRKKIEKLARDIL-IDPIRVVQGD 199
Cdd:cd17948   163 FLRRfplasRRSENtdgldpgtQLVLVSATMPSGVGEVLSKVIdVDSIETVTSD 216
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 9-196 4.29e-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: 123.32  E-value: 4.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIwpmlIHIMDQKELEPgDGPIAVIVCPTRELCQQIHAECKRFGKA 88
Cdd:cd18046    19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS----ISILQQIDTSL-KATQALVLAPTRELAQQIQKVVMALGDY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDR 168
Cdd:cd18046    94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173

                         170       180
                  ....*....|....*....|....*...
gi 1371977166 169 QTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd18046   174 QVVLLSATMPNDVLEVTTKFMRDPIRIL 201
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 9-195 7.08e-32

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: 122.81  E-value: 7.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMdqkelepgdgpiAVIVCPTRELCQQIHAECKRFgKA 88
Cdd:cd17938    19 WLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEPSRELAEQTYNCIENF-KK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 Y----NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH- 163
Cdd:cd17938    86 YldnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRi 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371977166 164 ----VRPDR-QTLLFSATFRK-KIEKLARDILIDPIRV 195
Cdd:cd17938   166 pkitSDGKRlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 219-329 1.13e-31

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: 118.85  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 219 SKWNWLtRRLVEFTSSGSVLLFV--TKKANAEELasnLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAAR 296
Cdd:pfam00271   1 EKLEAL-LELLKKERGGKVLIFSqtKKTLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1371977166 297 GLDIPSIKTVINYDVARDIDTHTHRIGRTGRAG 329
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 4-186 2.02e-31

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


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 120.83  E-value: 2.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   4 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDqkeLEPGdGPIAVIVCPTRELCQQIHAECK 83
Cdd:cd17943     5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIHDVFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 163
Cdd:cd17943    80 KIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159

                         170       180
                  ....*....|....*....|....
gi 1371977166 164 VRPDRQTLLFSATFRKK-IEKLAR 186
Cdd:cd17943   160 LPKNKQVIAFSATYPKNlDNLLAR 183
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 14-176 6.80e-31

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: 119.95  E-value: 6.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  14 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKayNLR 92
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  93 SVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS-----HVRPD 167
Cdd:cd17944    93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172


                  ....*....
gi 1371977166 168 RQTLLFSAT 176
Cdd:cd17944   173 PQTLLFSAT 181
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 12-186 1.45e-30

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: 120.04  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  12 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKeLEPGDGPI--AVIVCPTRELCQQIHAECKRFGKAY 89
Cdd:cd17956    22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIVVPTKELVQQVYKVFESLCKGT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  90 NLRSVAVYGGGSMWEQAKALQEG--------AEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEY---QV 157
Cdd:cd17956    96 GLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRFLVIDEADRLLNQSFQDwleTV 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1371977166 158 -RSIASHVRPDR----------------QTLLFSATFRKKIEKLAR 186
Cdd:cd17956   176 mKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 9-196 7.93e-29

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: 114.10  E-value: 7.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKA 88
Cdd:cd18045    19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQ----ALILSPTRELAVQIQKVLLALGDY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  89 YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDR 168
Cdd:cd18045    94 MNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT 173

                         170       180
                  ....*....|....*....|....*...
gi 1371977166 169 QTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd18045   174 QVVLVSATLPQDILEMTNKFMTDPIRIL 201
HELICc smart00490
helicase superfamily c-terminal domain;
248-329 1.11e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.22  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  248 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 327
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1371977166  328 AG 329
Cdd:smart00490  81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
26-324 3.68e-26

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 113.20  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  26 GRDMIGIAKTGSGKTAafiwpMLIHIMDQKelepGDGPIAVIVCPTRELCQQIHAECKRFgkaynLRSVAVYGGgsmweq 105
Cdd:COG1061   100 GGRGLVVAPTGTGKTV-----LALALAAEL----LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG------ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 106 akALQEGAEIVVCTPGRLIDHVKKKATNlQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRqTLLFSAT--------- 176
Cdd:COG1061   160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgrei 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 177 ---------FRKKIEKLARDILIDPIRVV---------QGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVL 238
Cdd:COG1061   232 llflfdgivYEYSLKEAIEDGYLAPPEYYgirvdltdeRAEYDALSERLRE--ALAADAERKDKILRELLREHPDDRKTL 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 239 LFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVInydVARDIDTH 318
Cdd:COG1061   310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSP 386


                  ....*....
gi 1371977166 319 TH---RIGR 324
Cdd:COG1061   387 REfiqRLGR 395
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 7-196 3.44e-21

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: 93.21  E-value: 3.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   7 SEYTQPTPIQCQGVPvALSGRDMIGI-----------------AKTGSGKTAAFIWPMLIHIMDQKELEPGDG------- 62
Cdd:cd17965    26 DEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesa 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  63 -----PIAVIVCPTRELCQQIHAECKRFGKA--YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQ 135
Cdd:cd17965   105 kdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILS 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371977166 136 RVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 196
Cdd:cd17965   185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
24-335 8.65e-17

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 83.79  E-value: 8.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  24 LSGRDMIGIAKTGSGKTA-AFIWpMLIHIMDqkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGgsm 102
Cdd:COG1204    36 LEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 103 WEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA------DRmfdmGFEYQVrsIASHVR---PDRQTLLF 173
Cdd:COG1204   104 YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPTLEV--LLARLRrlnPEAQIVAL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 174 SATFrKKIEKLAR----DILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEE 249
Cdd:COG1204   178 SATI-GNAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLE--EGGQVLVFVSSRRDAES 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 250 LASNLKQE------GHNLGLL-------------------------------HGDMDQSERNKVISDFKKKDIPVLVATD 292
Cdd:COG1204   255 LAKKLADElkrrltPEEREELeelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATP 334

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371977166 293 VAARGLDIPSiKTVINYDVAR----DIDTHTHR--IGRTGRAG--EKGVAY 335
Cdd:COG1204   335 TLAAGVNLPA-RRVIIRDTKRggmvPIPVLEFKqmAGRAGRPGydPYGEAI 384
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 9-192 1.02e-16

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: 79.68  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFG 86
Cdd:cd18048    38 FNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-DALKLYPQ----CLCLSPTFELALQTGKVVEEMG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  87 KAYNLRSV--AVYGGgsmwEQAKALQEGAEIVVCTPGRLIDHV-KKKATNLQRVSYLVFDEADRMFDM-GFEYQVRSIAS 162
Cdd:cd18048   113 KFCVGIQViyAIRGN----RPGKGTDIEAQIVIGTPGTVLDWCfKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKR 188

                         170       180       190
                  ....*....|....*....|....*....|
gi 1371977166 163 HVRPDRQTLLFSATFRKKIEKLARDILIDP 192
Cdd:cd18048   189 SMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 9-192 4.05e-16

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: 77.45  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImdqkelEPG-DGPIAVIVCPTRELCQQIHAECKRF 85
Cdd:cd18047    21 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnKYPQCLCLSPTYELALQTGKVIEQM 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  86 GKAYNLRSVAVYGGGSMWEQAKALQEgaEIVVCTPGRLIDH-VKKKATNLQRVSYLVFDEADRMF-DMGFEYQVRSIASH 163
Cdd:cd18047    95 GKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRM 172

                         170       180
                  ....*....|....*....|....*....
gi 1371977166 164 VRPDRQTLLFSATFRKKIEKLARDILIDP 192
Cdd:cd18047   173 LPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
212-343 3.96e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.92  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 212 EILHSGPSKwnwlTRRLVEFT----SSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGD--------MDQSERNKVISD 279
Cdd:COG1111   331 DIEHPKLSK----LREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILER 406

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166 280 FKKKDIPVLVATDVAARGLDIPSIKTVINYD-VA---RDIdthtHRIGRTGRAGEKGVaYTLLTpKDS 343
Cdd:COG1111   407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPseiRSI----QRKGRTGRKREGRV-VVLIA-KGT 468
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
220-342 8.24e-12

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 67.86  E-value: 8.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 220 KWNWLTRRLVEFTSsGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGL 298
Cdd:COG0514   217 KLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1371977166 299 DIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 342
Cdd:COG0514   295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 33-331 1.13e-11

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: 66.68  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  33 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHAECKR-FGKAYNLRSVAVYGGGSMWEQAKALQ 110
Cdd:cd09639     6 APTGYGKTeAALLW--ALHSLKSQKADRV-----IIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 111 E-------------GAEIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAshvRPD 167
Cdd:cd09639    79 HlfplyihsndtlfLDPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK---DND 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 168 RQTLLFSATFRKKIEKLARDILIDpirvvqgdigEANE-------DVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLF 240
Cdd:cd09639   155 VPILLMSATLPKFLKEYAEKIGYV----------EENEpldlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 241 VTKKANAEELASNLKQEGH--NLGLLHGDMDQSERNK----VISDFKKKDIPVLVATDVAARGLDIPSikTVINYDVArD 314
Cdd:cd09639   225 VNTVDRAQEFYQQLKEKGPeeEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-P 301

                         330
                  ....*....|....*..
gi 1371977166 315 IDTHTHRIGRTGRAGEK 331
Cdd:cd09639   302 IDSLIQRLGRLHRYGEK 318
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 28-325 1.46e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 67.56  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  28 DMigiaktGSGKTA---AFIwpmlihimdQKELEPGDGPIAVIVCPTReLCQQIHAECKRFgkAYNLRSVAVYGGGSMWE 104
Cdd:COG0553   268 DM------GLGKTIqalALL---------LELKERGLARPVLIVAPTS-LVGNWQRELAKF--APGLRVLVLDGTRERAK 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 105 QAKALQEgAEIVVCTpgrlIDHVKKKATNLQRV--SYLVFDEADRMFDMG-FEYQ-VRSIASHVR--------------- 165
Cdd:COG0553   330 GANPFED-ADLVITS----YGLLRRDIELLAAVdwDLVILDEAQHIKNPAtKRAKaVRALKARHRlaltgtpvenrleel 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 166 ------------PDRQTllFSATFRKKIEK--------LAR------------DILID-PIRVVQ--------------- 197
Cdd:COG0553   405 wslldflnpgllGSLKA--FRERFARPIEKgdeealerLRRllrpfllrrtkeDVLKDlPEKTEEtlyveltpeqralye 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 198 -------GDIGEANEDVTQIV----------------------EILHSGPSKWNWLTRRLVEFTSSG-SVLLFVTKKANA 247
Cdd:COG0553   483 avleylrRELEGAEGIRRRGLilaaltrlrqicshpallleegAELSGRSAKLEALLELLEELLAEGeKVLVFSQFTDTL 562

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 248 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFK-KKDIPV-LVATDVAARGLDIPSIKTVINYD-----------VARd 314
Cdd:COG0553   563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPVfLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR- 641

                         410
                  ....*....|.
gi 1371977166 315 idthTHRIGRT 325
Cdd:COG0553   642 ----AHRIGQT 648
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 33-176 2.80e-11

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: 61.65  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  33 AKTGSGKT-AAFIWpmLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKaYNLRSVAVYGGGSMWEQAKALQE 111
Cdd:cd00046     8 APTGSGKTlAALLA--ALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166 112 GAEIVVCTPGRLIDHVK-KKATNLQRVSYLVFDEADRM-FDMGFEYQVR-SIASHVRPDRQTLLFSAT 176
Cdd:cd00046    79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALlIDSRGALILDlAVRKAGLKNAQVILLSAT 146
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
 35-344 5.54e-11

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: 65.49  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  35 TGSGKT-AAFIWpMLIHimdqkeLEPGDGPIAVIVCPTRELCQQIHaecKRFGKAYNLrSVAVYGGGSMWEQAKALQEG- 112
Cdd:COG1203   156 TGGGKTeAALLF-ALRL------AAKHGGRRIIYALPFTSIINQTY---DRLRDLFGE-DVLLHHSLADLDLLEEEEEYe 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 113 --------------AEIVVCTPGRLIDHV-------KKKATNLQRvSYLVFDEADrMFDMgfEYQ---VRSIASHVRPDR 168
Cdd:COG1203   225 searwlkllkelwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVIILDEVQ-AYPP--YMLallLRLLEWLKNLGG 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 169 QTLLFSATFRKKIeklaRDILIDPIRVVQGDIGEANEDVTQIVE---ILHSGPSKWNWLTRRLVE-FTSSGSVLLFVTKK 244
Cdd:COG1203   301 SVILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVRkrvELKEGPLSDEELAELILEaLHKGKSVLVIVNTV 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 245 ANAEELASNLKQEGHNLG--LLHGDMDQSERNKVISD----FKKKDIPVLVATDVAARGLDipsiktvINYDVA-RD--- 314
Cdd:COG1203   377 KDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVD-------IDFDVViRDlap 449

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1371977166 315 IDTHTHRIGRT---GRAGEKGVAYtLLTPKDSN 344
Cdd:COG1203   450 LDSLIQRAGRCnrhGRKEEEGNVY-VFDPEDEG 481
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
 33-331 5.75e-11

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


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 64.78  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  33 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 111
Cdd:TIGR01587   6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 112 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 163
Cdd:TIGR01587  76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 164 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 243
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 244 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 316
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308

                         330
                  ....*....|....*
gi 1371977166 317 THTHRIGRTGRAGEK 331
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 35-145 1.23e-10

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: 61.13  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  35 TGSGKTaaFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQihaECKRFGKAYNLRSVAVYG--GGSMWEQAKALQE 111
Cdd:cd18034    25 TGSGKT--LIAVMLIKEMgELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKWTKERWKEE 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1371977166 112 --GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA 145
Cdd:cd18034   100 leKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 211-323 4.56e-10

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: 57.87  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 211 VEILHSGpsKWNWLTRRLVEFTSSGS-VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKK-KDIPV- 287
Cdd:cd18793     5 IEEVVSG--KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIRVf 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1371977166 288 LVATDVAARGLDIPSIKTVINYDV----ARD---IDtHTHRIG 323
Cdd:cd18793    83 LLSTKAGGVGLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 13-145 4.96e-10

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: 59.20  E-value: 4.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  13 TPIQCQGV-PVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNL 91
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166  92 RSVAVYGGGSMweqAKALQEGAEIVVCTP----GRLIDHvkkKATNLQRVSYLVFDEA 145
Cdd:cd17921    76 NVGLLTGDPSV---NKLLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 244-369 8.74e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.65  E-value: 8.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 244 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 323
Cdd:PRK11057  246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371977166 324 RTGRAGEKGVAYTLLTPKDSNFagdLVRNLE----GANQHVSKELLDlAM 369
Cdd:PRK11057  326 RAGRDGLPAEAMLFYDPADMAW---LRRCLEekpaGQQQDIERHKLN-AM 371
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 268-338 1.25e-09

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: 56.98  E-value: 1.25e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371977166 268 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLL 338
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 16-338 1.27e-09

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: 61.39  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  16 QCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDqkelepGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SV 94
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DPGATALYLYPTKALARDQLRRLRELAEALGLGvRV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  95 AVYGGGSMWEQAKALQEGAEIVVCTP-----GrLIDHVKKKATNLQRVSYLVFDEA---------------DRMfdmgfe 154
Cdd:COG1205   135 ATYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAhtyrgvfgshvanvlRRL------ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 155 yqvRSIASHVRPDRQTLLFSATfrkkI---EKLARDILIDPIRVVQGDiGEAnedvTQIVEILHSGPSKWNWLTRR---- 227
Cdd:COG1205   208 ---RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVDED-GSP----RGERTFVLWNPPLVDDGIRRsala 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 228 -----LVEFTSSG-SVLLFVTKKANAEELASNLKQEGHNLGLL------HGDMDQSERNKVISDFKKKDIPVLVATDVAA 295
Cdd:COG1205   276 eaarlLADLVREGlRTLVFTRSRRGAELLARYARRALREPDLAdrvaayRAGYLPEERREIERGLRSGELLGVVSTNALE 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1371977166 296 RGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 338
Cdd:COG1205   356 LGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 224-327 1.37e-09

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: 56.89  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 224 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQ------EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 297
Cdd:cd18796    28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 1371977166 298 LDIPSIKTVINYDVARDIDTHTHRIGRTGR 327
Cdd:cd18796   108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 246-340 2.10e-09

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 56.89  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 246 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI- 322
Cdd:cd18792    46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125

                          90
                  ....*....|....*...
gi 1371977166 323 GRTGRAGEKGVAYtLLTP 340
Cdd:cd18792   126 GRVGRGKHQSYCY-LLYP 142
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 230-354 3.71e-09

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 55.81  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 230 EFTSSGSVLLFVTKKANAEELASNLKQ--EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 307
Cdd:cd18810    21 ELLRGGQVFYVHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1371977166 308 --NYDVARDIDTHTHRiGRTGRAGEKGVAYtLLTPKDSNFAGDLVRNLE 354
Cdd:cd18810   101 ieRADKFGLAQLYQLR-GRVGRSKERAYAY-FLYPDQKKLTEDALKRLE 147
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 287-339 1.24e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.32  E-value: 1.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371977166 287 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLT 339
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 243-355 1.35e-08

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: 54.27  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 243 KKANA--EELASNLKQEgHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTH 320
Cdd:cd18811    45 KAAVAmyEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLH 123

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1371977166 321 RI-GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEG 355
Cdd:cd18811   124 QLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 226-330 2.08e-08

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: 53.37  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 226 RRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKT 305
Cdd:cd18794    22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101

                          90       100
                  ....*....|....*....|....*
gi 1371977166 306 VINYDVARDIDTHTHRIGRTGRAGE 330
Cdd:cd18794   102 VIHYSLPKSMESYYQESGRAGRDGL 126
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
245-307 3.31e-08

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 56.60  E-value: 3.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371977166 245 ANAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdvaargldipsikTVI 307
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT-------------TVI 539
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 238-339 3.56e-08

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: 52.59  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 238 LLFVTKKANAEELASNLKQEGHNLGLLHGD---------------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPS 302
Cdd:cd18802    29 IIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1371977166 303 IKTVINYDVARDIdthTHRIGRTGRAGEKGVAYTLLT 339
Cdd:cd18802   109 CNLVIRFDLPKTL---RSYIQSRGRARAPNSKYILMV 142
PRK13766 PRK13766
Hef nuclease; Provisional
 268-339 3.57e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 56.81  E-value: 3.57e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371977166 268 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLLT 339
Cdd:PRK13766  407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIA 477
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
6-350 9.71e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 55.49  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   6 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKELEPGDGPIAVI-VCPTRELCQQIHaeck 83
Cdd:COG1201    19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPA-LDELARRPRPGELPDGLRVLyISPLKALANDIE---- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  84 RfgkayNLR-----------------SVAV-YGGGSMWEQAKALQEGAEIVVCTPGRLidHV----KKKATNLQRVSYLV 141
Cdd:COG1201    94 R-----NLRapleeigeaaglplpeiRVGVrTGDTPASERQRQRRRPPHILITTPESL--ALlltsPDARELLRGVRTVI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 142 FDEadrmfdmgfeyqVRSIAS---------------HVRPDR-QTLLFSATFRkKIEKLAR----DILIDPIRVVQGDIG 201
Cdd:COG1201   167 VDE------------IHALAGskrgvhlalslerlrALAPRPlQRIGLSATVG-PLEEVARflvgYEDPRPVTIVDAGAG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 202 -----EANEDVTQIVEILHSGPSKWNWLTRRLVEF-TSSGSVLLFVTKKANAEELASNLKQ----EGHNLGLLHGDMDQS 271
Cdd:COG1201   234 kkpdlEVLVPVEDLIERFPWAGHLWPHLYPRVLDLiEAHRTTLVFTNTRSQAERLFQRLNElnpeDALPIAAHHGSLSRE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 272 ERNKVISDFKKKDIPVLVAT---DVaarGLDIPSIKTVINYD----VARDIdthtHRIGRTG-RAGEKGVAYtlLTPKDs 343
Cdd:COG1201   314 QRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGspksVARLL----QRIGRAGhRVGEVSKGR--LVPTH- 383


                  ....*..
gi 1371977166 344 nfAGDLV 350
Cdd:COG1201   384 --RDELV 388
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 236-307 1.91e-07

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 49.87  E-value: 1.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371977166 236 SVLLFVTKKANAEELASNLKQEGHNLGLLHGD--MDQSERNKVISDFK-KKDIPVLVATDVAARGLDIPSIKTVI 307
Cdd:cd18799     8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFgELKPPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 230-337 9.51e-07

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: 49.09  E-value: 9.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 230 EFTSSGSVLLFVTKKANAEELASNLKqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVI-- 307
Cdd:cd18795    39 TVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPA-RTVIik 113

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1371977166 308 -----NYDVARDIDTHTHR--IGRTGRAG--EKGVAYTL 337
Cdd:cd18795   114 gtqryDGKGYRELSPLEYLqmIGRAGRPGfdTRGEAIIM 152
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 246-301 1.19e-06

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 51.69  E-value: 1.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166 246 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 301
Cdd:PRK10917  491 SAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 35-177 1.48e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.07  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  35 TGSGKT---AAFIWpmliHIMDQKELepgdgpiavIVCPTRELCQQIHAECKRFGKAynlRSVAVYGGGSmweqaKALQE 111
Cdd:cd17926    27 TGSGKTltaLALIA----YLKELRTL---------IVVPTDALLDQWKERFEDFLGD---SSIGLIGGGK-----KKDFD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371977166 112 GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRQtLLFSATF 177
Cdd:cd17926    86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTATP 146
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 12-144 1.81e-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: 49.01  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  12 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEPGDGPIAVIVCPTRELC-QQIHAECKRFGKAYN 90
Cdd:cd18036     3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKGYK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166  91 LrsVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATN----LQRVSYLVFDE 144
Cdd:cd18036    81 V--TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 238-331 2.85e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 50.66  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  238 LLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDT 317
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763

                           90
                   ....*....|....
gi 1371977166  318 HTHRIGRTGRAGEK 331
Cdd:PLN03137   764 YHQECGRAGRDGQR 777
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 26-144 3.21e-06

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: 47.58  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  26 GRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKElepgdGPIAVI-VCPTRELCQQIHAECKRFGKAYNL-RSVAV-YGGGS 101
Cdd:cd17922     1 GRNVLIAAPTGSGKTeAAFLPA-LSSLADEPE-----KGVQVLyISPLKALINDQERRLEEPLDEIDLeIPVAVrHGDTS 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1371977166 102 MWEQAKALQEGAEIVVCTP---GRLIDHvKKKATNLQRVSYLVFDE 144
Cdd:cd17922    75 QSEKAKQLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDE 119
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 237-310 4.48e-06

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 47.24  E-value: 4.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371977166 237 VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD 310
Cdd:cd18790    30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
 265-354 6.55e-06

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 49.74  E-value: 6.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  265 HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI-----NYDVARdidTHTHRiGRTGRAGEKGVAYtLLT 339
Cdd:PRK10689   842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieradHFGLAQ---LHQLR-GRVGRSHHQAYAW-LLT 916

                           90
                   ....*....|....*
gi 1371977166  340 PKDSNFAGDLVRNLE 354
Cdd:PRK10689   917 PHPKAMTTDAQKRLE 931
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 11-147 1.28e-05

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 46.66  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  11 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTaaFIwPMLI--HIMDQKELEPGdGPIAVIVcPTRELC-QQIHAECKRFGK 87
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FV-AVLIceHHLKKFPAGRK-GKVVFLA-NKVPLVeQQKEVFRKHFER 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371977166  88 AYnLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADR 147
Cdd:cd17927    77 PG-YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 15-120 4.61e-05

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: 45.04  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  15 IQCQGVPVAL-SGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK-RFGKaYNLR 92
Cdd:cd18023     5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82

                          90       100
                  ....*....|....*....|....*...
gi 1371977166  93 SVAVYGGGSMWEQAKAlqEGAEIVVCTP 120
Cdd:cd18023    83 CAELTGDTEMDDTFEI--QDADIILTTP 108
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 238-344 4.90e-05

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: 44.22  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 238 LLFVTK---KANAEELASNLKQEGHNLGLLHgdmdqSERNKVISDFKKKDIPVLVAT----DVAARGLDIP-SIKTVINY 309
Cdd:cd18798    28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFY 102

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1371977166 310 DVArdIDTHTHRIGRTGR--AGE--KGVAYTLLTPKDSN 344
Cdd:cd18798   103 GVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPELF 139
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 233-337 7.42e-05

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 43.68  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 233 SSGSVLLFVTKKANAEELASNLKQEGHNLGL-------LHGDMDQSERNKVI---SDFKKKdipVLVATDVAARGLDIPS 302
Cdd:cd18791    42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkllvlpLHSSLPPEEQQRVFeppPPGVRK---VVLATNIAETSITIPG 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371977166 303 IKTVI--------NYDVARDIDT-HTHRIG------RTGRAG--EKGVAYTL 337
Cdd:cd18791   119 VVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRL 170
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 32-87 1.23e-04

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 44.98  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371977166  32 IAKTGSGKTAAFIWPMLIHimdqkeLEPGDGpiAVIVCPTRELCQQIHAECKRFGK 87
Cdd:COG3505     5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
PRK01172 PRK01172
ATP-dependent DNA helicase;
145-329 1.25e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 45.26  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 145 ADRMFDMGFEYQ------VRSIASHVRPDRQTLLFSATFRKKIEK---LARDILIDPIRVVQGDIGEANEDvTQIVEILH 215
Cdd:PRK01172  141 ADEIHIIGDEDRgptletVLSSARYVNPDARILALSATVSNANELaqwLNASLIKSNFRPVPLKLGILYRK-RLILDGYE 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 216 SGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEELASNLKQE-------------------------GHNLGLLHGDMDQ 270
Cdd:PRK01172  220 RSQVDINSLIKETVN--DGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnvyddslnemlPHGVAFHHAGLSN 297

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371977166 271 SERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVINYDVARDIDTHT---------HRIGRTGRAG 329
Cdd:PRK01172  298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA-RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 22-147 1.28e-04

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 43.27  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  22 VALSGRDMIgIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIaVIVCPTRELCQQiHAEckRFGKAYNL--RSVAVYGG 99
Cdd:cd18035    13 VALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQ-HAE--NLKRVLNIpdKITSLTGE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1371977166 100 GSMWEQAKALQEGaEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 147
Cdd:cd18035    82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
secA PRK12898
preprotein translocase subunit SecA; Reviewed
 219-378 2.31e-04

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237253 [Multi-domain]  Cd Length: 656  Bit Score: 44.23  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 219 SKWNWLTRRLVEFTSSGSVLLFVTKK-ANAEELASNLKQEGHNLGLLHGDMDQSErNKVISDFKKKDiPVLVATDVAARG 297
Cdd:PRK12898  457 AKWAAVAARVRELHAQGRPVLVGTRSvAASERLSALLREAGLPHQVLNAKQDAEE-AAIVARAGQRG-RITVATNMAGRG 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 298 LDIPsiktvINYDVARD-----IDTHTHR--------IGRTGRAGEKGVAYTLLTPKD---SNFAGDLVRNLEGANQHVS 361
Cdd:PRK12898  535 TDIK-----LEPGVAARgglhvILTERHDsaridrqlAGRCGRQGDPGSYEAILSLEDdllQSFLGSRGLAIRRMELLGP 609

                         170
                  ....*....|....*..
gi 1371977166 362 KELLDLAMQNAWFRKSR 378
Cdd:PRK12898  610 RGGRALGALLLRRAQRR 626
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 237-332 6.09e-04

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 40.70  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 237 VLLFVTKKANAEELASNLkqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIktvinyDVARDID 316
Cdd:cd18789    52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA------NVAIQIS 120

                          90       100
                  ....*....|....*....|...
gi 1371977166 317 TH-------THRIGRTGRAGEKG 332
Cdd:cd18789   121 GHggsrrqeAQRLGRILRPKKGG 143
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 28-145 9.04e-04

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 41.01  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  28 DMigiaktGSGKTAAfiwpMLIHIMDQKElEPGDGPiAVIVCPTrELCQQIHAECKRFgkAYNLRSVAVYGGGSMWEQAK 107
Cdd:cd18012    31 DM------GLGKTLQ----TLALLLSRKE-EGRKGP-SLVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1371977166 108 ALqEGAEIVVCTPG---RLIDHVKKkatnlQRVSYLVFDEA 145
Cdd:cd18012    96 AL-EDYDLVITSYGllrRDIELLKE-----VKFHYLVLDEA 130
ResIII pfam04851
Type III restriction enzyme, res subunit;
35-177 9.77e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.35  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  35 TGSGKTAafiwpMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSvAVYGGGSMweqaKALQEGAE 114
Cdd:pfam04851  32 TGSGKTL-----TAAKLIARL-FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIG-EIISGDKK----DESVDDNK 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371977166 115 IVVCTP---GRLIDHVKKKATNLQRVsYLVFDEADRMFDMGFeyqvRSIASHVRPdrQTLL-FSATF 177
Cdd:pfam04851 101 IVVTTIqslYKALELASLELLPDFFD-VIIIDEAHRSGASSY----RNILEYFKP--AFLLgLTATP 160
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 23-145 1.58e-03

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: 39.88  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  23 ALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGG-G 100
Cdd:cd17923    12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATYDGdT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1371977166 101 SMWEQAKALQEGAEIVVCTPGRL----IDHVKKKATNLQRVSYLVFDEA 145
Cdd:cd17923    86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 380-625 1.66e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 41.52  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 380 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSnyeAYKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 459
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGC---TNPPPSGSHE---------------------SFSNSGGS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 460 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 539
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166 540 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 619
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358


                  ....*.
gi 1371977166 620 GFNREN 625
Cdd:cd21118   359 PFNFDT 364
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 14-145 4.28e-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: 39.16  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166  14 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdQKELEPGdgpIAVIVCPTRELCQ-QIHAeCKRFGKAYNLR 92
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQVDA-LPRAIKAAALN 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371977166  93 SVAvyGGGSMWEQAKALQEG-AEIVVCTPGRLID-HVKKKATNLQRVSYLVFDEA 145
Cdd:cd18018    87 SSL--TREERRRILEKLRAGeVKILYVSPERLVNeSFRELLRQTPPISLLVVDEA 139
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 9-145 5.65e-03

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: 38.67  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371977166   9 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdqkelepgDGPIAVIVCPTRELCQ-QIHaECKRFGK 87
Cdd:cd17920    10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-RLQQLGI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371977166  88 aynlRSVAVYGGGSMWEQAKALQEGAE----IVVCTPGRLI-DHVKK---KATNLQRVSYLVFDEA 145
Cdd:cd17920    78 ----RAAALNSTLSPEEKREVLLRIKNgqykLLYVTPERLLsPDFLEllqRLPERKRLALIVVDEA 139
 
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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