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Conserved domains on  [gi|1907083232|ref|XP_036012900|]
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ATP-dependent RNA helicase DDX42 isoform X1 [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];
91-515 1.03e-159

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 469.24  E-value: 1.03e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 170
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:COG0513    79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 328
Cdd:COG0513   159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 329 LVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:COG0513   235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 409 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 487
Cdd:COG0513   315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
                         410       420
                  ....*....|....*....|....*...
gi 1907083232 488 LNIGGGGLGYRERPGlGSENSDRGNNNN 515
Cdd:COG0513   391 LKGKKAGRGGRPGPK-GERKARRGKRRR 417
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
481-726 5.93e-04

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: 43.06  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 481 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSNYeayKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 560
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGCTN---PPPSGSHE---------------------SFSNSGGS 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 561 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 640
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 641 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 720
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358

                  ....*.
gi 1907083232 721 GFNREN 726
Cdd:cd21118   359 PFNFDT 364
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
91-515 1.03e-159

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 469.24  E-value: 1.03e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 170
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:COG0513    79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 328
Cdd:COG0513   159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 329 LVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:COG0513   235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 409 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 487
Cdd:COG0513   315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
                         410       420
                  ....*....|....*....|....*...
gi 1907083232 488 LNIGGGGLGYRERPGlGSENSDRGNNNN 515
Cdd:COG0513   391 LKGKKAGRGGRPGPK-GERKARRGKRRR 417
PTZ00110 PTZ00110
helicase; Provisional
30-489 5.99e-149

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 446.53  E-value: 5.99e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  30 SKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLR--HKLNLrVSGAAPPRPGSSFAHFGFDEQLMHQIRK 107
Cdd:PTZ00110   69 SSTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRkeKEITI-IAGENVPKPVVSFEYTSFPDYILKSLKN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 108 SEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFG 187
Cdd:PTZ00110  148 AGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 188 KAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRP 267
Cdd:PTZ00110  228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRP 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 268 DRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLLFVT 343
Cdd:PTZ00110  308 DRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILIFVE 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 344 KKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 423
Cdd:PTZ00110  386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 424 GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 489
Cdd:PTZ00110  466 GRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
101-297 5.77e-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: 414.89  E-value: 5.77e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17952    81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17952   161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
114-285 6.97e-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: 6.97e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 114 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 193
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 194 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 273
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 1907083232 274 FSATFRKKIEKL 285
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
105-311 4.04e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 4.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  105 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 183
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  184 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 262
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907083232  263 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 311
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
134-432 7.04e-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: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 212
Cdd:TIGR01587   6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 213 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 264
Cdd:TIGR01587  76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 265 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 344
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 417
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308
                         330
                  ....*....|....*
gi 1907083232 418 THTHRIGRTGRAGEK 432
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
481-726 5.93e-04

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: 43.06  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 481 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSNYeayKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 560
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGCTN---PPPSGSHE---------------------SFSNSGGS 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 561 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 640
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 641 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 720
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358

                  ....*.
gi 1907083232 721 GFNREN 726
Cdd:cd21118   359 PFNFDT 364
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
91-515 1.03e-159

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 469.24  E-value: 1.03e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 170
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:COG0513    79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 328
Cdd:COG0513   159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 329 LVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:COG0513   235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 409 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 487
Cdd:COG0513   315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
                         410       420
                  ....*....|....*....|....*...
gi 1907083232 488 LNIGGGGLGYRERPGlGSENSDRGNNNN 515
Cdd:COG0513   391 LKGKKAGRGGRPGPK-GERKARRGKRRR 417
PTZ00110 PTZ00110
helicase; Provisional
30-489 5.99e-149

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 446.53  E-value: 5.99e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  30 SKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLR--HKLNLrVSGAAPPRPGSSFAHFGFDEQLMHQIRK 107
Cdd:PTZ00110   69 SSTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRkeKEITI-IAGENVPKPVVSFEYTSFPDYILKSLKN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 108 SEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFG 187
Cdd:PTZ00110  148 AGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFG 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 188 KAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRP 267
Cdd:PTZ00110  228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRP 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 268 DRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLLFVT 343
Cdd:PTZ00110  308 DRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILIFVE 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 344 KKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 423
Cdd:PTZ00110  386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 424 GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 489
Cdd:PTZ00110  466 GRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
101-297 5.77e-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: 414.89  E-value: 5.77e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17952    81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17952   161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
110-450 4.00e-106

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 332.54  E-value: 4.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 110 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKELepgdGPIAVIVCPTRELCQQIHAECKRFGKA 189
Cdd:PRK11776   24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAKEIRRLARF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 190 -YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 268
Cdd:PRK11776   99 iPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 269 RQTLLFSATFRKKIEKLARDILIDPIRVvqgdIGEANEDVTQI----VEILHSGpsKWNWLTRRLVEFTSSgSVLLFVTK 344
Cdd:PRK11776  179 RQTLLFSATYPEGIAAISQRFQRDPVEV----KVESTHDLPAIeqrfYEVSPDE--RLPALQRLLLHHQPE-SCVVFCNT 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 424
Cdd:PRK11776  252 KKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIG 331
                         330       340
                  ....*....|....*....|....*.
gi 1907083232 425 RTGRAGEKGVAYTLLTPKDSNFAGDL 450
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) ...
79-296 1.29e-102

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: 314.70  E-value: 1.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  79 RVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL 158
Cdd:cd17953     1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 159 EPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV---KKKATNL 235
Cdd:cd17953    81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 236 QRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17953   161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
101-297 6.46e-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: 298.90  E-value: 6.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17966    81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17966   161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
101-296 1.04e-96

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 298.20  E-value: 1.04e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd00268    80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd00268   160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
92-438 1.69e-93

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 298.78  E-value: 1.69e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCP 171
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:PRK11192   82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFR-KKIEKLARDILIDPIRVvqgdigEAN------EDVTQIVEILHSGPSKWNW 324
Cdd:PRK11192  162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKTAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLlFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 404
Cdd:PRK11192  236 LCHLLKQPEVTRSIV-FVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1907083232 405 KTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 438
Cdd:PRK11192  315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
41-296 1.60e-89

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: 282.28  E-value: 1.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  41 DHSEIdyPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQG 120
Cdd:cd18050    15 DLSEL--PKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 121 VPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGG 200
Cdd:cd18050    93 FPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 201 GSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRK 280
Cdd:cd18050   173 APKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPK 252
                         250
                  ....*....|....*.
gi 1907083232 281 KIEKLARDILIDPIRV 296
Cdd:cd18050   253 EVRQLAEDFLRDYVQI 268
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
91-515 8.49e-81

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 265.90  E-value: 8.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPI-AVIV 169
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:PRK10590   82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIV---------EILHSGPS 320
Cdd:PRK10590  162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVhfvdkkrkrELLSQMIG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 321 KWNWltrrlveftssGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLD 400
Cdd:PRK10590  242 KGNW-----------QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 401 IPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEganqhvsKELLDLAM---------- 470
Cdd:PRK10590  311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK-------KEIPRIAIpgyepdpsik 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1907083232 471 ----QNAwfRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENSDRGNNNN 515
Cdd:PRK10590  384 aepiQNG--RQQRGGGGRGQGGGRGQQQGQPRRGEGGAKSASAKPAEKP 430
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
91-302 1.05e-79

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: 254.72  E-value: 1.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDG-----PI 165
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 166 AVIVCPTRELCQQIHAECKRFgkAYN--LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVF 243
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 244 DEADRMFDMGFEYQVRSIASH----VRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 302
Cdd:cd17967   159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
27-467 2.78e-79

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 263.57  E-value: 2.78e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  27 IAPSKKIIDPLPPIDHSEIDyppfeKNFYNEHEEITN-LTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQI 105
Cdd:PLN00206   62 VAKSRVAVGAPKPKRLPATD-----ECFYVRDPGSTSgLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 106 RKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD--GPIAVIVCPTRELCQQIHAEC 183
Cdd:PLN00206  137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 184 KRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS 263
Cdd:PLN00206  217 KVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 264 HVrPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKwnwltRRLVEFTSSGS-----V 338
Cdd:PLN00206  297 AL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhfkppA 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTKKANAEELASNL-KQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDID 417
Cdd:PLN00206  371 VVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907083232 418 THTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLD 467
Cdd:PLN00206  451 EYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
67-296 2.67e-77

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: 248.77  E-value: 2.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  67 QQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIW 146
Cdd:cd18049     1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 147 PMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLID 226
Cdd:cd18049    81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 227 HVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd18049   161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
86-444 1.25e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 255.22  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  86 PRPGSS-FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAF---IWPMLIHIMDQKELEPG 161
Cdd:PRK01297   82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 162 DgPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSY 240
Cdd:PRK01297  162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 241 LVFDEADRMFDMGFEYQVRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILhSG 318
Cdd:PRK01297  241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AG 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 319 PSKWNwLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 398
Cdd:PRK01297  320 SDKYK-LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 399 LDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDS 444
Cdd:PRK01297  399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
34-302 2.54e-74

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


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 242.18  E-value: 2.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  34 IDPLPPIDHSEIdYPPFEK--NFyNEHEEItnltpqqLIDlrhklnlrVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYT 111
Cdd:cd18052     2 IPPPPPEDEDEI-FATIQTgiNF-DKYDEI-------PVE--------VTGRNPPPAILTFEEANLCETLLKNIRKAGYE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-------DQKELEPgdgPIAVIVCPTRELCQQIHAECK 184
Cdd:cd18052    65 KPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQE---PQALIVAPTRELANQIFLEAR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 264
Cdd:cd18052   142 KFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSE 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907083232 265 V----RPDRQTLLFSATFRKKIEKLARDIL-IDPIRVVQGDIG 302
Cdd:cd18052   222 PgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
92-438 1.72e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 245.27  E-value: 1.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIV 169
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvNQPRALIM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:PRK04837   90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 250 FDMGFeyqVRSIASHVR--PD---RQTLLFSATFRKKIEKLARDILIDPIRVVqgdIGEANEDVTQIVEILH--SGPSKW 322
Cdd:PRK04837  170 FDLGF---IKDIRWLFRrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVE---VEPEQKTGHRIKEELFypSNEEKM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 323 NwLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 402
Cdd:PRK04837  244 R-LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1907083232 403 SIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 438
Cdd:PRK04837  323 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
90-455 3.19e-73

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 250.54  E-value: 3.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  90 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEpgdGPIAVIV 169
Cdd:PRK11634    6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGK-AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 248
Cdd:PRK11634   81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV-VQGDIgEANEDVTQIVEILHsGPSKWNWLTR 327
Cdd:PRK11634  161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVrIQSSV-TTRPDISQSYWTVW-GMRKNEALVR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 328 RLvEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTV 407
Cdd:PRK11634  239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1907083232 408 INYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLE 455
Cdd:PRK11634  318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR----LLRNIE 361
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
101-296 1.89e-72

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: 235.29  E-value: 1.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMD---QKELEPGDGPIAVIVCPTRELCQ 177
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 178 QIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17945    81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083232 258 VRSIASHV-----RPD---------------RQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17945   161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
91-435 7.29e-71

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 242.55  E-value: 7.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL---EPGDgPIAV 167
Cdd:PRK04537   10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 168 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEA 246
Cdd:PRK04537   89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 247 DRMFDMGFEYQVRSIASHV--RPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQivEILHSGPSKWNW 324
Cdd:PRK04537  169 DRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ--RIYFPADEEKQT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 404
Cdd:PRK04537  247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1907083232 405 KTVINYDVARDIDTHTHRIGRTGRAGEKGVA 435
Cdd:PRK04537  327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
112-296 3.88e-69

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: 3.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE---LEPGDGPIAVIVCPTRELCQQIHAECKRFGK 188
Cdd:cd17951    12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEGPYGLIVCPSRELARQTHEVIEYYCK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 189 AYN------LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 262
Cdd:cd17951    92 ALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIF 171
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907083232 263 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
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 ...
101-297 8.56e-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: 8.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL-EPGDGPIAVIVCPTRELCQQI 179
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 180 HAECKRFgKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17958    81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17958   160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
101-299 2.85e-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: 215.53  E-value: 2.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---KKGLRALILAPTRELASQIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVygGGSMWEQAKALQE---GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17957    78 RELLKLSKGTGLRIVLL--SKSLEAKAKDGPKsitKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907083232 258 VRSI-ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 299
Cdd:cd17957   156 TDEIlAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
91-296 1.17e-64

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: 214.10  E-value: 1.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgdGPIAVIVC 170
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRM 249
Cdd:cd17954    76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17954   156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
90-296 2.07e-63

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


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 210.62  E-value: 2.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  90 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdqKELEPGDGPIAVIV 169
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:cd17959    78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17959   158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
114-285 6.97e-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: 6.97e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 114 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 193
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 194 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 273
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 1907083232 274 FSATFRKKIEKL 285
Cdd:pfam00270 154 LSATLPRNLEDL 165
PTZ00424 PTZ00424
helicase 45; Provisional
91-443 9.57e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 204.68  E-value: 9.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVC 170
Cdd:PTZ00424   29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQ----ALILA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:PTZ00424  104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRrLV 330
Cdd:PTZ00424  184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD-LY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINY 410
Cdd:PTZ00424  263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907083232 411 DVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 443
Cdd:PTZ00424  343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
80-302 1.39e-58

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: 199.11  E-value: 1.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  80 VSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQ---K 156
Cdd:cd18051    11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 157 ELEPGDG--------PIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV 228
Cdd:cd18051    91 SLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 229 KKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH-VRP---DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 302
Cdd:cd18051   171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
DEXDc smart00487
DEAD-like helicases superfamily;
105-311 4.04e-58

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 196.17  E-value: 4.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  105 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 183
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  184 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 262
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907083232  263 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 311
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
92-293 3.50e-56

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: 190.90  E-value: 3.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKELEPGDGPIAVIVCP 171
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVK---KKATNLQRVSYLVFDEADR 248
Cdd:cd17955    76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
Cdd:cd17955   156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
101-296 1.39e-53

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: 1.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmlihIMDQKELEPGDGPI--AVIVCPTRELCQQ 178
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 179 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17947    77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADE 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907083232 258 VRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17947   157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
308-439 6.04e-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: 179.24  E-value: 6.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 308 VTQIVEILHSGpSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIP 387
Cdd:cd18787     1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 388 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 439
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 ...
101-296 1.40e-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: 180.82  E-value: 1.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIH 180
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAY-NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17962    76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17962   156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
105-296 1.02e-49

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: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 105 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECK 184
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAYNLRSVAVYGGGSMWEQAKALQEgAEIVVCTPGRLIDHVKKK----ATNLQrvsYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17941    84 KVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpgfdTSNLQ---MLVLDEADRILDMGFKETLDA 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17941   160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
97-290 8.40e-49

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: 171.23  E-value: 8.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  97 FDEQLMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTREL 175
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKR---FGKAYNLRSvaVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVK--KKATNLQRVSYLVFDEADRM 249
Cdd:cd17964    81 ALQIAAEAKKllqGLRKLRVQS--AVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907083232 250 FDMGFEYQVRSIASHVRP----DRQTLLFSATFRKKIEKLARDIL 290
Cdd:cd17964   159 LDMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
107-297 4.65e-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: 4.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 107 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKR 185
Cdd:cd17949     8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 186 FGK-AYNLRSVAVYGGgsmwEQAKA----LQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17949    88 LLKpFHWIVPGYLIGG----EKRKSekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 260 SIASHVR-------------PDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17949   164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
105-297 9.71e-47

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 165.06  E-value: 9.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 105 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 184
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAY--NLRSVAVYGGGSMWEQ-AKALQEGAEIVVCTPGRLIDHVKKKAT--NLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17960    85 SFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLN 164
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
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 ...
98-294 1.25e-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: 164.68  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  98 DEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD-GPIAVIVCPTRELC 176
Cdd:cd17961     2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 177 QQIHAE-------CKRFgkaynLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADR 248
Cdd:cd17961    82 QQVSKVleqltayCRKD-----VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 294
Cdd:cd17961   157 VLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
92-296 1.51e-45

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: 161.70  E-value: 1.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKElepgDGPIAVIVCP 171
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKK----DVIQALILVP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd17940    76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17940   156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
101-278 1.83e-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: 162.79  E-value: 1.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE----LEPGDGPIAVIVCPTREL 175
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKK---ATNLQRVSYLVFDEADRMFDM 252
Cdd:cd17946    81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907083232 253 G-FEyQVRSIASHV-------RPDRQTLLFSATF 278
Cdd:cd17946   161 GhFA-ELEKILELLnkdragkKRKRQTFVFSATL 193
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
102-287 5.00e-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: 5.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 102 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 181
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 182 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKA----TNLQrvsYLVFDEADRMFDMGFEYQ 257
Cdd:cd17942    81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907083232 258 VRSIASHVRPDRQTLLFSATFRKKIEKLAR 287
Cdd:cd17942   158 MRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
98-294 6.63e-38

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: 140.02  E-value: 6.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  98 DEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTREL 175
Cdd:cd17963     2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQ----ALCLAPTREL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKRFGK------AYNLRSVAVYGGGSMWEQakalqegaeIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:cd17963    77 ARQIGEVVEKMGKftgvkvALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 250 FDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 294
Cdd:cd17963   148 LDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNAN 193
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
89-296 1.02e-37

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: 139.79  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  89 GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIAVI 168
Cdd:cd17950     1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 169 V-CPTRELCQQIHAECKRFGKaY--NLRSVAVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFD 244
Cdd:cd17950    75 ViCHTRELAFQISNEYERFSK-YmpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 245 EADRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17950   154 ECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
96-296 3.24e-37

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: 138.23  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  96 GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHI-MDQKELEpgdgpiAVIVCPTRE 174
Cdd:cd17939     3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 175 LCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 254
Cdd:cd17939    77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907083232 255 EYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17939   157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
101-300 1.78e-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: 128.64  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQ 178
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 179 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQV 258
Cdd:cd17948    81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 259 RSIASH-----VRPDR--------QTLLFSATFRKKIEKLARDIL-IDPIRVVQGD 300
Cdd:cd17948   161 SHFLRRfplasRRSENtdgldpgtQLVLVSATMPSGVGEVLSKVIdVDSIETVTSD 216
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
92-296 2.69e-33

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: 127.05  E-value: 2.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMdqkelepgdgpiAVIVCP 171
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFgKAY----NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEAD 247
Cdd:cd17938    69 SRELAEQTYNCIENF-KKYldnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 248 RMFDMGFEYQVRSIASH-----VRPDR-QTLLFSATFRK-KIEKLARDILIDPIRV 296
Cdd:cd17938   148 RLLSQGNLETINRIYNRipkitSDGKRlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
92-297 3.31e-33

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: 126.79  E-value: 3.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIwpmlIHIMDQKELEPgDGPIAVIVCP 171
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS----ISILQQIDTSL-KATQALVLAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd18046    76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd18046   156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
320-430 7.66e-32

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: 119.62  E-value: 7.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 320 SKWNWLtRRLVEFTSSGSVLLFV--TKKANAEELasnLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAAR 397
Cdd:pfam00271   1 EKLEAL-LELLKKERGGKVLIFSqtKKTLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907083232 398 GLDIPSIKTVINYDVARDIDTHTHRIGRTGRAG 430
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, ...
101-287 2.01e-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: 121.22  E-value: 2.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDqkeLEPGdGPIAVIVCPTRELCQQIH 180
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17943    76 DVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
                         170       180
                  ....*....|....*....|....*...
gi 1907083232 261 IASHVRPDRQTLLFSATFRKK-IEKLAR 287
Cdd:cd17943   156 IFSSLPKNKQVIAFSATYPKNlDNLLAR 183
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
101-287 6.44e-31

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: 121.20  E-value: 6.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSG---------RDMIGIAKTGSGKTAAFIWPMLihimdQKeLEPGDGPI--AVIV 169
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG--------AEIVVCTPGRLIDHVKKKAT-NLQRVSY 240
Cdd:cd17956    75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 241 LVFDEADRMFDMGFEY---QV-RSIASHVRPDR----------------QTLLFSATFRKKIEKLAR 287
Cdd:cd17956   155 LVIDEADRLLNQSFQDwleTVmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
92-297 6.48e-31

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 120.26  E-value: 6.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCP 171
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQ----ALILSP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd18045    76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd18045   156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
115-277 1.03e-30

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: 119.57  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 115 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKayNLR 193
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 194 SVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS-----HVRPD 268
Cdd:cd17944    93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172

                  ....*....
gi 1907083232 269 RQTLLFSAT 277
Cdd:cd17944   173 PQTLLFSAT 181
HELICc smart00490
helicase superfamily c-terminal domain;
349-430 6.84e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 109.99  E-value: 6.84e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  349 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 428
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1907083232  429 AG 430
Cdd:smart00490  81 AG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
127-425 5.19e-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: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 127 GRDMIGIAKTGSGKTAafiwpMLIHIMDQKelepGDGPIAVIVCPTRELCQQIHAECKRFgkaynLRSVAVYGGgsmweq 206
Cdd:COG1061   100 GGRGLVVAPTGTGKTV-----LALALAAEL----LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG------ 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 207 akALQEGAEIVVCTPGRLIDHVKKKATNlQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRqTLLFSAT--------- 277
Cdd:COG1061   160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgrei 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 278 ---------FRKKIEKLARDILIDPIRVV---------QGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVL 339
Cdd:COG1061   232 llflfdgivYEYSLKEAIEDGYLAPPEYYgirvdltdeRAEYDALSERLRE--ALAADAERKDKILRELLREHPDDRKTL 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 340 LFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVInydVARDIDTH 419
Cdd:COG1061   310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSP 386

                  ....*....
gi 1907083232 420 TH---RIGR 425
Cdd:COG1061   387 REfiqRLGR 395
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
108-297 4.16e-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: 4.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 108 SEYTQPTPIQCQGVPvALSGRDMIGI-----------------AKTGSGKTAAFIWPMLIHIMDQKELEPGDG------- 163
Cdd:cd17965    26 DEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesa 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 164 -----PIAVIVCPTRELCQQIHAECKRFGKA--YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQ 236
Cdd:cd17965   105 kdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILS 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 237 RVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17965   185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
77-293 1.64e-18

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 85.46  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  77 NLRVSGAAPPRP---GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIH 151
Cdd:cd18048     2 RVEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 152 ImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKAYNLRSV--AVYGGgsmwEQAKALQEGAEIVVCTPGRLIDHV- 228
Cdd:cd18048    82 V-DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQViyAIRGN----RPGKGTDIEAQIVIGTPGTVLDWCf 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 229 KKKATNLQRVSYLVFDEADRMFDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
Cdd:cd18048   153 KLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
91-293 1.74e-17

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 81.69  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImdqkelEPG-DGPIAV 167
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnKYPQCL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 168 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEgaEIVVCTPGRLIDH-VKKKATNLQRVSYLVFDEA 246
Cdd:cd18047    76 CLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907083232 247 DRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
Cdd:cd18047   154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
125-436 1.12e-16

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 83.79  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 125 LSGRDMIGIAKTGSGKTA-AFIWpMLIHIMDqkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGgsm 203
Cdd:COG1204    36 LEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 204 WEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA------DRmfdmGFEYQVrsIASHVR---PDRQTLLF 274
Cdd:COG1204   104 YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPTLEV--LLARLRrlnPEAQIVAL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 275 SATFrKKIEKLAR----DILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEE 350
Cdd:COG1204   178 SATI-GNAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLE--EGGQVLVFVSSRRDAES 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 351 LASNLKQE------GHNLGLL-------------------------------HGDMDQSERNKVISDFKKKDIPVLVATD 393
Cdd:COG1204   255 LAKKLADElkrrltPEEREELeelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATP 334
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 394 VAARGLDIPSiKTVINYDVAR----DIDTHTHR--IGRTGRAG--EKGVAY 436
Cdd:COG1204   335 TLAAGVNLPA-RRVIIRDTKRggmvPIPVLEFKqmAGRAGRPGydPYGEAI 384
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
313-444 5.69e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.54  E-value: 5.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 313 EILHSGPSKwnwlTRRLVEFT----SSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGD--------MDQSERNKVISD 380
Cdd:COG1111   331 DIEHPKLSK----LREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILER 406
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 381 FKKKDIPVLVATDVAARGLDIPSIKTVINYD-VA---RDIdthtHRIGRTGRAGEKGVaYTLLTpKDS 444
Cdd:COG1111   407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPseiRSI----QRKGRTGRKREGRV-VVLIA-KGT 468
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
321-443 1.03e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 67.86  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 321 KWNWLTRRLVEFTSsGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGL 399
Cdd:COG0514   217 KLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907083232 400 DIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 443
Cdd:COG0514   295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
134-432 1.38e-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: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHAECKR-FGKAYNLRSVAVYGGGSMWEQAKALQ 211
Cdd:cd09639     6 APTGYGKTeAALLW--ALHSLKSQKADRV-----IIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 212 E-------------GAEIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAshvRPD 268
Cdd:cd09639    79 HlfplyihsndtlfLDPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK---DND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 269 RQTLLFSATFRKKIEKLARDILIDpirvvqgdigEANE-------DVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLF 341
Cdd:cd09639   155 VPILLMSATLPKFLKEYAEKIGYV----------EENEpldlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 342 VTKKANAEELASNLKQEGH--NLGLLHGDMDQSERNK----VISDFKKKDIPVLVATDVAARGLDIPSikTVINYDVArD 415
Cdd:cd09639   225 VNTVDRAQEFYQQLKEKGPeeEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-P 301
                         330
                  ....*....|....*..
gi 1907083232 416 IDTHTHRIGRTGRAGEK 432
Cdd:cd09639   302 IDSLIQRLGRLHRYGEK 318
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
129-426 1.83e-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: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 129 DMigiaktGSGKTA---AFIwpmlihimdQKELEPGDGPIAVIVCPTReLCQQIHAECKRFgkAYNLRSVAVYGGGSMWE 205
Cdd:COG0553   268 DM------GLGKTIqalALL---------LELKERGLARPVLIVAPTS-LVGNWQRELAKF--APGLRVLVLDGTRERAK 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 206 QAKALQEgAEIVVCTpgrlIDHVKKKATNLQRV--SYLVFDEADRMFDMG-FEYQ-VRSIASHVR--------------- 266
Cdd:COG0553   330 GANPFED-ADLVITS----YGLLRRDIELLAAVdwDLVILDEAQHIKNPAtKRAKaVRALKARHRlaltgtpvenrleel 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 267 ------------PDRQTllFSATFRKKIEK--------LAR------------DILID-PIRVVQ--------------- 298
Cdd:COG0553   405 wslldflnpgllGSLKA--FRERFARPIEKgdeealerLRRllrpfllrrtkeDVLKDlPEKTEEtlyveltpeqralye 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 299 -------GDIGEANEDVTQIV----------------------EILHSGPSKWNWLTRRLVEFTSSG-SVLLFVTKKANA 348
Cdd:COG0553   483 avleylrRELEGAEGIRRRGLilaaltrlrqicshpallleegAELSGRSAKLEALLELLEELLAEGeKVLVFSQFTDTL 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 349 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFK-KKDIPV-LVATDVAARGLDIPSIKTVINYD-----------VARd 415
Cdd:COG0553   563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPVfLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR- 641
                         410
                  ....*....|.
gi 1907083232 416 idthTHRIGRT 426
Cdd:COG0553   642 ----AHRIGQT 648
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
134-277 3.28e-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: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKaYNLRSVAVYGGGSMWEQAKALQE 212
Cdd:cd00046     8 APTGSGKTlAALLA--ALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 213 GAEIVVCTPGRLIDHVK-KKATNLQRVSYLVFDEADRM-FDMGFEYQVR-SIASHVRPDRQTLLFSAT 277
Cdd:cd00046    79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALlIDSRGALILDlAVRKAGLKNAQVILLSAT 146
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
136-445 6.90e-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: 6.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKT-AAFIWpMLIHimdqkeLEPGDGPIAVIVCPTRELCQQIHaecKRFGKAYNLrSVAVYGGGSMWEQAKALQEG- 213
Cdd:COG1203   156 TGGGKTeAALLF-ALRL------AAKHGGRRIIYALPFTSIINQTY---DRLRDLFGE-DVLLHHSLADLDLLEEEEEYe 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 214 --------------AEIVVCTPGRLIDHV-------KKKATNLQRvSYLVFDEADrMFDMgfEYQ---VRSIASHVRPDR 269
Cdd:COG1203   225 searwlkllkelwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVIILDEVQ-AYPP--YMLallLRLLEWLKNLGG 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 270 QTLLFSATFRKKIeklaRDILIDPIRVVQGDIGEANEDVTQIVE---ILHSGPSKWNWLTRRLVE-FTSSGSVLLFVTKK 345
Cdd:COG1203   301 SVILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVRkrvELKEGPLSDEELAELILEaLHKGKSVLVIVNTV 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 346 ANAEELASNLKQEGHNLG--LLHGDMDQSERNKVISD----FKKKDIPVLVATDVAARGLDipsiktvINYDVA-RD--- 415
Cdd:COG1203   377 KDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVD-------IDFDVViRDlap 449
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907083232 416 IDTHTHRIGRT---GRAGEKGVAYtLLTPKDSN 445
Cdd:COG1203   450 LDSLIQRAGRCnrhGRKEEEGNVY-VFDPEDEG 481
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
134-432 7.04e-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: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 212
Cdd:TIGR01587   6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 213 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 264
Cdd:TIGR01587  76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 265 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 344
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 417
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308
                         330
                  ....*....|....*
gi 1907083232 418 THTHRIGRTGRAGEK 432
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
136-246 1.47e-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: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKTaaFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQihaECKRFGKAYNLRSVAVYG--GGSMWEQAKALQE 212
Cdd:cd18034    25 TGSGKT--LIAVMLIKEMgELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKWTKERWKEE 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907083232 213 --GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA 246
Cdd:cd18034   100 leKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
312-424 5.35e-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: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 312 VEILHSGpsKWNWLTRRLVEFTSSGS-VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKK-KDIPV- 388
Cdd:cd18793     5 IEEVVSG--KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIRVf 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907083232 389 LVATDVAARGLDIPSIKTVINYDV----ARD---IDtHTHRIG 424
Cdd:cd18793    83 LLSTKAGGVGLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
114-246 5.86e-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: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 114 TPIQCQGV-PVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNL 192
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 193 RSVAVYGGGSMweqAKALQEGAEIVVCTP----GRLIDHvkkKATNLQRVSYLVFDEA 246
Cdd:cd17921    76 NVGLLTGDPSV---NKLLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
85-439 7.38e-10

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: 62.55  E-value: 7.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  85 PPRPGSsFAHF--GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDqkelepGD 162
Cdd:COG1205    28 PAREAR-YAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 163 GPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGGGSMWEQAKALQEGAEIVVCTP-----GrLIDHVKKKATNLQ 236
Cdd:COG1205   101 GATALYLYPTKALARDQLRRLRELAEALGLGvRVATYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFR 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 237 RVSYLVFDEA---------------DRMfdmgfeyqvRSIASHVRPDRQTLLFSATfrkkI---EKLARDILIDPIRVVQ 298
Cdd:COG1205   180 NLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 299 GDiGEAnedvTQIVEILHSGPSKWNWLTRR---------LVEFTSSG-SVLLFVTKKANAEELASNLKQEGHNLGLL--- 365
Cdd:COG1205   247 ED-GSP----RGERTFVLWNPPLVDDGIRRsalaeaarlLADLVREGlRTLVFTRSRRGAELLARYARRALREPDLAdrv 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 366 ---HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 439
Cdd:COG1205   322 aayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
345-470 1.08e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.65  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 424
Cdd:PRK11057  246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907083232 425 RTGRAGEKGVAYTLLTPKDSNFagdLVRNLE----GANQHVSKELLDlAM 470
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 ...
369-439 1.22e-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: 57.37  E-value: 1.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 369 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLL 439
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
325-428 1.34e-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: 57.27  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQ------EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 398
Cdd:cd18796    28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907083232 399 LDIPSIKTVINYDVARDIDTHTHRIGRTGR 428
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 ...
347-441 2.69e-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: 56.51  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 347 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI- 423
Cdd:cd18792    46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125
                          90
                  ....*....|....*...
gi 1907083232 424 GRTGRAGEKGVAYtLLTP 441
Cdd:cd18792   126 GRVGRGKHQSYCY-LLYP 142
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
331-455 4.79e-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: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKQ--EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:cd18810    21 ELLRGGQVFYVHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907083232 409 --NYDVARDIDTHTHRiGRTGRAGEKGVAYtLLTPKDSNFAGDLVRNLE 455
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 ...
388-440 1.43e-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: 1.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 388 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLT 440
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
344-456 1.59e-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: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 344 KKANA--EELASNLKQEgHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTH 421
Cdd:cd18811    45 KAAVAmyEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLH 123
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907083232 422 RI-GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEG 456
Cdd:cd18811   124 QLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
327-431 1.87e-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: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 327 RRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKT 406
Cdd:cd18794    22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101
                          90       100
                  ....*....|....*....|....*
gi 1907083232 407 VINYDVARDIDTHTHRIGRTGRAGE 431
Cdd:cd18794   102 VIHYSLPKSMESYYQESGRAGRDGL 126
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
346-408 4.08e-08

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 56.60  E-value: 4.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 346 ANAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdvaargldipsikTVI 408
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT-------------TVI 539
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
339-440 4.18e-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: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTKKANAEELASNLKQEGHNLGLLHGD---------------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPS 403
Cdd:cd18802    29 IIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907083232 404 IKTVINYDVARDIdthTHRIGRTGRAGEKGVAYTLLT 440
Cdd:cd18802   109 CNLVIRFDLPKTL---RSYIQSRGRARAPNSKYILMV 142
PRK13766 PRK13766
Hef nuclease; Provisional
369-440 4.62e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 56.81  E-value: 4.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 369 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLLT 440
Cdd:PRK13766  407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIA 477
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
107-451 1.19e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 55.49  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 107 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKELEPGDGPIAVI-VCPTRELCQQIHaeck 184
Cdd:COG1201    19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPA-LDELARRPRPGELPDGLRVLyISPLKALANDIE---- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RfgkayNLR-----------------SVAV-YGGGSMWEQAKALQEGAEIVVCTPGRLidHV----KKKATNLQRVSYLV 242
Cdd:COG1201    94 R-----NLRapleeigeaaglplpeiRVGVrTGDTPASERQRQRRRPPHILITTPESL--ALlltsPDARELLRGVRTVI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 243 FDEadrmfdmgfeyqVRSIAS---------------HVRPDR-QTLLFSATFRkKIEKLAR----DILIDPIRVVQGDIG 302
Cdd:COG1201   167 VDE------------IHALAGskrgvhlalslerlrALAPRPlQRIGLSATVG-PLEEVARflvgYEDPRPVTIVDAGAG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 303 -----EANEDVTQIVEILHSGPSKWNWLTRRLVEF-TSSGSVLLFVTKKANAEELASNLKQ----EGHNLGLLHGDMDQS 372
Cdd:COG1201   234 kkpdlEVLVPVEDLIERFPWAGHLWPHLYPRVLDLiEAHRTTLVFTNTRSQAERLFQRLNElnpeDALPIAAHHGSLSRE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 373 ERNKVISDFKKKDIPVLVAT---DVaarGLDIPSIKTVINYD----VARDIdthtHRIGRTG-RAGEKGVAYtlLTPKDs 444
Cdd:COG1201   314 QRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGspksVARLL----QRIGRAGhRVGEVSKGR--LVPTH- 383

                  ....*..
gi 1907083232 445 nfAGDLV 451
Cdd:COG1201   384 --RDELV 388
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
337-408 2.23e-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: 2.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 337 SVLLFVTKKANAEELASNLKQEGHNLGLLHGD--MDQSERNKVISDFK-KKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:cd18799     8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFgELKPPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
331-438 1.12e-06

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: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVI-- 408
Cdd:cd18795    39 TVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPA-RTVIik 113
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907083232 409 -----NYDVARDIDTHTHR--IGRTGRAG--EKGVAYTL 438
Cdd:cd18795   114 gtqryDGKGYRELSPLEYLqmIGRAGRPGfdTRGEAIIM 152
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
347-402 1.45e-06

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 51.69  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 347 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 402
Cdd:PRK10917  491 SAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
136-278 1.74e-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: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKT---AAFIWpmliHIMDQKELepgdgpiavIVCPTRELCQQIHAECKRFGKAynlRSVAVYGGGSmweqaKALQE 212
Cdd:cd17926    27 TGSGKTltaLALIA----YLKELRTL---------IVVPTDALLDQWKERFEDFLGD---SSIGLIGGGK-----KKDFD 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 213 GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRQtLLFSATF 278
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 ...
113-245 2.15e-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: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 113 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEPGDGPIAVIVCPTRELC-QQIHAECKRFGKAYN 191
Cdd:cd18036     3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKGYK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 192 LrsVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATN----LQRVSYLVFDE 245
Cdd:cd18036    81 V--TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
339-432 3.47e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 50.66  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  339 LLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDT 418
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                           90
                   ....*....|....
gi 1907083232  419 HTHRIGRTGRAGEK 432
Cdd:PLN03137   764 YHQECGRAGRDGQR 777
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
127-245 3.78e-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: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 127 GRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKElepgdGPIAVI-VCPTRELCQQIHAECKRFGKAYNL-RSVAV-YGGGS 202
Cdd:cd17922     1 GRNVLIAAPTGSGKTeAAFLPA-LSSLADEPE-----KGVQVLyISPLKALINDQERRLEEPLDEIDLeIPVAVrHGDTS 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907083232 203 MWEQAKALQEGAEIVVCTP---GRLIDHvKKKATNLQRVSYLVFDE 245
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) ...
338-411 5.38e-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: 5.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083232 338 VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD 411
Cdd:cd18790    30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
366-455 1.02e-05

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 49.36  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232  366 HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI-----NYDVARdidTHTHRiGRTGRAGEKGVAYtLLT 440
Cdd:PRK10689   842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieradHFGLAQ---LHQLR-GRVGRSHHQAYAW-LLT 916
                           90
                   ....*....|....*
gi 1907083232  441 PKDSNFAGDLVRNLE 455
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 ...
112-248 1.52e-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: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTaaFIwPMLI--HIMDQKELEPGdGPIAVIVcPTRELC-QQIHAECKRFGK 188
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FV-AVLIceHHLKKFPAGRK-GKVVFLA-NKVPLVeQQKEVFRKHFER 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 189 AYnLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADR 248
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 ...
116-221 5.46e-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: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 116 IQCQGVPVAL-SGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK-RFGKaYNLR 193
Cdd:cd18023     5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
                          90       100
                  ....*....|....*....|....*...
gi 1907083232 194 SVAVYGGGSMWEQAKAlqEGAEIVVCTP 221
Cdd:cd18023    83 CAELTGDTEMDDTFEI--QDADIILTTP 108
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
339-445 5.78e-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: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTK---KANAEELASNLKQEGHNLGLLHgdmdqSERNKVISDFKKKDIPVLVAT----DVAARGLDIP-SIKTVINY 410
Cdd:cd18798    28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFY 102
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907083232 411 DVArdIDTHTHRIGRTGR--AGE--KGVAYTLLTPKDSN 445
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 ...
334-438 8.74e-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: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 334 SSGSVLLFVTKKANAEELASNLKQEGHNLGL-------LHGDMDQSERNKVI---SDFKKKdipVLVATDVAARGLDIPS 403
Cdd:cd18791    42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkllvlpLHSSLPPEEQQRVFeppPPGVRK---VVLATNIAETSITIPG 118
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 404 IKTVI--------NYDVARDIDT-HTHRIG------RTGRAG--EKGVAYTL 438
Cdd:cd18791   119 VVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRL 170
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
133-188 1.47e-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: 1.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 133 IAKTGSGKTAAFIWPMLIHimdqkeLEPGDGpiAVIVCPTRELCQQIHAECKRFGK 188
Cdd:COG3505     5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
123-248 1.51e-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: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 123 VALSGRDMIgIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIaVIVCPTRELCQQiHAEckRFGKAYNL--RSVAVYGG 200
Cdd:cd18035    13 VALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQ-HAE--NLKRVLNIpdKITSLTGE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907083232 201 GSMWEQAKALQEGaEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 248
Cdd:cd18035    82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
PRK01172 PRK01172
ATP-dependent DNA helicase;
246-430 1.96e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 44.87  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 246 ADRMFDMGFEYQ------VRSIASHVRPDRQTLLFSATFRKKIEK---LARDILIDPIRVVQGDIGEANEDVTQIVEILH 316
Cdd:PRK01172  141 ADEIHIIGDEDRgptletVLSSARYVNPDARILALSATVSNANELaqwLNASLIKSNFRPVPLKLGILYRKRLILDGYER 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 317 SGPSKwNWLTRRLVEftSSGSVLLFVTKKANAEELASNLKQE-------------------------GHNLGLLHGDMDQ 371
Cdd:PRK01172  221 SQVDI-NSLIKETVN--DGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnvyddslnemlPHGVAFHHAGLSN 297
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 372 SERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVINYDVARDIDTHT---------HRIGRTGRAG 430
Cdd:PRK01172  298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA-RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
secA PRK12898
preprotein translocase subunit SecA; Reviewed
320-479 2.22e-04

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237253 [Multi-domain]  Cd Length: 656  Bit Score: 44.62  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 320 SKWNWLTRRLVEFTSSGSVLLFVTKK-ANAEELASNLKQEGHNLGLLHGDMDQSErNKVISDFKKKDiPVLVATDVAARG 398
Cdd:PRK12898  457 AKWAAVAARVRELHAQGRPVLVGTRSvAASERLSALLREAGLPHQVLNAKQDAEE-AAIVARAGQRG-RITVATNMAGRG 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 399 LDIPsiktvINYDVARD-----IDTHTHR--------IGRTGRAGEKGVAYTLLTPKD---SNFAGDLVRNLEGANQHVS 462
Cdd:PRK12898  535 TDIK-----LEPGVAARgglhvILTERHDsaridrqlAGRCGRQGDPGSYEAILSLEDdllQSFLGSRGLAIRRMELLGP 609
                         170
                  ....*....|....*..
gi 1907083232 463 KELLDLAMQNAWFRKSR 479
Cdd:PRK12898  610 RGGRALGALLLRRAQRR 626
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
481-726 5.93e-04

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: 43.06  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 481 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSNYeayKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 560
Cdd:cd21118   168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGCTN---PPPSGSHE---------------------SFSNSGGS 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 561 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 640
Cdd:cd21118   221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 641 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 720
Cdd:cd21118   301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358

                  ....*.
gi 1907083232 721 GFNREN 726
Cdd:cd21118   359 PFNFDT 364
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
338-433 7.14e-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: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 338 VLLFVTKKANAEELASNLkqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIktvinyDVARDID 417
Cdd:cd18789    52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA------NVAIQIS 120
                          90       100
                  ....*....|....*....|...
gi 1907083232 418 TH-------THRIGRTGRAGEKG 433
Cdd:cd18789   121 GHggsrrqeAQRLGRILRPKKGG 143
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
129-246 1.07e-03

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: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 129 DMigiaktGSGKTAAfiwpMLIHIMDQKElEPGDGPiAVIVCPTrELCQQIHAECKRFgkAYNLRSVAVYGGGSMWEQAK 208
Cdd:cd18012    31 DM------GLGKTLQ----TLALLLSRKE-EGRKGP-SLVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLR 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907083232 209 ALqEGAEIVVCTPG---RLIDHVKKkatnlQRVSYLVFDEA 246
Cdd:cd18012    96 AL-EDYDLVITSYGllrRDIELLKE-----VKFHYLVLDEA 130
ResIII pfam04851
Type III restriction enzyme, res subunit;
136-278 1.15e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.35  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKTAafiwpMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSvAVYGGGSMweqaKALQEGAE 215
Cdd:pfam04851  32 TGSGKTL-----TAAKLIARL-FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIG-EIISGDKK----DESVDDNK 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 216 IVVCTP---GRLIDHVKKKATNLQRVsYLVFDEADRMFDMGFeyqvRSIASHVRPdrQTLL-FSATF 278
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 ...
124-246 1.86e-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: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 124 ALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGG-G 201
Cdd:cd17923    12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATYDGdT 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907083232 202 SMWEQAKALQEGAEIVVCTPGRL----IDHVKKKATNLQRVSYLVFDEA 246
Cdd:cd17923    86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
115-246 5.05e-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: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 115 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdQKELEPGdgpIAVIVCPTRELCQ-QIHAeCKRFGKAYNLR 193
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQVDA-LPRAIKAAALN 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 194 SVAvyGGGSMWEQAKALQEG-AEIVVCTPGRLID-HVKKKATNLQRVSYLVFDEA 246
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 ...
110-246 6.66e-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: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 110 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdqkelepgDGPIAVIVCPTRELCQ-QIHaECKRFGK 188
Cdd:cd17920    10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-RLQQLGI 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 189 aynlRSVAVYGGGSMWEQAKALQEGAE----IVVCTPGRLI-DHVKK---KATNLQRVSYLVFDEA 246
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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