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Conserved domains on  [gi|528490122|ref|XP_005167777|]
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ATP-dependent RNA helicase DDX3X isoform X14 [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
187-442 0e+00

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: 578.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 187 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 266
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 267 SQIYSEGPGEALQatkastqQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLE 346
Cdd:cd18051   81 SQIYEQGPGESLP-------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 347 RGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILAR 426
Cdd:cd18051  154 RGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLAR 233
                        250
                 ....*....|....*.
gi 528490122 427 DFLEEYIFLAVGRVGS 442
Cdd:cd18051  234 DFLDNYIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-577 2.95e-60

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: 198.12  E-value: 2.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 447 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528490122 527 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 577
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
187-442 0e+00

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: 578.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 187 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 266
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 267 SQIYSEGPGEALQatkastqQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLE 346
Cdd:cd18051   81 SQIYEQGPGESLP-------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 347 RGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILAR 426
Cdd:cd18051  154 RGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLAR 233
                        250
                 ....*....|....*.
gi 528490122 427 DFLEEYIFLAVGRVGS 442
Cdd:cd18051  234 DFLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
208-649 1.63e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 489.27  E-value: 1.63e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIySEGPGEALQAtkastqq 287
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-DPSRPRAPQA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:COG0513   75 --------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 368 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENI 447
Cdd:COG0513  141 LDLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETI 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 448 TQKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIM 527
Cdd:COG0513  217 EQRYYLVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 528 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKD---LLDILVEaKQEVPSWLE 604
Cdd:COG0513  296 VATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekLIGQKIE-EEELPGFEP 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 528490122 605 NLAYEHQH-KSTNRGRPKRFSGGFGARDYRQMPGGGNTfGNRGARN 649
Cdd:COG0513  375 VEEKRLERlKPKIKEKLKGKKAGRGGRPGPKGERKARR-GKRRRRK 419
PTZ00110 PTZ00110
helicase; Provisional
89-640 6.38e-134

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 405.31  E-value: 6.38e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  89 HNAGYGTYENKDGGWNSVVNRDAYASFGGRSDRGKSAFFNDRGASSRGRY---ERGGFGGGTGGNSRWVEESRD---EED 162
Cdd:PTZ00110   1 MRSTDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPgygNYSGGYGGFGMNSYGSSTLGKrlqPID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 163 WSK----PMPPNERLEHELFSASNTginfEKYDDIPVE-----ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPV 233
Cdd:PTZ00110  81 WKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 234 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqqengKYVRRKQYPISLVLAPTRELALQ 313
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQ------------------PLLRYGDGPIVLVLAPTRELAEQ 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 314 IYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQI 393
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQI 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 394 RRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATG 471
Cdd:PTZ00110 299 RKIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIM 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 472 KD-SLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDL 550
Cdd:PTZ00110 375 RDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDF 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 551 PSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILVEAKQEVPSWLENLAYEHqhkSTNRGRPKRFSGGFGAR 630
Cdd:PTZ00110 455 PNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---SNGTERRRWGGYGRFSN 531
                        570
                 ....*....|
gi 528490122 631 DYRQMPGGGN 640
Cdd:PTZ00110 532 NVNNIPLGGS 541
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-577 2.95e-60

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: 198.12  E-value: 2.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 447 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528490122 527 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 577
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
231-424 6.96e-60

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: 198.62  E-value: 6.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  231 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqqengkyvrrkqyPISLVLAPTREL 310
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG-----------------------PQALVLAPTREL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  311 ALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCKYLVLDEADRMLDMGFE 390
Cdd:pfam00270  58 AEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190
                  ....*....|....*....|....*....|....
gi 528490122  391 PQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQIL 424
Cdd:pfam00270 136 PDLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
222-450 1.14e-54

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 185.77  E-value: 1.14e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   222 ITLSRYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgealqatkastqqengKYVRRKQYPI 300
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL------------------------EALKRGKGGR 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   301 SLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCKYLVLD 379
Cdd:smart00487  57 VLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILD 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528490122   380 EADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRvgSTSENITQK 450
Cdd:smart00487 137 EAHRLLDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
458-568 1.60e-37

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: 135.42  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  458 DKRSFLLDLLNaTGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGL 537
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 528490122  538 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 568
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
487-568 4.61e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 110.38  E-value: 4.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   487 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 566
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 528490122   567 VG 568
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
336-578 3.85e-22

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 100.22  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 336 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdyckyLVLDEA--------DrmldmgFEP---QIRRIVE 398
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 399 QDTMPPkgsrqTMMFSATFPKEIQ--ILARDFLEE-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLNATGKDS 474
Cdd:COG0514  163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGS 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 475 lTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATaVA-ARGLDISNVKHVINFDLPSD 553
Cdd:COG0514  233 -GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKS 310
                        250       260
                 ....*....|....*....|....*
gi 528490122 554 IEEYVHRIGRTGRVGNLGLATSFYN 578
Cdd:COG0514  311 IEAYYQEIGRAGRDGLPAEALLLYG 335
PRK13766 PRK13766
Hef nuclease; Provisional
455-566 3.08e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.35  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 455 EENDKRSFLLDLLNAT---GKDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGR 523
Cdd:PRK13766 344 IEHPKLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGE 423
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528490122 524 CPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 566
Cdd:PRK13766 424 FNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
411-568 5.81e-03

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: 39.36  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  411 MMFSATFPKEIQILARDFleEYIFLAVGRVGSTSENITQKVVWVEENDKR---SFLLDLLNATGKDSLTLVFVETKKGAD 487
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILIESDKVgeiSSLERLLEFIKKGGSIAIIVNTVDRAQ 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  488 ALEDFLYREGYACTSI--HGDRSQRDRE----EALHQFRSGRCP-IMVATAVAARGLDISnvkhvinFDL----PSDIEE 556
Cdd:TIGR01587 237 EFYQQLKEKAPEEEIIlyHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLDIS-------ADVmiteLAPIDS 309
                         170
                  ....*....|..
gi 528490122  557 YVHRIGRTGRVG 568
Cdd:TIGR01587 310 LIQRLGRLHRYG 321
 
Name Accession Description Interval E-value
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
187-442 0e+00

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: 578.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 187 FEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVL 266
Cdd:cd18051    1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 267 SQIYSEGPGEALQatkastqQENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLE 346
Cdd:cd18051   81 SQIYEQGPGESLP-------SESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 347 RGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILAR 426
Cdd:cd18051  154 RGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLAR 233
                        250
                 ....*....|....*.
gi 528490122 427 DFLEEYIFLAVGRVGS 442
Cdd:cd18051  234 DFLDNYIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
208-649 1.63e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 489.27  E-value: 1.63e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIySEGPGEALQAtkastqq 287
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-DPSRPRAPQA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:COG0513   75 --------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 368 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENI 447
Cdd:COG0513  141 LDLSGVETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETI 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 448 TQKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIM 527
Cdd:COG0513  217 EQRYYLVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 528 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKD---LLDILVEaKQEVPSWLE 604
Cdd:COG0513  296 VATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAiekLIGQKIE-EEELPGFEP 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 528490122 605 NLAYEHQH-KSTNRGRPKRFSGGFGARDYRQMPGGGNTfGNRGARN 649
Cdd:COG0513  375 VEEKRLERlKPKIKEKLKGKKAGRGGRPGPKGERKARR-GKRRRRK 419
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
208-441 5.11e-157

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: 451.94  E-value: 5.11e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPgealqatkastqq 287
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 ENGKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:cd17967   68 PSVGRGRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGR 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528490122 368 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVG 441
Cdd:cd17967  148 ISLSSIKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
166-441 4.62e-150

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: 435.94  E-value: 4.62e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 166 PMPPNErlEHELFSASNTGINFEKYDDIPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKR 245
Cdd:cd18052    4 PPPPED--EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 246 DLMACAQTGSGKTAAFLLPVLSQIYSEGpgeaLQATKASTQQEngkyvrrkqyPISLVLAPTRELALQIYDEARKFAYRS 325
Cdd:cd18052   82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSEVQE----------PQALIVAPTRELANQIFLEARKFSYGT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 326 RVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPK 405
Cdd:cd18052  148 CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSK 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 528490122 406 GSRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG 441
Cdd:cd18052  228 EDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
89-640 6.38e-134

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 405.31  E-value: 6.38e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  89 HNAGYGTYENKDGGWNSVVNRDAYASFGGRSDRGKSAFFNDRGASSRGRY---ERGGFGGGTGGNSRWVEESRD---EED 162
Cdd:PTZ00110   1 MRSTDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPgygNYSGGYGGFGMNSYGSSTLGKrlqPID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 163 WSK----PMPPNERLEHELFSASNTginfEKYDDIPVE-----ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPV 233
Cdd:PTZ00110  81 WKSinlvPFEKNFYKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 234 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqqengKYVRRKQYPISLVLAPTRELALQ 313
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQ------------------PLLRYGDGPIVLVLAPTRELAEQ 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 314 IYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQI 393
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQI 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 394 RRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFL-EEYIFLAVGRVG-STSENITQKVVWVEENDKRSFLLDLLNATG 471
Cdd:PTZ00110 299 RKIVSQ----IRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIM 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 472 KD-SLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDL 550
Cdd:PTZ00110 375 RDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDF 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 551 PSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILVEAKQEVPSWLENLAYEHqhkSTNRGRPKRFSGGFGAR 630
Cdd:PTZ00110 455 PNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER---SNGTERRRWGGYGRFSN 531
                        570
                 ....*....|
gi 528490122 631 DYRQMPGGGN 640
Cdd:PTZ00110 532 NVNNIPLGGS 541
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
227-580 1.99e-101

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 318.28  E-value: 1.99e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgeaLQATKASTQqengkyvrrkqypiSLVLAP 306
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQK---------LDVKRFRVQ--------------ALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFAyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLD 379
Cdd:PRK11776  81 TRELADQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 380 EADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYifLAVgRVGSTSEN--ITQKVVWVEEN 457
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 458 DKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGL 537
Cdd:PRK11776 228 ERLPALQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGL 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 528490122 538 DISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDK 580
Cdd:PRK11776 307 DIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
227-648 5.41e-94

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 298.65  E-value: 5.41e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkaSTQQENGKYVRrkqyPI-SLVLA 305
Cdd:PRK10590  21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHL--------------ITRQPHAKGRR----PVrALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRML 385
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 386 DMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEENDKRSfLLD 465
Cdd:PRK10590 163 DMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRE-LLS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 466 LLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHV 545
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 546 INFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNITKDLLDILveaKQEVPSwLENLAYEH----QHKSTNRGRPK 621
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIPR-IAIPGYEPdpsiKAEPIQNGRQQ 393
                        410       420
                 ....*....|....*....|....*..
gi 528490122 622 RFSGGFGARDYRQMPGGGNTFGNRGAR 648
Cdd:PRK10590 394 RGGGGRGQGGGRGQQQGQPRRGEGGAK 420
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
193-622 2.80e-92

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 296.31  E-value: 2.80e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 193 IPVEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLS---QI 269
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 270 YSEGPGEalqatkastqqengkyvRRKqyPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGC 349
Cdd:PLN00206 187 RSGHPSE-----------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGV 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 350 HLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgsrQTMMFSATFPKEIQILARDFL 429
Cdd:PLN00206 248 ELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLA 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 430 EEYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLnaTGKDSLT---LVFVETKKGADALEDFLYR-EGYACTSIHG 505
Cdd:PLN00206 323 KDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAITVvTGLKALSIHG 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 506 DRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSNIT 585
Cdd:PLN00206 401 EKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 528490122 586 KDLLDILVEAKQEVPSWLENLAYEHQHKSTNRGRPKR 622
Cdd:PLN00206 481 PELVALLKSSGAAIPRELANSRYLGSGRKRKKKRRYG 517
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
218-435 3.85e-92

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: 284.33  E-value: 3.85e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPgealqatkastqqengkyvRRKQ 297
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-------------------KKGR 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 298 YPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLV 377
Cdd:cd00268   62 GPQALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLV 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528490122 378 LDEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFL 435
Cdd:cd00268  142 LDEADRMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
209-582 2.41e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 289.89  E-value: 2.41e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 209 FHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgeaLQATKASTQQE 288
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ---------LLQTPPPKERY 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 289 NGKyvrrkqyPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGK 367
Cdd:PRK01297 160 MGE-------PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGE 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 368 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENI 447
Cdd:PRK01297 233 VHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTV 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 448 TQKVVWVEENDKRSFLLDLLNATGKDSLtLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIM 527
Cdd:PRK01297 311 EQHVYAVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVL 389
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528490122 528 VATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNS 582
Cdd:PRK01297 390 VATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
218-435 1.47e-84

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: 264.62  E-value: 1.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkaSTQQengkYVRRKQ 297
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI--------------NAQP----PLERGD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 298 YPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLV 377
Cdd:cd17966   63 GPIVLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLV 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528490122 378 LDEADRMLDMGFEPQIRRIVEQdTMPpkgSRQTMMFSATFPKEIQILARDFLEEYIFL 435
Cdd:cd17966  143 LDEADRMLDMGFEPQIRKIVDQ-IRP---DRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
208-601 6.17e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 273.36  E-value: 6.17e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgPGEAlqatkastqq 287
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:PRK04537  79 -----DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 368 I-GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSEN 446
Cdd:PRK04537 154 VvSLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 447 ITQKVVWVEENDKRSFLLDLLNATgKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 526
Cdd:PRK04537 232 VRQRIYFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEI 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528490122 527 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDKNSnitKDLLDILVEAKQEVPS 601
Cdd:PRK04537 311 LVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYA---MSLPDIEAYIEQKIPV 382
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
227-576 1.41e-80

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 262.96  E-value: 1.41e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqatkastqqengkYVRRKQYPIS-LVLA 305
Cdd:PRK11192  21 YTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD--------------------FPRRKSGPPRiLILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRML 385
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 386 DMGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKE-IQILARDFLEEYIFLAVGrvGSTSE--NITQkvvWVEEND---- 458
Cdd:PRK11192 161 DMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQ---WYYRADdleh 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 459 KRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLD 538
Cdd:PRK11192 232 KTALLCHLLKQPEVTR-SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 528490122 539 ISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 576
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
231-576 5.25e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 250.27  E-value: 5.25e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 231 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqatkasTQQENGkyvRRKQYPISLVLAPTREL 310
Cdd:PRK04837  32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS-------------HPAPED---RKVNQPRALIMAPTREL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 311 ALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFE 390
Cdd:PRK04837  96 AVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 391 PQIRRIVEQdtMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEENDKRSFLLDLLNAT 470
Cdd:PRK04837 176 KDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 471 GKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDL 550
Cdd:PRK04837 254 WPDR-AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332
                        330       340
                 ....*....|....*....|....*.
gi 528490122 551 PSDIEEYVHRIGRTGRVGNLGLATSF 576
Cdd:PRK04837 333 PDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
195-438 1.00e-70

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: 229.90  E-value: 1.00e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 195 VEATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgp 274
Cdd:cd18049   12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 275 gealqatkastqqengKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA 354
Cdd:cd18049   90 ----------------PFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 355 TPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFLEEYIF 434
Cdd:cd18049  154 TPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLKDYIH 229

                 ....
gi 528490122 435 LAVG 438
Cdd:cd18049  230 INIG 233
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
208-580 1.59e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 238.98  E-value: 1.59e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeaLQAtkastqq 287
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyvrrkqyPISLVLAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERG 366
Cdd:PRK11634  75 -----------PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 367 KIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPpkGSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSEN 446
Cdd:PRK11634 144 TLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 447 ITQKVVWVEENDKRSFLLDLLNATGKDSlTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 526
Cdd:PRK11634 220 ISQSYWTVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDI 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528490122 527 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYNDK 580
Cdd:PRK11634 299 LIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENR 352
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
199-438 2.10e-69

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: 227.97  E-value: 2.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 199 GTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeal 278
Cdd:cd18050   54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ------ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 279 qatkastqqengKYVRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGR 358
Cdd:cd18050  128 ------------PYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGR 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 359 LVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGSRQTMMFSATFPKEIQILARDFLEEYIFLAVG 438
Cdd:cd18050  196 LIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
197-429 1.48e-68

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: 223.79  E-value: 1.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 197 ATGTNSPGHIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGE 276
Cdd:cd17953    2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 277 AlqatkastqqENGkyvrrkqyPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATP 356
Cdd:cd17953   82 P----------GEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTP 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528490122 357 GRLVDM--MERGKI-GLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPkgSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17953  144 GRMIDIltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRP--DRQTVLFSATFPRKVEALARKVL 215
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
218-433 2.10e-68

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: 222.29  E-value: 2.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastqqengKYVRRKQ 297
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ------------------RELEKGE 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 298 YPISLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLV 377
Cdd:cd17952   63 GPIAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLV 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528490122 378 LDEADRMLDMGFEPQIRRIVEQdTMPpkgSRQTMMFSATFPKEIQILARDFLEEYI 433
Cdd:cd17952  143 LDEADRMFDMGFEYQVRSIVGH-VRP---DRQTLLFSATFKKKIEQLARDILSDPI 194
PTZ00424 PTZ00424
helicase 45; Provisional
167-588 7.09e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 217.39  E-value: 7.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 167 MPPNERLEHELFSASNTGINfEKYDDIpveatgtnspghIESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRD 246
Cdd:PTZ00424   1 MATSEQKNQSEQVASTGTIE-SNYDEI------------VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 247 LMACAQTGSGKTAAFLLPVLSQI-YSegpgeaLQATKAstqqengkyvrrkqypisLVLAPTRELALQIYDEARKFAYRS 325
Cdd:PTZ00424  68 TIGQAQSGTGKTATFVIAALQLIdYD------LNACQA------------------LILAPTRELAQQIQKVVLALGDYL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 326 RVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPk 405
Cdd:PTZ00424 124 KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP- 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 406 gSRQTMMFSATFPKEIQILARDFLEEYIFLAVGRVGSTSENITQKVVWVEEND-KRSFLLDLLnatgkDSLTLV----FV 480
Cdd:PTZ00424 201 -DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLY-----ETLTITqaiiYC 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 481 ETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHR 560
Cdd:PTZ00424 275 NTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHR 354
                        410       420
                 ....*....|....*....|....*...
gi 528490122 561 IGRTGRVGNLGLATSFYNDKNSNITKDL 588
Cdd:PTZ00424 355 IGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
226-429 9.68e-64

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: 211.02  E-value: 9.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 226 RYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGEalqatkastqqengkYVRRKQYPISLVLA 305
Cdd:cd17945    9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLD---------------EETKDDGPYALILA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRML 385
Cdd:cd17945   74 PTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528490122 386 DMGFEPQIRRIVeqDTMPP------------------KGSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17945  154 DMGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
447-577 2.95e-60

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: 198.12  E-value: 2.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 447 ITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPI 526
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528490122 527 MVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 577
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
231-424 6.96e-60

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: 198.62  E-value: 6.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  231 TPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqqengkyvrrkqyPISLVLAPTREL 310
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG-----------------------PQALVLAPTREL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  311 ALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDYCKYLVLDEADRMLDMGFE 390
Cdd:pfam00270  58 AEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFG 135
                         170       180       190
                  ....*....|....*....|....*....|....
gi 528490122  391 PQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQIL 424
Cdd:pfam00270 136 PDLEEILRR--LPKK--RQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
222-426 2.46e-59

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: 198.58  E-value: 2.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 222 ITLSRYTRPTPVQKYAI-PIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKAstqqengkyvRRKQYPI 300
Cdd:cd17964    9 LTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAI---------QSLLNTKP----------AGRRSGV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 301 S-LVLAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDYCKY 375
Cdd:cd17964   70 SaLIISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDY 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528490122 376 LVLDEADRMLDMGFEPQIRRIVeqDTMPPKGS--RQTMMFSATFPKEIQILAR 426
Cdd:cd17964  150 LVLDEADRLLDMGFRPDLEQIL--RHLPEKNAdpRQTLLFSATVPDEVQQIAR 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
227-426 7.70e-58

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: 194.01  E-value: 7.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKastqqengkyvRRKQYPISLVLAP 306
Cdd:cd17947   10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL---------ERLLYRP-----------KKKAATRVLVLVP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDEADRML 385
Cdd:cd17947   70 TRELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRML 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528490122 386 DMGFEPQIRRIVEqdtMPPKgSRQTMMFSATFPKEIQILAR 426
Cdd:cd17947  150 EEGFADELKEILR---LCPR-TRQTMLFSATMTDEVKDLAK 186
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
218-431 8.90e-57

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: 191.52  E-value: 8.90e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgeaLQATKASTQQENGkyvrrkq 297
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIH---------LDLQPIPREQRNG------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 298 yPISLVLAPTRELALQIYDEARKFAYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLV 377
Cdd:cd17958   65 -PGVLVLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLV 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528490122 378 LDEADRMLDMGFEPQIRRIVeQDTMPpkgSRQTMMFSATFPKEIQILARDFLEE 431
Cdd:cd17958  143 LDEADRMLDMGFEPQIRKIL-LDIRP---DRQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
229-429 9.81e-56

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: 189.09  E-value: 9.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 229 RPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQiysegpgealqatkaSTQQENGKYVRRKQYPISLVLAPTR 308
Cdd:cd17951   12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMF---------------ALEQEKKLPFIKGEGPYGLIVCPSR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 309 ELALQIYDEARKFAYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEAD 382
Cdd:cd17951   77 ELARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEAD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528490122 383 RMLDMGFEPQIRRIVEQDtmppKGSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17951  157 RMIDMGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEXDc smart00487
DEAD-like helicases superfamily;
222-450 1.14e-54

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 185.77  E-value: 1.14e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   222 ITLSRYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgealqatkastqqengKYVRRKQYPI 300
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL------------------------EALKRGKGGR 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   301 SLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDYCKYLVLD 379
Cdd:smart00487  57 VLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILD 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528490122   380 EADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAVGRvgSTSENITQK 450
Cdd:smart00487 137 EAHRLLDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
218-438 7.11e-54

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: 183.56  E-value: 7.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsegpgealqatkastQQENGKYVRrkq 297
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG---------------KPRKKKGLR--- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 298 ypiSLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYL 376
Cdd:cd17957   63 ---ALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYL 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528490122 377 VLDEADRMLDMGFEPQIRRIVEQDTMPPKgsrQTMMFSATFPKEIQILARDFLEEYIFLAVG 438
Cdd:cd17957  140 VLDEADKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
227-434 5.08e-52

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: 178.96  E-value: 5.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSEGPgealqatkastqqengkyvrrkqYPI-SLVLA 305
Cdd:cd17955   19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-QRLSEDP-----------------------YGIfALVLT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDYCKYLVLDEAD 382
Cdd:cd17955   75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEAD 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528490122 383 RMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIF 434
Cdd:cd17955  155 RLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
223-435 1.08e-50

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: 175.47  E-value: 1.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 223 TLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqQENGKYVRRKQYPISL 302
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL-----------------LSLEPRVDRSDGTLAL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 303 VLAPTRELALQIYDEARKFAYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDE 380
Cdd:cd17949   70 VLVPTRELALQIYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528490122 381 ADRMLDMGFEPQIRRIVE---------QDTMPPKGSRQTMMFSATFPKEIQILARDFLEEYIFL 435
Cdd:cd17949  150 ADRLLDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
209-433 4.39e-50

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: 173.25  E-value: 4.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 209 FHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGeaLQAtkastqqe 288
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV--IQA-------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 289 ngkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI 368
Cdd:cd17940   71 -------------LILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVA 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528490122 369 GLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgsRQTMMFSATFPKEIQilarDFLEEYI 433
Cdd:cd17940  138 DLSHCKTLVLDEADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
227-426 1.09e-49

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: 172.50  E-value: 1.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqqengkyVRRKQYPISLVLAP 306
Cdd:cd17954   20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL-----------------------LENPQRFFALVLAP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDYCKYLVLDEADRML 385
Cdd:cd17954   77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528490122 386 DMGFEPQIRRIVEqdTMPPKgsRQTMMFSATFPKEIQILAR 426
Cdd:cd17954  157 NMDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
208-435 4.27e-48

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: 168.25  E-value: 4.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsqiysegpgEALQATKASTQq 287
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI---------EKLKAHSPTVG- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyVRrkqypiSLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK 367
Cdd:cd17959   72 -----AR------ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528490122 368 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDFLEEYIFL 435
Cdd:cd17959  141 LKLSSVEYVVFDEADRLFEMGFAEQLHEILSR--LPE--NRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
227-429 4.71e-46

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: 162.36  E-value: 4.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsegpgealqatkastqqeNGKYVRRKQYPISLVLAP 306
Cdd:cd17960   10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL------------------KRKANLKKGQVGALIISP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFA--YRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDY--CKYLVLDEA 381
Cdd:cd17960   72 TRELATQIYEVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528490122 382 DRMLDMGFEPQIRRIVEQdtmPPKgSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17960  152 DRLLDLGFEADLNRILSK---LPK-QRRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
225-437 6.58e-46

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: 162.07  E-value: 6.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 225 SRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSE--GPGEALQAtkastqqengkyvrrkqypisL 302
Cdd:cd17941    8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwTPEDGLGA---------------------L 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 303 VLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDY--CKYLVL 378
Cdd:cd17941   67 IISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528490122 379 DEADRMLDMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEEYIFLAV 437
Cdd:cd17941  143 DEADRILDMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
221-433 3.21e-44

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: 156.94  E-value: 3.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 221 NITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSqiysegpgealqatKASTQQENgkyvrrkqyPI 300
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII--------------RCLTEHRN---------PS 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 301 SLVLAPTRELALQIYDEARKFAY-RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLD 379
Cdd:cd17962   61 ALILTPTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVD 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528490122 380 EADRMLDMGFEPQIRRIVEQDTMPPkgsrQTMMFSATFPKEIQILARDFLEEYI 433
Cdd:cd17962  141 EADTMLKMGFQQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
214-416 4.19e-44

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: 157.10  E-value: 4.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 214 MGEIIMGnITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSegpgealqatkastqqengkyv 293
Cdd:cd17938    7 MPELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV---------------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 294 rrkqypiSLVLAPTRELALQIYDEARKFAY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 370
Cdd:cd17938   63 -------ALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDL 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528490122 371 DYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGSR----QTMMFSAT 416
Cdd:cd17938  136 SSVRFFVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
226-422 1.10e-41

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


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 151.62  E-value: 1.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 226 RYTRPTPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgealqatkastQQENGKYVRRKqYPISLVL 304
Cdd:cd17946    9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ-------------KSSNGVGGKQK-PLRALIL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 305 APTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DYCKYLVLDEA 381
Cdd:cd17946   75 TPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528490122 382 DRMLDMG-FEP--QIRRIVEQDTMPPKGSRQTMMFSATFPKEIQ 422
Cdd:cd17946  155 DRMLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQ 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
227-426 2.60e-41

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: 149.05  E-value: 2.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsegpgealqatKASTQQENGKYVrrkqypisLVLAP 306
Cdd:cd17942   10 FTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLY-----------KLKFKPRNGTGV--------IIISP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKF-AYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiGLDY--CKYLVLDEADR 383
Cdd:cd17942   71 TRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK-GFLYknLQCLIIDEADR 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528490122 384 MLDMGFEPQIRRIVEqdtMPPKgSRQTMMFSATFPKEIQILAR 426
Cdd:cd17942  149 ILEIGFEEEMRQIIK---LLPK-RRQTMLFSATQTRKVEDLAR 187
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
227-433 1.24e-39

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: 144.26  E-value: 1.24e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqqengkyVRRKQYPISLVL 304
Cdd:cd17963   14 FNKPSKIQETALPLIlsDPPENLIAQSQSGTGKTAAFVLAMLSRV-----------------------DPTLKSPQALCL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 305 APTRELALQIYDEARKFA------YRSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDYCKYLVL 378
Cdd:cd17963   71 APTRELARQIGEVVEKMGkftgvkVALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528490122 379 DEADRMLDM-GFEPQIRRIveQDTMPPkgSRQTMMFSATFPKEIqilaRDFLEEYI 433
Cdd:cd17963  142 DEADVMLDTqGHGDQSIRI--KRMLPR--NCQILLFSATFPDSV----RKFAEKIA 189
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
227-429 2.06e-39

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: 144.00  E-value: 2.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAI-PIIKtKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqaTKASTQqengkyvrrkqypiSLVLA 305
Cdd:cd17939   17 FEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDT---------TVRETQ--------------ALVLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYD--EARKFAYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADR 383
Cdd:cd17939   73 PTRELAQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADE 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528490122 384 MLDMGFEPQIRRIVEQdtMPPKGsrQTMMFSATFPKEIQILARDFL 429
Cdd:cd17939  151 MLSRGFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFM 192
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
458-568 1.60e-37

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: 135.42  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  458 DKRSFLLDLLNaTGKDSLTLVFVETKKGADAlEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGL 537
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 528490122  538 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 568
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
227-429 7.62e-37

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: 136.94  E-value: 7.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgeaLQATKAStqqengkyvRRKQYPISLVLAP 306
Cdd:cd17961   14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAES---------GEEQGTRALILVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFAY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DYCKYLVLDEAD 382
Cdd:cd17961   77 TRELAQQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEAD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528490122 383 RMLDMGFEPQIRRIVEqdtMPPKGSrQTMMFSATFPKEIQILARDFL 429
Cdd:cd17961  156 LVLSYGYEEDLKSLLS---YLPKNY-QTFLMSATLSEDVEALKKLVL 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
209-433 9.77e-37

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: 136.42  E-value: 9.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 209 FHDVDMGEIIMGNITLSRYTRPTPVQKYAI-PIIKtKRDLMACAQTGSGKTAAFLLPVLSQIYSEgpgeaLQATKAstqq 287
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIK-GYDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQA---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyvrrkqypisLVLAPTRELALQIYD--EARKFAYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMER 365
Cdd:cd18046   71 --------------LVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINR 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528490122 366 GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDFLEEYI 433
Cdd:cd18046  135 RYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPP--DTQVVLLSATMPNDVLEVTTKFMRDPI 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
208-429 1.07e-35

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


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 134.01  E-value: 1.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 208 SFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatKASTQQ 287
Cdd:cd17950    3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------------EPVDGQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 288 engkyvrrkqypIS-LVLAPTRELALQIYDEARKFA-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMME 364
Cdd:cd17950   71 ------------VSvLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 365 RGKIGLDYCKYLVLDEADRM---LDMgfepqiRRIVeQD--TMPPKgSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17950  139 EKKLKLSHVKHFVLDECDKMleqLDM------RRDV-QEifRATPH-DKQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
227-434 2.50e-35

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: 132.39  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPvlsqiysegpgeALQATKASTQQengkyvrrkqyPISLVLAP 306
Cdd:cd17943   10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVI------------ALESLDLERRH-----------PQVLILAP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 307 TRELALQIYDEARKFA-YRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRML 385
Cdd:cd17943   67 TREIAVQIHDVFKKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLM 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528490122 386 DMGFEPQIRRIveqDTMPPKgSRQTMMFSATFPKE-IQILARdFLEEYIF 434
Cdd:cd17943  146 EGSFQKDVNWI---FSSLPK-NKQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
227-431 1.06e-31

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 122.19  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 227 YTRPTPVQKYAI-PIIKTkRDLMACAQTGSGKTAAFLLPVLSqiysegpgeALQATKASTQqengkyvrrkqypiSLVLA 305
Cdd:cd18045   19 FEKPSAIQQRAIkPIIKG-RDVIAQSQSGTGKTATFSISVLQ---------CLDIQVRETQ--------------ALILS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 306 PTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRML 385
Cdd:cd18045   75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528490122 386 DMGFEPQIRRIVEQdtMPPKgsRQTMMFSATFPKEIQILARDFLEE 431
Cdd:cd18045  155 NKGFKEQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
232-429 3.32e-31

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 120.72  E-value: 3.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 232 PVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqQENGKYVRRKQYPISLVLAPTRELA 311
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL-----------------QEDQQPRKRGRAPKVLVLAPTRELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 312 LQIYDEARKFAYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRMLDMGFEP 391
Cdd:cd17944   78 NQVTKDFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAE 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528490122 392 QIRRIV-EQDTMPPKGSRQTMMFSATFPKEIQILARDFL 429
Cdd:cd17944  156 QVEEILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
223-426 3.69e-29

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: 115.93  E-value: 3.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 223 TLSRY--TRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgeaLQATKASTQQENGkyvrrkqyPI 300
Cdd:cd17948    4 ILQRQgiTKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRL--------LRYKLLAEGPFNA--------PR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 301 SLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDYCKYLVLD 379
Cdd:cd17948   68 GLVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLD 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528490122 380 EADRMLDMGFEPQIRRIVEQ-----------DTMPPKGsrQTMMFSATFPKEI-QILAR 426
Cdd:cd17948  147 EADTLLDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPSGVgEVLSK 203
HELICc smart00490
helicase superfamily c-terminal domain;
487-568 4.61e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 110.38  E-value: 4.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122   487 DALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 566
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 528490122   567 VG 568
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
218-426 3.89e-27

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: 110.03  E-value: 3.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 218 IMGNITLSRYTRPTPVQKYAIP-IIKT--------KRDLMACAQTGSGKTAAFLLPVLsQIYSEGPGEALQAtkastqqe 288
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 289 ngkyvrrkqypisLVLAPTRELALQIYDEARKFAYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLV 360
Cdd:cd17956   72 -------------LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 361 DMMERGK-IGLDYCKYLVLDEADRMLDMGFE---PQIRRIVEQDTMPPKGSR-------------QTMMFSATFPKEIQI 423
Cdd:cd17956  139 DHLNSTPgFTLKHLRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFgdanllersvrplQKLLFSATLTRDPEK 218

                 ...
gi 528490122 424 LAR 426
Cdd:cd17956  219 LSS 221
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
336-578 3.85e-22

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 100.22  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 336 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdyckyLVLDEA--------DrmldmgFEP---QIRRIVE 398
Cdd:COG0514   94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 399 QDTMPPkgsrqTMMFSATFPKEIQ--ILARDFLEE-YIFLA-VGRvgstsENITQKVVWVEENDKRSFLLDLLNATGKDS 474
Cdd:COG0514  163 RLPNVP-----VLALTATATPRVRadIAEQLGLEDpRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGS 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 475 lTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGRCPIMVATaVA-ARGLDISNVKHVINFDLPSD 553
Cdd:COG0514  233 -GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKS 310
                        250       260
                 ....*....|....*....|....*
gi 528490122 554 IEEYVHRIGRTGRVGNLGLATSFYN 578
Cdd:COG0514  311 IEAYYQEIGRAGRDGLPAEALLLYG 335
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
214-428 8.11e-22

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: 95.14  E-value: 8.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 214 MGEIIMGNITLSRYTRPTPVQKYAIPII-----------------KTKRDLMAcAQTGSGKTAAFLLPVLSQIYSegpgE 276
Cdd:cd17965   15 IKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrkvtkqtsneepKLEVFLLA-AETGSGKTLAYLAPLLDYLKR----Q 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 277 ALQATKASTQQENGKyvRRKQYPISLVLAPTRELALQIYDEARKFAYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVA 354
Cdd:cd17965   90 EQEPFEEAEEEYESA--KDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVT 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528490122 355 TPGRLVDMME-RGKIgLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgSRQTMMFSATFPKEIQILARDF 428
Cdd:cd17965  168 TPGKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
233-563 1.57e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 95.86  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 233 VQKYAIPIIKTKRDLMACAQTGSGKT--AAFLLpvlsqiysegpGEALQATKAstqqengkyvrrkqypisLVLAPTREL 310
Cdd:COG1061   89 LEALLAALERGGGRGLVVAPTGTGKTvlALALA-----------AELLRGKRV------------------LVLVPRREL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 311 ALQIYDEARKFayrsrvrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDYCKYLVLDEADRmldmGFE 390
Cdd:COG1061  140 LEQWAEELRRF-----------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGA 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 391 PQIRRIVEQdtMPPKgsrQTMMFSAT------FPKEI-------------QILARDFLEEYIFLAV--------GRVGST 443
Cdd:COG1061  202 PSYRRILEA--FPAA---YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDAL 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 444 SENITQKVVWVEENdKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR 523
Cdd:COG1061  277 SERLREALAADAER-KDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGE 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 528490122 524 CPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 563
Cdd:COG1061  356 LRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
206-417 1.82e-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: 85.07  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 206 IESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqatka 283
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLSRVDA------------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 284 stqqengkyvrRKQYPISLVLAPTRELALQ---IYDEARKFAYRSRV----RPCVVYGGADIGQQIrdlergchlLVATP 356
Cdd:cd18048   85 -----------LKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTP 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528490122 357 GRLVDMMERGK-IGLDYCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPkgSRQTMMFSATF 417
Cdd:cd18048  145 GTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPK--ECQMLLFSATF 203
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
455-566 6.98e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 81.70  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 455 EENDKRSFLLDLLN---ATGKDSLTLVFVETKKGADALEDFLYREGYACT------SIHGDR--SQRDREEALHQFRSGR 523
Cdd:COG1111  332 IEHPKLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGE 411
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528490122 524 CPIMVATAVAARGLDISNVKHVINFDL-PSDIeEYVHRIGRTGR 566
Cdd:COG1111  412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
463-563 1.47e-14

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: 71.08  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 463 LLDLLNAT---GKDSLTLVFVETKKGADALEDFL-----YREGYACTSIHG----------DRSQRDREEALHQFRSGRC 524
Cdd:cd18802   12 LIEILREYfpkTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGEL 91
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528490122 525 PIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 563
Cdd:cd18802   92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
444-577 5.87e-14

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: 69.16  E-value: 5.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 444 SENITQKVVWVEENDKRSFLLDLLNATGKDSLTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR 523
Cdd:cd18794    1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528490122 524 CPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFY 577
Cdd:cd18794   81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
249-416 3.33e-13

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: 67.43  E-value: 3.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 249 ACAQTGSGKTAAFLLPVLSQIYSEGPGealqatkastqqengkyvrrkqypiSLVLAPTRELALQIYDEARKFAYRS-RV 327
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKKGKK-------------------------VLVLVPTKALALQTAERLRELFGPGiRV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 328 RpcVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKG 406
Cdd:cd00046   61 A--VLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA 138
                        170
                 ....*....|
gi 528490122 407 srQTMMFSAT 416
Cdd:cd00046  139 --QVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
207-421 5.33e-13

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: 68.59  E-value: 5.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 207 ESFHDVDMGEIIMGNITLSRYTRPTPVQKYAIPII--KTKRDLMACAQTGSGKTAAFLLPVLSQIYSegpgealqATKAS 284
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQVEP--------ANKYP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 285 TqqengkyvrrkqypiSLVLAPTRELALQIydeARKFAYRSRVRPCVVYGGADIGQQirdLERGC----HLLVATPGRLV 360
Cdd:cd18047   73 Q---------------CLCLSPTYELALQT---GKVIEQMGKFYPELKLAYAVRGNK---LERGQkiseQIVIGTPGTVL 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528490122 361 DMMERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGSrQTMMFSATFPKEI 421
Cdd:cd18047  132 DWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSV 190
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
460-562 1.39e-11

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: 62.49  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 460 RSFLLDLLNATGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSG-RCPIM-VATAVAARGL 537
Cdd:cd18793   17 LELLEELREPGEK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFlLSTKAGGVGL 93
                         90       100       110
                 ....*....|....*....|....*....|.
gi 528490122 538 DISNVKHVINFDL---PSDIE---EYVHRIG 562
Cdd:cd18793   94 NLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
228-573 1.29e-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: 64.86  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 228 TRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYsEGPGealqATkastqqengkyvrrkqypiSLVLAPT 307
Cdd:COG1205   55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL-EDPG----AT-------------------ALYLYPT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 308 RELAlqiYDEARKF-----AYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERGkIgLDY-------- 372
Cdd:COG1205  111 KALA---RDQLRRLrelaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHYG-L-LPHhtrwarff 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 373 --CKYLVLDEA---------------DRMldmgfepqiRRIVEQdtmppKGSRQTMMF-SATF--PKEiqiLARDFLEEY 432
Cdd:COG1205  179 rnLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 433 iFLAVGRVGSTSENITQkVVW----VEENDKRSFLLD----LLNATGKDSLTLVFVETKKGA--------DALEDFL--- 493
Cdd:COG1205  242 -VTVVDEDGSPRGERTF-VLWnpplVDDGIRRSALAEaarlLADLVREGLRTLVFTRSRRGAellaryarRALREPDlad 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 494 ----YREGYactsihgdrSQRDREEALHQFRSGRCPIMVAT-AVAArGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 568
Cdd:COG1205  320 rvaaYRAGY---------LPEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389

                 ....*
gi 528490122 569 NLGLA 573
Cdd:COG1205  390 QDSLV 394
PRK13766 PRK13766
Hef nuclease; Provisional
455-566 3.08e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 63.35  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 455 EENDKRSFLLDLLNAT---GKDSLTLVFVETKKGADALEDFLYREGYAC------TSIHGDR--SQRDREEALHQFRSGR 523
Cdd:PRK13766 344 IEHPKLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGE 423
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528490122 524 CPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 566
Cdd:PRK13766 424 FNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
508-566 4.64e-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: 55.44  E-value: 4.64e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 508 SQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 566
Cdd:cd18801   75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
450-567 6.35e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.08  E-value: 6.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 450 KVVWVEEndkrsFLLDLLNATGKdslTLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDREEALHQFRSGR-CP-IM 527
Cdd:COG0553  534 KLEALLE-----LLEELLAEGEK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFL 605
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 528490122 528 VATAVAARGLDISNVKHVINFDLP--SDIEEY----VHRIGRTGRV 567
Cdd:COG0553  606 ISLKAGGEGLNLTAADHVIHYDLWwnPAVEEQaidrAHRIGQTRDV 651
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
526-566 3.53e-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: 50.78  E-value: 3.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 528490122 526 IMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 566
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
225-279 2.74e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 53.95  E-value: 2.74e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528490122 225 SRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKT-AAFlLPVLSQIYSEGPGEALQ 279
Cdd:COG1201   20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
PRK13767 PRK13767
ATP-dependent helicase; Provisional
224-279 1.63e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 51.43  E-value: 1.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528490122 224 LSRYTRPTPVQKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEGPGEALQ 279
Cdd:PRK13767  27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGELE 82
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
231-381 5.18e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 49.51  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 231 TPVQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqQENGKyvrrkqypiSLVLAPTRE 309
Cdd:COG1204   24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL-----------------LNGGK---------ALYIVPLRA 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528490122 310 LALQIYDEARKFAYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIG-LDYCKYLVLDEA 381
Cdd:COG1204   78 LASEKYREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
229-354 6.12e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 47.03  E-value: 6.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 229 RPTPVQKYAIPII------KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkastqqENGKYVrrkqypisL 302
Cdd:cd17918   15 SLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGAALLAY------------------KNGKQV--------A 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528490122 303 VLAPTRELALQIYDEARKFAyrSRVRPCVVYGG--ADIGQQIrDLERGCHLLVA 354
Cdd:cd17918   69 ILVPTEILAHQHYEEARKFL--PFINVELVTGGtkAQILSGI-SLLVGTHALLH 119
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
231-381 3.58e-05

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: 44.95  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 231 TPVQKYAI-PIIKTKRDLMACAQTGSGKTAAfllpvlsqiysegpgeALQATKASTQQENGKyvrrkqypiSLVLAPTRE 309
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLI----------------AELAILRALATSGGK---------AVYIAPTRA 57
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528490122 310 LALQIYDEARKFAYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLvDMMER--GKIGLDYCKYLVLDEA 381
Cdd:cd17921   58 LVNQKEADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKL-DLLLRngGERLIQDVRLVVVDEA 127
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
476-566 5.48e-05

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: 43.79  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 476 TLVFVETKKGA--------DALEDFLYREGYACTsiHG--DRSQRDR-EEALhqfRSGRCPIMVATAVAARGLDISNVKH 544
Cdd:cd18796   41 TLVFTNTRSQAerlaqrlrELCPDRVPPDFIALH--HGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDL 115
                         90       100
                 ....*....|....*....|..
gi 528490122 545 VINFDLPSDIEEYVHRIGRTGR 566
Cdd:cd18796  116 VIQIGSPKSVARLLQRLGRSGH 137
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
234-381 5.94e-05

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: 44.50  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 234 QKYAIPIIKTKRDLMACAQTGSGKTAAFLLPVLSQIYSEgPGealqaTKAstqqengkyvrrkqypisLVLAPTRELAlq 313
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PG-----SRA------------------LYLYPTKALA-- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 314 iYDEARKF-----AYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMMERGKI-----------GLdycKYLV 377
Cdd:cd17923   59 -QDQLRSLrelleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHYALLphhdrwarflrNL---RYVV 130

                 ....
gi 528490122 378 LDEA 381
Cdd:cd17923  131 LDEA 134
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
526-578 8.59e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.86  E-value: 8.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528490122 526 IMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFYN 578
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
503-594 1.01e-04

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 503 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISN-----VKHVINFDLPSdieeyVHRI-GRTGRVGNLGLATSF 576
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDHQSYCLLV 141
                         90
                 ....*....|....*...
gi 528490122 577 YNDKNSNITKDLLDILVE 594
Cdd:cd18811  142 YKDPLTETAKQRLRVMTE 159
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
476-563 5.65e-04

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: 40.24  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 476 TLVFVETKKGADALEDFLYREGYACTSIHGDRSQRDRE-EALHQFRSG--RCPIMVATAVAARGLDISNVKHVInFDLP- 551
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                         90
                 ....*....|...
gi 528490122 552 -SDIeEYVHRIGR 563
Cdd:cd18799   88 eSRT-LFLQMLGR 99
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
242-417 1.03e-03

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: 39.98  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 242 KTKRDLMACAQTGSGKTA-AFLLPVLsqiysegpgealqatkastqqengkyvrRKQYPIsLVLAPTRELALQIYDEARK 320
Cdd:cd17926   16 KNNRRGILVLPTGSGKTLtALALIAY----------------------------LKELRT-LIVVPTDALLDQWKERFED 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 321 FAYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEADRmldmGFEPQIRRIVEQD 400
Cdd:cd17926   67 FLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKEL 134
                        170
                 ....*....|....*..
gi 528490122 401 TMPPKgsrqtMMFSATF 417
Cdd:cd17926  135 NAKYR-----LGLTATP 146
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
233-365 1.51e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.42  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 233 VQKYAIP-IIKTKRDLMACAQTGSGKTAAFLLPVLsQIYSEGPGEALQATKAstqqengkyvrrkqypisLVLAPTRELA 311
Cdd:cd18023    5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGNRKV------------------VYIAPIKALC 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528490122 312 LQIYDEAR-KFayrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 365
Cdd:cd18023   66 SEKYDDWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
243-381 2.93e-03

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: 39.56  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 243 TKRDLMACAQTGSGKTaafllpvlsQIysegpgeALQATKASTQQENGKYVRRKqypISLVLAPTRELALQIYDEARKFA 322
Cdd:cd18034   15 LKRNTIVVLPTGSGKT---------LI-------AVMLIKEMGELNRKEKNPKK---RAVFLVPTVPLVAQQAEAIRSHT 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528490122 323 YrSRVRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDYCKYLVLDEA 381
Cdd:cd18034   76 D-LKVGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
503-568 3.14e-03

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: 38.86  E-value: 3.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528490122 503 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 568
Cdd:cd18810   57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
502-610 3.20e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.06  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  502 SIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFYNDK 580
Cdd:PRK09751  306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                          90       100       110
                  ....*....|....*....|....*....|
gi 528490122  581 NSnitKDLLDILVEAKQEVPSWLENLAYEH 610
Cdd:PRK09751  384 TR---RDLVDSAVIVECMFAGRLENLTPPH 410
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
503-568 3.78e-03

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: 38.79  E-value: 3.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528490122 503 IHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 568
Cdd:cd18792   66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
302-383 4.05e-03

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: 39.03  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 302 LVLAPTRELALQIYDEARKFAyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDYCKYLVLDEA 381
Cdd:cd18035   49 LILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126

                 ..
gi 528490122 382 DR 383
Cdd:cd18035  127 HH 128
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
242-430 4.33e-03

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 38.95  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 242 KTKRDLMACAQTGSGKTAAFLLPVLSQIysegpgealqatkaSTQQENGKYVRRKQYPISLVlAPTRELALQIYDearKF 321
Cdd:cd18020   15 KTNENMLICAPTGAGKTNIAMLTILHEI--------------RQHVNQGGVIKKDDFKIVYI-APMKALAAEMVE---KF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 322 AyrSRVRPcvvyggadIGQQIRDLE----------RGCHLLVATPGRLvDMMERGKIG----LDYCKYLVLDEAdRMLDM 387
Cdd:cd18020   77 S--KRLAP--------LGIKVKELTgdmqltkkeiAETQIIVTTPEKW-DVVTRKSSGdvalSQLVRLLIIDEV-HLLHD 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528490122 388 GFEPQIRRIVEQdTMPPKGSRQTMM----FSATFPKEIQIlaRDFLE 430
Cdd:cd18020  145 DRGPVIESLVAR-TLRQVESTQSMIrivgLSATLPNYLDV--ADFLR 188
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
245-274 4.66e-03

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 38.33  E-value: 4.66e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 528490122 245 RDLMACAQTGSGKTAAFLLPVLSQIYSEGP 274
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLADEPE 31
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
462-566 5.27e-03

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: 38.00  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122 462 FLLDLLNATGKdslTLVFVETKKGADAL-EDFLYregYActsIHGDRSQRDREEALHQFRSGRCPIMVATAVAARGLDI- 539
Cdd:cd18789   41 ELLKRHEQGDK---IIVFTDNVEALYRYaKRLLK---PF---ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLp 111
                         90       100
                 ....*....|....*....|....*...
gi 528490122 540 -SNVKHVINFDLPSDiEEYVHRIGRTGR 566
Cdd:cd18789  112 eANVAIQISGHGGSR-RQEAQRLGRILR 138
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
411-568 5.81e-03

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: 39.36  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  411 MMFSATFPKEIQILARDFleEYIFLAVGRVGSTSENITQKVVWVEENDKR---SFLLDLLNATGKDSLTLVFVETKKGAD 487
Cdd:TIGR01587 159 LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILIESDKVgeiSSLERLLEFIKKGGSIAIIVNTVDRAQ 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490122  488 ALEDFLYREGYACTSI--HGDRSQRDRE----EALHQFRSGRCP-IMVATAVAARGLDISnvkhvinFDL----PSDIEE 556
Cdd:TIGR01587 237 EFYQQLKEKAPEEEIIlyHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLDIS-------ADVmiteLAPIDS 309
                         170
                  ....*....|..
gi 528490122  557 YVHRIGRTGRVG 568
Cdd:TIGR01587 310 LIQRLGRLHRYG 321
 
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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