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Conserved domains on  [gi|87196351|ref|NP_001347|]
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ATP-dependent RNA helicase DDX3X isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13030640)

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

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

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 ...
160-410 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: 591.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 160 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 239
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 240 SQIYSDGPGEALraMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 319
Cdd:cd18051  81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 320 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 399
Cdd:cd18051 159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                       250
                ....*....|.
gi 87196351 400 YIFLAVGRVGS 410
Cdd:cd18051 239 YIFLAVGRVGS 249
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
415-545 4.21e-61

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: 200.04  E-value: 4.21e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 415 ITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 494
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 87196351 495 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 545
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 ...
160-410 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: 591.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 160 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 239
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 240 SQIYSDGPGEALraMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 319
Cdd:cd18051  81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 320 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 399
Cdd:cd18051 159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                       250
                ....*....|.
gi 87196351 400 YIFLAVGRVGS 410
Cdd:cd18051 239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
181-568 1.18e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 488.50  E-value: 1.18e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEAlRAmkengry 260
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 261 grrkqypisLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 340
Cdd:COG0513  75 ---------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 341 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 420
Cdd:COG0513 146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 421 WVEESDKRSFLLDLLNATGKDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 500
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87196351 501 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 568
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
PTZ00110 PTZ00110
helicase; Provisional
57-580 3.91e-133

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 402.23  E-value: 3.91e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   57 SSGWSSSKDkdAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDY-DGIGSRGdrSGFGKFERGGN--SRWCDKSDE 133
Cdd:PTZ00110   3 STDGSSSNG--SVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFrPGYGNYS--GGYGGFGMNSYgsSTLGKRLQP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  134 DDWSK-PLPPSER---LEQELFSGGNTginfEKYDDIPVE-----ATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPT 204
Cdd:PTZ00110  79 IDWKSiNLVPFEKnfyKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  205 PVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSdgpgealramKENGRYGrrkQYPISLVLAPTRELAVQIYE 284
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA----------QPLLRYG---DGPIVLVLAPTRELAEQIRE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  285 EARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRI 364
Cdd:PTZ00110 222 QCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  365 VEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG-STSENITQKVVWVEESDKRSFLLDLLNATGKD- 441
Cdd:PTZ00110 302 VSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDg 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  442 SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSD 521
Cdd:PTZ00110 378 DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351  522 IEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHY 580
Cdd:PTZ00110 458 IEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSN 516
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
415-545 4.21e-61

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: 200.04  E-value: 4.21e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 415 ITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 494
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 87196351 495 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 545
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
204-392 6.09e-61

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: 200.93  E-value: 6.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   204 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGealramkengrygrrkqyPISLVLAPTRELAVQIY 283
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   284 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 363
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 87196351   364 IVEQdtMPPKgvRHTMMFSATFPKEIQML 392
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
195-418 7.04e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 7.04e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    195 IELTRYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgealramkengRYGRRKQYPISLVLA 273
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    274 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 352
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196351    353 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 418
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
426-536 3.77e-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: 134.26  E-value: 3.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   426 DKRSFLLDLLNaTGKDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 505
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 87196351   506 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 536
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
455-536 3.13e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 113.85  E-value: 3.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    455 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 534
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 87196351    535 VG 536
Cdd:smart00490  81 AG 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
304-558 1.14e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 95.59  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 304 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 366
Cdd:COG0514  94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 367 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEESDKRSFLLDLLNATGK 440
Cdd:COG0514 163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 441 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVKHVINFDLP 519
Cdd:COG0514 231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 87196351 520 SDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLD 558
Cdd:COG0514 309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
PRK13766 PRK13766
Hef nuclease; Provisional
431-534 3.20e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 60.27  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  431 LLDLLNAT---GKDSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATA 499
Cdd:PRK13766 352 LREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 87196351  500 VAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 534
Cdd:PRK13766 432 VAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
344-536 3.80e-05

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: 46.29  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   344 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 423
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   424 ESDKR---SFLLDLLNATGKDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 489
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 87196351   490 GKSPILVATAVAARGLDISnvkhvinFDL----PSDIEEYVHRIGRTGRVG 536
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 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 ...
160-410 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: 591.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 160 FEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPIL 239
Cdd:cd18051   1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 240 SQIYSDGPGEALraMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL 319
Cdd:cd18051  81 SQIYEQGPGESL--PSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 320 LVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDE 399
Cdd:cd18051 159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
                       250
                ....*....|.
gi 87196351 400 YIFLAVGRVGS 410
Cdd:cd18051 239 YIFLAVGRVGS 249
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
181-568 1.18e-168

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 488.50  E-value: 1.18e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEAlRAmkengry 260
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAP-QA------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 261 grrkqypisLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 340
Cdd:COG0513  75 ---------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 341 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 420
Cdd:COG0513 146 VETLVLDEADRMLDMGFIEDIERILKL--LPKE--RQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 421 WVEESDKRSFLLDLLNATGKDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 500
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87196351 501 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 568
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
181-409 2.62e-161

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: 461.96  E-value: 2.62e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPgealramkENGRY 260
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGP--------PSVGR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 261 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 340
Cdd:cd17967  73 GRRKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSS 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 341 CKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVG 409
Cdd:cd17967 153 IKFLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
139-409 1.02e-151

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: 439.02  E-value: 1.02e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 139 PLPPSERlEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKR 218
Cdd:cd18052   3 PPPPPED-EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 219 DLMACAQTGSGKTAAFLLPILSQIYSDGpgeaLRAMKENGrygrrKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPC 298
Cdd:cd18052  82 DLMACAQTGSGKTAAFLLPVLTGMMKEG----LTASSFSE-----VQEPQALIVAPTRELANQIFLEARKFSYGTCIRPV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 299 VVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHT 378
Cdd:cd18052 153 VVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQT 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 87196351 379 MMFSATFPKEIQMLARDFLDE-YIFLAVGRVG 409
Cdd:cd18052 233 LMFSATFPEEIQRLAAEFLKEdYLFLTVGRVG 264
PTZ00110 PTZ00110
helicase; Provisional
57-580 3.91e-133

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 402.23  E-value: 3.91e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   57 SSGWSSSKDkdAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDY-DGIGSRGdrSGFGKFERGGN--SRWCDKSDE 133
Cdd:PTZ00110   3 STDGSSSNG--SVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFrPGYGNYS--GGYGGFGMNSYgsSTLGKRLQP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  134 DDWSK-PLPPSER---LEQELFSGGNTginfEKYDDIPVE-----ATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPT 204
Cdd:PTZ00110  79 IDWKSiNLVPFEKnfyKEHPEVSALSS----KEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  205 PVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSdgpgealramKENGRYGrrkQYPISLVLAPTRELAVQIYE 284
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA----------QPLLRYG---DGPIVLVLAPTRELAEQIRE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  285 EARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRI 364
Cdd:PTZ00110 222 QCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  365 VEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL-DEYIFLAVGRVG-STSENITQKVVWVEESDKRSFLLDLLNATGKD- 441
Cdd:PTZ00110 302 VSQ--IRPD--RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDg 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  442 SLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSD 521
Cdd:PTZ00110 378 DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351  522 IEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHY 580
Cdd:PTZ00110 458 IEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSN 516
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
200-548 1.23e-99

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 312.51  E-value: 1.23e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpgealramkeNGRYgRRKQypiSLVLAPTRELA 279
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQ---ALVLCPTRELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  280 VQIYEEARKFSyrsRVRP-------CvvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 352
Cdd:PRK11776  86 DQVAKEIRRLA---RFIPnikvltlC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  353 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYifLAVgRVGSTSEN--ITQKVVWVEESDKRSF 430
Cdd:PRK11776 160 LDMGFQDAIDAIIRQ--APAR--RQTLLFSATYPEGIAAISQRFQRDP--VEV-KVESTHDLpaIEQRFYEVSPDERLPA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  431 LLDLLNATGKDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNV 510
Cdd:PRK11776 233 LQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 87196351  511 KHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNER 548
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
181-568 1.12e-96

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 304.81  E-value: 1.12e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPgealrAMKengry 260
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQP-----HAK----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  261 GRRkqyPI-SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 339
Cdd:PRK10590  72 GRR---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  340 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 419
Cdd:PRK10590 149 QVEILVLDEADRMLDMGFIHDIRRVLAK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  420 VWVEESDKRSfLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 499
Cdd:PRK10590 225 HFVDKKRKRE-LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATD 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351  500 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLveaKQEVP 568
Cdd:PRK10590 304 IAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
191-403 9.13e-96

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 292.81  E-value: 9.13e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPgealramkengrygRRKQYPISL 270
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK--------------KKGRGPQAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 271 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 350
Cdd:cd00268  67 VLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEAD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 87196351 351 RMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 403
Cdd:cd00268 147 RMLDMGFEEDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLKNPVRI 195
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
166-576 1.69e-92

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 295.93  E-value: 1.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  166 IPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILS---QI 242
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  243 YSDGPGEalramkengrygRRKqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVA 322
Cdd:PLN00206 187 RSGHPSE------------QRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVG 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  323 TPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPpkgvrHTMMFSATFPKEIQMLARDFLDEYIF 402
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIIL 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  403 LAVGRVGSTSENITQKVVWVEESDKRSFLLDLLnaTGKDSLT---LVFVETKKGADSLEDFL-YHEGYACTSIHGDRSQR 478
Cdd:PLN00206 328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL--KSKQHFKppaVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMK 405
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  479 DREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLD 558
Cdd:PLN00206 406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
                        410
                 ....*....|....*...
gi 87196351  559 LLVEAKQEVPSWLENMAY 576
Cdd:PLN00206 486 LLKSSGAAIPRELANSRY 503
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
182-547 1.17e-91

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 292.59  E-value: 1.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  182 FSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEAlRAMKEngryg 261
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKE-RYMGE----- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  262 rrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLE-RGCHLLVATPGRLVDMMERGKIGLDF 340
Cdd:PRK01297 163 -----PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDM 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  341 CKYLVLDEADRMLDMGFEPQIRRIVEQDtmPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVV 420
Cdd:PRK01297 238 VEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVY 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  421 WVEESDKRSFLLDLLNATGKDSLtLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 500
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 87196351  501 AARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNE 547
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
182-544 1.11e-83

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 270.28  E-value: 1.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  182 FSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsQIYSDGPgealramkengryg 261
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  262 RRKQYPIS-LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDF 340
Cdd:PRK11192  68 RRKSGPPRiLILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  341 CKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPKGVRHTMMFSATFPKE-IQMLARDFLDEYIFLAVGrvGSTSE--NITQ 417
Cdd:PRK11192 148 VETLILDEADRMLDMGFAQDIETIAAE----TRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQ 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  418 kvvWVEESD----KRSFLLDLLNATGKDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP 493
Cdd:PRK11192 222 ---WYYRADdlehKTALLCHLLKQPEVTR-SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVN 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 87196351  494 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSF 544
Cdd:PRK11192 298 VLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
181-569 3.08e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 273.36  E-value: 3.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDgPGEAlramkengry 260
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALA---------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  261 GRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKI-GLD 339
Cdd:PRK04537  79 DRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  340 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 419
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  420 VWVEESDKRSFLLDLLNATgKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 499
Cdd:PRK04537 237 YFPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  500 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERninITKDLLDLLVEAKQEVPS 569
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIPV 382
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
191-403 4.63e-83

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: 259.99  E-value: 4.63e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIySDGPgealramkengrYGRRKQYPISL 270
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-NAQP------------PLERGDGPIVL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 271 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 350
Cdd:cd17966  68 VLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEAD 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 87196351 351 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYIFL 403
Cdd:cd17966 148 RMLDMGFEPQIRKIVDQ-IRPD---RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
204-544 2.25e-78

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 256.05  E-value: 2.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  204 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEalramkengryGRRKQYPISLVLAPTRELAVQIY 283
Cdd:PRK04837  32 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE-----------DRKVNQPRALIMAPTRELAVQIH 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  284 EEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRR 363
Cdd:PRK04837 101 ADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDIRW 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  364 IVEQdtMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSl 443
Cdd:PRK04837 181 LFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDR- 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  444 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIE 523
Cdd:PRK04837 258 AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCE 337
                        330       340
                 ....*....|....*....|.
gi 87196351  524 EYVHRIGRTGRVGNLGLATSF 544
Cdd:PRK04837 338 DYVHRIGRTGRAGASGHSISL 358
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
181-548 2.21e-71

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 243.22  E-value: 2.21e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDgpgeaLRAmkengry 260
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE-----LKA------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  261 grrkqyPISLVLAPTRELAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 339
Cdd:PRK11634  75 ------PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  340 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKV 419
Cdd:PRK11634 149 KLSGLVLDEADEMLRMGFIEDVETIMAQ--IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  420 VWVEESDKRSFLLDLLNATGKDSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATA 499
Cdd:PRK11634 225 WTVWGMRKNEALVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATD 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 87196351  500 VAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNER 548
Cdd:PRK11634 304 VAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENR 352
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
170-397 9.92e-71

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: 228.80  E-value: 9.92e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 170 ATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGE 249
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 250 AlramkENGrygrrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVD 329
Cdd:cd17953  82 P-----GEG--------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMID 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 330 M--MERGKI-GLDFCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17953 149 IltANNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIV--NNIRPD--RQTVLFSATFPRKVEALARKVL 215
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
168-406 2.27e-69

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: 225.66  E-value: 2.27e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 168 VEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgp 247
Cdd:cd18049  12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 248 gealramkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRL 327
Cdd:cd18049  87 --------NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRL 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 328 VDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 406
Cdd:cd18049 159 IDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
172-406 3.06e-68

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: 224.12  E-value: 3.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 172 GNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpgeal 251
Cdd:cd18050  54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 252 ramkENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMM 331
Cdd:cd18050 125 ----NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL 200
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87196351 332 ERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVG 406
Cdd:cd18050 201 EAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPD--RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
191-401 4.93e-67

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: 218.05  E-value: 4.93e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpgealraMKEngRYGRRKQYPISL 270
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-----------MDQ--RELEKGEGPIAV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 271 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEAD 350
Cdd:cd17952  68 IVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEAD 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 87196351 351 RMLDMGFEPQIRRIVEQdTMPPkgvRHTMMFSATFPKEIQMLARDFLDEYI 401
Cdd:cd17952 148 RMFDMGFEYQVRSIVGH-VRPD---RQTLLFSATFKKKIEQLARDILSDPI 194
PTZ00424 PTZ00424
helicase 45; Provisional
179-556 1.21e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 218.93  E-value: 1.21e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  179 IESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDgpgeaLRAMKeng 258
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD-----LNACQ--- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  259 rygrrkqypiSLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 338
Cdd:PTZ00424  99 ----------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  339 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQK 418
Cdd:PTZ00424 169 DDLKLFILDEADEMLSRGFKGQIYDVFKK--LPPD--VQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQF 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  419 VVWVEESD-KRSFLLDLLnatgkDSLTLV----FVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP 493
Cdd:PTZ00424 245 YVAVEKEEwKFDTLCDLY-----ETLTITqaiiYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTR 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87196351  494 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDL 556
Cdd:PTZ00424 320 VLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
195-397 2.25e-63

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: 209.10  E-value: 2.25e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 195 IELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpGEALRAMKENGRYGrrkqyPISLVLAP 274
Cdd:cd17945   5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYI-----SRLPPLDEETKDDG-----PYALILAP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 275 TRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 354
Cdd:cd17945  75 TRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 355 MGFEPQIRRIVeqDTMPP------------------KGVRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17945 155 MGFEPQVTKIL--DAMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYL 213
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
415-545 4.21e-61

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: 200.04  E-value: 4.21e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 415 ITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPI 494
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 87196351 495 LVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFF 545
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
204-392 6.09e-61

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: 200.93  E-value: 6.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   204 TPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGealramkengrygrrkqyPISLVLAPTRELAVQIY 283
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------------------PQALVLAPTRELAEQIY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   284 EEARKFSYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKiGLDFCKYLVLDEADRMLDMGFEPQIRR 363
Cdd:pfam00270  63 EELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEE 140
                         170       180
                  ....*....|....*....|....*....
gi 87196351   364 IVEQdtMPPKgvRHTMMFSATFPKEIQML 392
Cdd:pfam00270 141 ILRR--LPKK--RQILLLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
199-394 2.14e-57

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: 193.18  E-value: 2.14e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 199 RYTRPTPVQKHAI-PIIKEKRDLMACAQTGSGKTAAFLLPilsqiysdgpgeALRAMKENGRYGRRKQYPIsLVLAPTRE 277
Cdd:cd17964  13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLP------------AIQSLLNTKPAGRRSGVSA-LIISPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 278 LAVQIYEEARKFSYRSR-VRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMME--RGKIGLDFCKYLVLDEADRML 353
Cdd:cd17964  80 LALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 87196351 354 DMGFEPQIRRIVeqDTMPPKGVRH--TMMFSATFPKEIQMLAR 394
Cdd:cd17964 160 DMGFRPDLEQIL--RHLPEKNADPrqTLLFSATVPDEVQQIAR 200
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
191-406 3.14e-57

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: 192.03  E-value: 3.14e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAmkengrygrrkqypisL 270
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRA----------------L 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 271 VLAPTRELAVQIYEEARKFSYRSRVRPCVVYGG-ADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 349
Cdd:cd17957  65 ILAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 87196351 350 DRMLDMGFEPQIRRIVEQDTMPPKgvrHTMMFSATFPKEIQMLARDFLDEYIFLAVG 406
Cdd:cd17957 145 DKLFEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
200-398 6.52e-57

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: 191.31  E-value: 6.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQ-IYSDGPGEALRAmkengrygrrkqypisLVLAPTREL 278
Cdd:cd17947  10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERlLYRPKKKAATRV----------------LVLVPTREL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 279 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMGF 357
Cdd:cd17947  74 AMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 87196351 358 EPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLARDFLD 398
Cdd:cd17947 154 ADELKEILR---LCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
DEXDc smart00487
DEAD-like helicases superfamily;
195-418 7.04e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 191.17  E-value: 7.04e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    195 IELTRYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgealramkengRYGRRKQYPISLVLA 273
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPAL-------------------EALKRGKGGRVLVLV 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    274 PTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 352
Cdd:smart00487  62 PTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196351    353 LDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRvgSTSENITQK 418
Cdd:smart00487 142 LDGGFGDQLEKLLKL--LPKN--VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
191-399 6.53e-55

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: 185.75  E-value: 6.53e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQI-YSDGPGEalramKENGrygrrkqyPIS 269
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdLQPIPRE-----QRNG--------PGV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 270 LVLAPTRELAVQIYEEARKFSYRSRVRPCVvYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 349
Cdd:cd17958  68 LVLTPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEA 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 87196351 350 DRMLDMGFEPQIRRIVeQDTMPPkgvRHTMMFSATFPKEIQMLARDFLDE 399
Cdd:cd17958 147 DRMLDMGFEPQIRKIL-LDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
200-402 1.44e-54

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: 185.12  E-value: 1.44e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGpgealramkengrYGrrkqyPISLVLAPTRELA 279
Cdd:cd17955  19 IKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP-------------YG-----IFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 280 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMME---RGKIGLDFCKYLVLDEADRMLDMG 356
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 87196351 357 FEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIF 402
Cdd:cd17955 161 FEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
202-397 9.04e-54

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: 183.31  E-value: 9.04e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 202 RPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgeaLRAMKENGRYG-RRKQYPISLVLAPTRELAV 280
Cdd:cd17951  12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-----------MFALEQEKKLPfIKGEGPYGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 281 QIYEEARKFSYR------SRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLD 354
Cdd:cd17951  81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 87196351 355 MGFEPQIRRIVEQDtmppKGVRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17951 161 MGFEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
181-394 1.58e-52

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: 179.82  E-value: 1.58e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 181 SFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYsdgpgealramkengry 260
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL----------------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 261 gRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLD 339
Cdd:cd17954  64 -ENPQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLK 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 87196351 340 FCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPKgvRHTMMFSATFPKEIQMLAR 394
Cdd:cd17954 143 SLKFLVMDEADRLLNMDFEPEIDKILK--VIPRE--RTTYLFSATMTTKVAKLQR 193
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
199-403 5.33e-49

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 170.46  E-value: 5.33e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 199 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPgealRAMKENGRYGrrkqypisLVLAPTREL 278
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP----RVDRSDGTLA--------LVLVPTREL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 279 AVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGK-IGLDFCKYLVLDEADRMLDMG 356
Cdd:cd17949  78 ALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMG 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 87196351 357 FEPQIRRIVE--------QDTMPPKGV-RHTMMFSATFPKEIQMLARDFLDEYIFL 403
Cdd:cd17949 158 FEKDITKILEllddkrskAGGEKSKPSrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
189-401 2.24e-48

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: 168.25  E-value: 2.24e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 189 EIIMGNIELTrYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGealramkengrygrrkqypI 268
Cdd:cd17940   9 ELLMGIFEKG-FEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV-------------------I 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 269 -SLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLD 347
Cdd:cd17940  69 qALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 87196351 348 EADRMLDMGFEPQIRRIVeqDTMPPKgvRHTMMFSATFPKEIQmlarDFLDEYI 401
Cdd:cd17940 149 EADKLLSQDFQPIIEKIL--NFLPKE--RQILLFSATFPLTVK----NFMDRHM 194
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
200-403 6.85e-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: 167.10  E-value: 6.85e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAmkengrygrrkqypisLVLAPTRELA 279
Cdd:cd17959  21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARA----------------LILSPTRELA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 280 VQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEP 359
Cdd:cd17959  85 LQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAE 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 87196351 360 QIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFL 403
Cdd:cd17959 165 QLHEILSR--LPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
200-397 5.03e-47

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 164.67  E-value: 5.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYsdgpgealramkeNGRYGRRKQYPISLVLAPTRELA 279
Cdd:cd17960  10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL-------------KRKANLKKGQVGALIISPTRELA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 280 VQIYEEARKF--SYRSRVRPCVVYGGADIGQQIRDLER-GCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDEADRMLD 354
Cdd:cd17960  77 TQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLD 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 87196351 355 MGFEPQIRRIVEQdtmPPKGvRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17960 157 LGFEADLNRILSK---LPKQ-RRTGLFSATQTDAVEELIKAGL 195
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
200-405 4.22e-45

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: 159.38  E-value: 4.22e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSD--GPGEALRAmkengrygrrkqypisLVLAPTRE 277
Cdd:cd17941  10 FIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwTPEDGLGA----------------LIISPTRE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 278 LAVQIYEEARKFSYRSRVRPCVVYGGADIGQQirdLER--GCHLLVATPGRLVDMMERgKIGLDF--CKYLVLDEADRML 353
Cdd:cd17941  74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEE---KERinRMNILVCTPGRLLQHMDE-TPGFDTsnLQMLVLDEADRIL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 87196351 354 DMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDEYIFLAV 405
Cdd:cd17941 150 DMGFKETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
186-384 1.36e-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: 158.25  E-value: 1.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 186 EMG---EIIMGnIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsQIYSdgpgealramkengrygr 262
Cdd:cd17938   3 ELGvmpELIKA-VEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV------------------ 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 263 rkqypiSLVLAPTRELAVQIYEEARKFSY---RSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLD 339
Cdd:cd17938  63 ------ALILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLS 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 87196351 340 FCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKGVR----HTMMFSAT 384
Cdd:cd17938 137 SVRFFVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
194-401 5.00e-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: 156.17  E-value: 5.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 194 NIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSqiysdgpgealRAMKEngrygrrKQYPISLVLA 273
Cdd:cd17962   4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII-----------RCLTE-------HRNPSALILT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 274 PTRELAVQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM 352
Cdd:cd17962  66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 87196351 353 LDMGFEPQIRRIVEQDTMPPKgvrhTMMFSATFPKEIQMLARDFLDEYI 401
Cdd:cd17962 146 LKMGFQQQVLDILENISHDHQ----TILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
199-394 1.53e-41

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


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 150.85  E-value: 1.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 199 RYTRPTPVQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpgeaLRAMKENGRYGRRKqYPISLVLAPTRE 277
Cdd:cd17946   9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERL--------LSQKSSNGVGGKQK-PLRALILTPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 278 LAVQI---YEEARKFsyrSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL---DFCKYLVLDEADR 351
Cdd:cd17946  80 LAVQVkdhLKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 87196351 352 MLDMG-FEP--QIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLAR 394
Cdd:cd17946 157 MLEKGhFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLK 202
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
191-394 4.93e-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: 148.28  E-value: 4.93e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 191 IMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSdgpgeaLRAMKENGRYGrrkqypisL 270
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK------LKFKPRNGTGV--------I 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 271 VLAPTRELAVQIYEEARKF-SYRSRVRPCVVyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKiglDF----CKYLV 345
Cdd:cd17942  67 IISPTRELALQIYGVAKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTK---GFlyknLQCLI 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 87196351 346 LDEADRMLDMGFEPQIRRIVEqdtMPPKGvRHTMMFSATFPKEIQMLAR 394
Cdd:cd17942 143 IDEADRILEIGFEEEMRQIIK---LLPKR-RQTMLFSATQTRKVEDLAR 187
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
200-397 9.11e-40

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: 145.03  E-value: 9.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIysdgpgeaLRAMKENGRYgrrkQYPISLVLAPTRELA 279
Cdd:cd17961  14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI--------LKAKAESGEE----QGTRALILVPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 280 VQIYEEARKFSY--RSRVRpCV-VYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL-DFCKYLVLDEADRMLDM 355
Cdd:cd17961  82 QQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 87196351 356 GFEPQIRRIVEqdtMPPKGVRHTMMfSATFPKEIQMLARDFL 397
Cdd:cd17961 161 GYEEDLKSLLS---YLPKNYQTFLM-SATLSEDVEALKKLVL 198
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
200-397 3.33e-38

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: 140.15  E-value: 3.33e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYSDgpgeaLRAMKengrygrrkqypiSLVLAPTREL 278
Cdd:cd17939  17 FEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSIGALQRIDTT-----VRETQ-------------ALVLAPTREL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 279 AVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMG 356
Cdd:cd17939  78 AQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 87196351 357 FEPQIRRIVeqdTMPPKGVRhTMMFSATFPKEIQMLARDFL 397
Cdd:cd17939 156 FKDQIYDIF---QFLPPETQ-VVLFSATMPHEVLEVTKKFM 192
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
200-396 5.62e-38

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


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 139.63  E-value: 5.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSQIysDgpgealramkengrygRRKQYPISLVLAPTRE 277
Cdd:cd17963  14 FNKPSKIQETALPLIlsDPPENLIAQSQSGTGKTAAFVLAMLSRV--D----------------PTLKSPQALCLAPTRE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 278 LAVQIYEEARKF-SY-----RSRVRPCVVYGGADIGQQIrdlergchlLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 351
Cdd:cd17963  76 LARQIGEVVEKMgKFtgvkvALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 87196351 352 MLDM-GFEPQIRRIVEqdtMPPKGVRhTMMFSATFPKEIQMLARDF 396
Cdd:cd17963 147 MLDTqGHGDQSIRIKR---MLPRNCQ-ILLFSATFPDSVRKFAEKI 188
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
426-536 3.77e-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: 134.26  E-value: 3.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   426 DKRSFLLDLLNaTGKDSLTLVFVETKKGADsLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGL 505
Cdd:pfam00271   1 EKLEALLELLK-KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 87196351   506 DISNVKHVINFDLPSDIEEYVHRIGRTGRVG 536
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
182-397 7.93e-35

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: 131.03  E-value: 7.93e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 182 FSDVEMGEIIMGNIELTRYTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYSDgpgeaLRAMKengry 260
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAImPCIK-GYDVIAQAQSGTGKTATFSISILQQIDTS-----LKATQ----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 261 grrkqypiSLVLAPTRELAVQIYE--EARKFSYRSRVRPCVvyGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGL 338
Cdd:cd18046  70 --------ALVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRT 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 339 DFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd18046 140 DYIKMFVLDEADEMLSRGFKDQIYDIFQK--LPPD--TQVVLLSATMPNDVLEVTTKFM 194
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
203-397 7.99e-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: 131.31  E-value: 7.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 203 PTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQI-YSDGPGEALramkengrygrrkqypislVLAPTRELAVQ 281
Cdd:cd17950  25 PSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLePVDGQVSVL-------------------VICHTRELAFQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 282 IYEEARKFS-YRSRVRPCVVYGGADIGQQIRDLERGC-HLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRM---LDMg 356
Cdd:cd17950  86 ISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMleqLDM- 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 87196351 357 fepqiRRIVeQD--TMPPKGvRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17950 165 -----RRDV-QEifRATPHD-KQVMMFSATLSKEIRPVCKKFM 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
200-402 3.80e-34

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: 128.54  E-value: 3.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgEALRamkengrygRRKQYPISLVLAPTRELA 279
Cdd:cd17943  10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL---------ESLD---------LERRHPQVLILAPTREIA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 280 VQIYEEARKF-SYRSRVRPCVVYGGADIGQQIRDLeRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 358
Cdd:cd17943  72 VQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 87196351 359 PQIRRIveqDTMPPKGvRHTMMFSATFPKE-IQMLARdFLDEYIF 402
Cdd:cd17943 151 KDVNWI---FSSLPKN-KQVIAFSATYPKNlDNLLAR-YMRKPVL 190
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
205-397 1.41e-30

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 118.80  E-value: 1.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 205 PVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgEALRAMKENGRYGRRkqyPISLVLAPTRELAVQIYE 284
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLI---------EKLQEDQQPRKRGRA---PKVLVLAPTRELANQVTK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 285 EARKFSYRSRVrpCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRI 364
Cdd:cd17944  83 DFKDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 87196351 365 V-EQDTMPPKGVRHTMMFSATFPKEIQMLARDFL 397
Cdd:cd17944 161 LsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
200-399 3.03e-30

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: 117.95  E-value: 3.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 200 YTRPTPVQKHAI-PIIKeKRDLMACAQTGSGKTAAFLLPILSQIYSdgpgealrAMKEngrygrrkqyPISLVLAPTREL 278
Cdd:cd18045  19 FEKPSAIQQRAIkPIIK-GRDVIAQSQSGTGKTATFSISVLQCLDI--------QVRE----------TQALILSPTREL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 279 AVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFE 358
Cdd:cd18045  80 AVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 87196351 359 PQIRRIVEQdtMPPKgvRHTMMFSATFPKEIQMLARDFLDE 399
Cdd:cd18045 160 EQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTD 196
HELICc smart00490
helicase superfamily c-terminal domain;
455-536 3.13e-30

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 113.85  E-value: 3.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351    455 DSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 534
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 87196351    535 VG 536
Cdd:smart00490  81 AG 82
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
197-387 2.78e-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: 116.31  E-value: 2.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 197 LTRY--TRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQI--YSDGPGEALRAmkengrygrrkqyPISLVL 272
Cdd:cd17948   5 LQRQgiTKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPFNA-------------PRGLVI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 273 APTRELAVQIYEEARKFSYRSRVRPCVVYGGADIgQQIRDLERG-CHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 351
Cdd:cd17948  72 TPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADT 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 87196351 352 MLDMGFEPQIRRIVEQ-----------DTMPPKGvrHTMMFSATFPK 387
Cdd:cd17948 151 LLDDSFNEKLSHFLRRfplasrrsentDGLDPGT--QLVLVSATMPS 195
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
199-392 2.04e-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: 110.80  E-value: 2.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 199 RYTRPTPVQKHAIP-IIKE--------KRDLMACAQTGSGKTAAFLLPILsQIYSDGPGEALRAmkengrygrrkqypis 269
Cdd:cd17956   9 GITSAFPVQAAVIPwLLPSskstppyrPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRLRA---------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 270 LVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHL--------LVATPGRLVDMMERGK-IGLDF 340
Cdd:cd17956  72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTPgFTLKH 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 341 CKYLVLDEADRMLDMGFE---PQIRRIVEQDTMP------------PKGVR-HTMMFSATF---PKEIQML 392
Cdd:cd17956 152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPdlgsfgdanlleRSVRPlQKLLFSATLtrdPEKLSSL 222
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
187-396 6.12e-24

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: 101.30  E-value: 6.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 187 MGEIIMGNIELTRYTRPTPVQKHAIPII------KEKRD-----------LMAcAQTGSGKTAAFLLPILSQIYSD--GP 247
Cdd:cd17965  15 IKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrKVTKQtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQeqEP 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 248 GEALRAMKEN-GRYGRrkqyPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVV-YGGADIGQQIRDLERG-CHLLVATP 324
Cdd:cd17965  94 FEEAEEEYESaKDTGR----PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVTTP 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87196351 325 GRLVDMME-RGKIgLDFCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPkgVRHTMMFSATFPKEIQMLARDF 396
Cdd:cd17965 170 GKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APK--LKHLILCSATIPKEFDKTLRKL 237
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
215-531 1.57e-22

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 102.03  E-value: 1.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 215 KEKRDLMACAQTGSGKTAAfllpilsqiysdgpgeALRAMKENGRYGRrkqypiSLVLAPTRELAVQIYEEARKFsyrsr 294
Cdd:COG1061  98 RGGGRGLVVAPTGTGKTVL----------------ALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF----- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 295 vrpcvvYGGADIGQQIRDleRGCHLLVATPGRLVDMMERGKIGlDFCKYLVLDEADRmldmGFEPQIRRIVEQdtMPPKg 374
Cdd:COG1061 151 ------LGDPLAGGGKKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEA--FPAA- 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 375 vrHTMMFSAT------FPKEI-------------QMLARDFLDEYIFLAV--------GRVGSTSENITQKVVwVEESDK 427
Cdd:COG1061 215 --YRLGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALA-ADAERK 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 428 RSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI 507
Cdd:COG1061 292 DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
                       330       340
                ....*....|....*....|....
gi 87196351 508 SNVKHVINFDLPSDIEEYVHRIGR 531
Cdd:COG1061 372 PRLDVAILLRPTGSPREFIQRLGR 395
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
304-558 1.14e-20

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 95.59  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 304 ADIGQQIRDLERG-CHLLVATPGRL-----VDMMERGKIGLdfckyLVLDEA--------DrmldmgFEP---QIRRIVE 366
Cdd:COG0514  94 EERREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRE 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 367 QDTMPPkgvrhTMMFSATFPKE-----IQMLARDflDEYIFLA-VGRvgstsENITQKVVWVEESDKRSFLLDLLNATGK 440
Cdd:COG0514 163 RLPNVP-----VLALTATATPRvradiAEQLGLE--DPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPG 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 441 DSlTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATaVA-ARGLDISNVKHVINFDLP 519
Cdd:COG0514 231 GS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLP 308
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 87196351 520 SDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLD 558
Cdd:COG0514 309 KSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
179-393 1.27e-18

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 85.46  E-value: 1.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 179 IESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSqiysdgpgealramke 256
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMlaDPPQNLIAQSQSGTGKTAAFVLAMLS---------------- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 257 ngRYGRRKQYPISLVLAPTRELAVQ---IYEEARKFSYRSRV----RPCVVYGGADIGQQIrdlergchlLVATPGRLVD 329
Cdd:cd18048  81 --RVDALKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQViyaiRGNRPGKGTDIEAQI---------VIGTPGTVLD 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196351 330 MMERGK-IGLDFCKYLVLDEADRMLDM-GFEPQIRRIveQDTMPPKGvrHTMMFSATFPKEIQMLA 393
Cdd:cd18048 150 WCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKEC--QMLLFSATFEDSVWAFA 211
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
423-534 2.05e-15

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 80.16  E-value: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 423 EESDKRSFLLDLLN---ATGKDSLTLVFVETKKGADSLEDFLYHEGYACT------SIHGDR--SQRDREEALHQFRSGK 491
Cdd:COG1111 332 IEHPKLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGE 411
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 87196351 492 SPILVATAVAARGLDISNVKHVINFDL-PSDIeEYVHRIGRTGR 534
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
431-531 1.22e-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: 71.47  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 431 LLDLLNAT---GKDSLTLVFVETKKGADSLEDFLYHEGYACTSI-------HGDRSQ--------RDREEALHQFRSGKS 492
Cdd:cd18802  12 LIEILREYfpkTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligRGNSSQrkrslmtqRKQKETLDKFRDGEL 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 87196351 493 PILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGR 531
Cdd:cd18802  92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
180-393 1.27e-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: 70.13  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 180 ESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPII--KEKRDLMACAQTGSGKTAAFLLPILSQIysdGPGealramken 257
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV---EPA--------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 258 grygrrKQYPISLVLAPTRELAVQ---IYEEARKFSyrsrvrPCVVYGGADIGQQirdLERGC----HLLVATPGRLVDM 330
Cdd:cd18047  69 ------NKYPQCLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDW 133
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 87196351 331 MERGK-IGLDFCKYLVLDEADRML-DMGFEPQIRRIveqDTMPPKGVRhTMMFSATFPKEIQMLA 393
Cdd:cd18047 134 CSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNCQ-MLLFSATFEDSVWKFA 194
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
222-384 1.39e-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: 68.58  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 222 ACAQTGSGKTAAFLLPILSQIYSDGPGealramkengrygrrkqypiSLVLAPTRELAVQIYEEARK-FSYRSRVRpcVV 300
Cdd:cd00046   6 ITAPTGSGKTLAALLAALLLLLKKGKK--------------------VLVLVPTKALALQTAERLRElFGPGIRVA--VL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 301 YGGADIGQQIRDLERGCHLLVATPGRLVDMMER-GKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpPKGVRhTM 379
Cdd:cd00046  64 VGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG-LKNAQ-VI 141

                ....*
gi 87196351 380 MFSAT 384
Cdd:cd00046 142 LLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
428-530 2.38e-12

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: 64.42  E-value: 2.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 428 RSFLLDLLNATGKdslTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--ILVATAVAARGL 505
Cdd:cd18793  17 LELLEELREPGEK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGL 93
                        90       100       110
                ....*....|....*....|....*....|.
gi 87196351 506 DISNVKHVINFDL---PSDIE---EYVHRIG 530
Cdd:cd18793  94 NLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
422-536 6.10e-12

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: 63.38  E-value: 6.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 422 VEESDKRSFLLDLLNATGKDSL---TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVAT 498
Cdd:cd18794   8 VRPKDKKDEKLDLLKRIKVEHLggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 87196351 499 AVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 536
Cdd:cd18794  88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
201-541 2.28e-11

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: 67.17  E-value: 2.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 201 TRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEAlramkengrygrrkqypisLVLAPTRELAV 280
Cdd:COG1205  55 ERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------------------LYLYPTKALAR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 281 QIYEEARKF--SYRSRVRPCVVYGgaDIGQQIRD--LERGcHLLVATPgrlvDMMERgkiGL--------DF---CKYLV 345
Cdd:COG1205 116 DQLRRLRELaeALGLGVRVATYDG--DTPPEERRwiREHP-DIVLTNP----DMLHY---GLlphhtrwaRFfrnLRYVV 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 346 LDEA---------------DRMldmgfepqiRRIVEQdtmppKGVRHTMMF-SATF--PKEiqmLARDFLDEYiFLAVGR 407
Cdd:COG1205 186 IDEAhtyrgvfgshvanvlRRL---------RRICRH-----YGSDPQFILaSATIgnPAE---HAERLTGRP-VTVVDE 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 408 VGSTSENITQkVVW----VEESDKRSFLLD----LLNATGKDSLTLVFVETKKGA----DSLEDFLYHEGYAcTSIHGDR 475
Cdd:COG1205 248 DGSPRGERTF-VLWnpplVDDGIRRSALAEaarlLADLVREGLRTLVFTRSRRGAellaRYARRALREPDLA-DRVAAYR 325
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 476 SQ---RDREEALHQFRSGKSPILVAT-AVAArGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLA 541
Cdd:COG1205 326 AGylpEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
476-534 1.05e-09

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 57.37  E-value: 1.05e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 476 SQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 534
Cdd:cd18801  75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
418-535 1.63e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.01  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 418 KVVWVEEsdkrsFLLDLLNATGKdslTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSP--IL 495
Cdd:COG0553 534 KLEALLE-----LLEELLAEGEK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFL 605
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 87196351 496 VATAVAARGLDISNVKHVINFDLP--SDIEEY----VHRIGRTGRV 535
Cdd:COG0553 606 ISLKAGGEGLNLTAADHVIHYDLWwnPAVEEQaidrAHRIGQTRDV 651
PRK13766 PRK13766
Hef nuclease; Provisional
431-534 3.20e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 60.27  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  431 LLDLLNAT---GKDSLTLVFVETKKGADSLEDFLYHEGYAC------TSIHGDR--SQRDREEALHQFRSGKSPILVATA 499
Cdd:PRK13766 352 LREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 87196351  500 VAARGLDISNVKHVINFD-LPSDIeEYVHRIGRTGR 534
Cdd:PRK13766 432 VAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
494-534 2.21e-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: 51.55  E-value: 2.21e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 87196351 494 ILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGR 534
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
202-384 2.25e-08

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: 54.34  E-value: 2.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 202 RPTPVQKHAIPII------KEKRDLMACAQTGSGKTAAFLLPILSQiysdgpgealramkengrYGRRKQypiSLVLAPT 275
Cdd:cd17918  15 SLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGAALLA------------------YKNGKQ---VAILVPT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 276 RELAVQIYEEARKfsYRSRVRPCVVYGG--ADIGQQIrDLERGCHLLVAtpgrlvdmMERGKIGLDFckyLVLDEADRMl 353
Cdd:cd17918  74 EILAHQHYEEARK--FLPFINVELVTGGtkAQILSGI-SLLVGTHALLH--------LDVKFKNLDL---VIVDEQHRF- 138
                       170       180       190
                ....*....|....*....|....*....|.
gi 87196351 354 dmgfepqirRIVEQDTMPPKGVRHTMMFSAT 384
Cdd:cd17918 139 ---------GVAQREALYNLGATHFLEATAT 160
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
204-349 2.56e-08

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 56.83  E-value: 2.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 204 TPVQKHAIP-IIKEKRDLMACAQTGSGKTAafllpiLSQIYsdgpgeALRAMKENGRygrrkqypiSLVLAPTRELAVQI 282
Cdd:COG1204  24 YPPQAEALEaGLLEGKNLVVSAPTASGKTL------IAELA------ILKALLNGGK---------ALYIVPLRALASEK 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 283 YEEARKFSYRSRVRPCVVYGGADIGqqIRDLERgCHLLVATPGRLvDMMERGKIGL--DFcKYLVLDEA 349
Cdd:COG1204  83 YREFKRDFEELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSWlrDV-DLVVVDEA 146
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
207-349 1.49e-07

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: 51.82  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 207 QKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDgpgealramkengrYGRRkqypiSLVLAPTRELAVQIYEEA 286
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD--------------PGSR-----ALYLYPTKALAQDQLRSL 65
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87196351 287 RKF--SYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPgrlvDMME-----RGKIGLDFC---KYLVLDEA 349
Cdd:cd17923  66 RELleQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallpHHDRWARFLrnlRYVVLDEA 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
199-252 1.83e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.34  E-value: 1.83e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 87196351 199 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKT-AAFlLPILSQIYSDGPGEALR 252
Cdd:COG1201  21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELP 74
PRK13767 PRK13767
ATP-dependent helicase; Provisional
199-324 7.12e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 52.58  E-value: 7.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  199 RYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALramkENGRYgrrkqypiSLVLAPTREL 278
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGEL----EDKVY--------CLYVSPLRAL 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 87196351  279 A-----------VQIYEEARKFSYR-SRVRPCVVYGGADIGQQIRDLERGCHLLVATP 324
Cdd:PRK13767  97 NndihrnleeplTEIREIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
217-349 1.84e-06

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: 49.19  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 217 KRDLMACAQTGSGKT--AAFLLPILSQIysdgpgeaLRAMKENGRygrrkqypISLVLAPTRELAVQIYEEARKFSYrSR 294
Cdd:cd18034  16 KRNTIVVLPTGSGKTliAVMLIKEMGEL--------NRKEKNPKK--------RAVFLVPTVPLVAQQAEAIRSHTD-LK 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 295 VRPCvvYGGADIGQQIRDLERGC----HLLVATPGRLVDMMERGKIGLDFCKYLVLDEA 349
Cdd:cd18034  79 VGEY--SGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
208-385 3.15e-06

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.30  E-value: 3.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 208 KHAIPIIKEKRDLMACAQTGSGKTAAfllpilsqiysdgpgeALRAMKEngrygrRKQYPIsLVLAPTRELAVQIYEEAR 287
Cdd:cd17926   9 LEAWLAHKNNRRGILVLPTGSGKTLT----------------ALALIAY------LKELRT-LIVVPTDALLDQWKERFE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 288 KFSYRSRVrpCVVYGGADIGQqirdleRGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRmldmGFEPQIRRIVEQ 367
Cdd:cd17926  66 DFLGDSSI--GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKE 133
                       170
                ....*....|....*...
gi 87196351 368 DTMPPKgvrhtMMFSATF 385
Cdd:cd17926 134 LNAKYR-----LGLTATP 146
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
204-349 3.35e-06

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: 48.03  E-value: 3.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 204 TPVQKHAI-PIIKEKRDLMACAQTGSGKTAAFLLPIlsqiysdgpgeaLRAMKENGRygrrkqypISLVLAPTRELAVQI 282
Cdd:cd17921   3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAI------------LRALATSGG--------KAVYIAPTRALVNQK 62
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 87196351 283 YEEARKFSYRSRVRPCVVYGGADIGqqiRDLERGCHLLVATPGRLVDMMERGKIGLDF-CKYLVLDEA 349
Cdd:cd17921  63 EADLRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEA 127
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
344-536 3.80e-05

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: 46.29  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   344 LVLDEADRMLDmgfEPQIRRIVEQDTMPPKGVRHTMMfSATFPKEIQMLARDFldEYIFLAVGRVGSTSENITQKVVWVE 423
Cdd:TIGR01587 128 LIFDEVHFYDE---YTLALILAVLEVLKDNDVPILLM-SATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENHRFILI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   424 ESDKR---SFLLDLLNATGKDSLTLVFVET-----------KKGADSLEDFLYHEGYActsiHGDRSQRDREEALHQFRS 489
Cdd:TIGR01587 202 ESDKVgeiSSLERLLEFIKKGGSIAIIVNTvdraqefyqqlKEKAPEEEIILYHSRFT----EKDRAKKEAELLREMKKS 277
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 87196351   490 GKSPILVATAVAARGLDISnvkhvinFDL----PSDIEEYVHRIGRTGRVG 536
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDIS-------ADVmiteLAPIDSLIQRLGRLHRYG 321
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
444-534 8.70e-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: 43.02  E-value: 8.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 444 TLVFVETKKGADSLED---FLYHEGYACTSI---HG--DRSQRDR-EEALhqfRSGKSPILVATAVAARGLDISNVKHVI 514
Cdd:cd18796  41 TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLELGIDIGDVDLVI 117
                        90       100
                ....*....|....*....|
gi 87196351 515 NFDLPSDIEEYVHRIGRTGR 534
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGH 137
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
471-536 1.24e-04

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: 42.72  E-value: 1.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 471 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 536
Cdd:cd18810  57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGL-AQLYQLRGRVGRSKERA 126
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
462-536 1.25e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.09  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 87196351  462 YHEGYactsihgDRSQRDR-EEAlhqFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVG 536
Cdd:PRK11057 266 YHAGL-------DNDVRADvQEA---FQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
444-531 1.73e-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: 41.39  E-value: 1.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 444 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDRE-EALHQFRSGKS--PILVATAVAARGLDISNVKHVInFDLP- 519
Cdd:cd18799   9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                        90
                ....*....|...
gi 87196351 520 -SDIeEYVHRIGR 531
Cdd:cd18799  88 eSRT-LFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
471-545 2.86e-04

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 41.85  E-value: 2.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87196351 471 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDI--SNVKHVINFDLPSDiEEYVHRIGRTGRVGNLGLATSFF 545
Cdd:cd18789  74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
217-351 5.19e-04

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 41.35  E-value: 5.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 217 KRDLMACAQTGSGKTAAFLLPILSqiysdgpgealRAMKENGRYgrrkqypisLVLAPTRELAVQIYEEARKFsyRSRVR 296
Cdd:cd18035  16 NGNTLIVLPTGLGKTIIAILVAAD-----------RLTKKGGKV---------LILAPSRPLVEQHAENLKRV--LNIPD 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 87196351 297 PCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADR 351
Cdd:cd18035  74 KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
470-579 5.23e-04

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 43.37  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   470 SIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTG-RVGnlGLATSFFNER 548
Cdd:PRK09751  306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPR 383
                          90       100       110
                  ....*....|....*....|....*....|.
gi 87196351   549 NiniTKDLLDLLVEAKQEVPSWLENMAYEHH 579
Cdd:PRK09751  384 T---RRDLVDSAVIVECMFAGRLENLTPPHN 411
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
471-536 8.32e-04

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: 40.33  E-value: 8.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 471 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVI-----NFDLpSDIEEYVHRIGRTGRVG 536
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGL-SQLHQLRGRVGRGKHQS 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
422-535 1.17e-03

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 42.10  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351   422 VEESDKRSFLLDLL-NATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFR---SGKSPILVA 497
Cdd:PLN03142  467 VENSGKMVLLDKLLpKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLS 546
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 87196351   498 TAVAARGLDISNVKHVINFDlpSD--------IEEYVHRIGRTGRV 535
Cdd:PLN03142  547 TRAGGLGINLATADIVILYD--SDwnpqvdlqAQDRAHRIGQKKEV 590
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
218-348 1.62e-03

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.87  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 218 RDLMACAQTGSGKTAAFLLPILSQIYsDGPGEALRAMkengrYgrrkqypISlvlaPTRELAVQIYE------EARKFSY 291
Cdd:cd17922   2 RNVLIAAPTGSGKTEAAFLPALSSLA-DEPEKGVQVL-----Y-------IS----PLKALINDQERrleeplDEIDLEI 64
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 87196351 292 RSRVRpcvvYGgaDIGQQIRD--LERGCHLLVATPGRLVDMMERGKIGLDF--CKYLVLDE 348
Cdd:cd17922  65 PVAVR----HG--DTSQSEKAkqLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDE 119
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
422-500 2.84e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.80  E-value: 2.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 87196351 422 VEESDKrsflLDLLNATgkdsltlvfvetkKGADSLEDFLyhEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAV 500
Cdd:COG1200 479 IEESEK----LDLQAAE-------------ETYEELREAF--PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
471-534 3.45e-03

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: 38.48  E-value: 3.45e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 471 IHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISN-----VKHVINFDLPSdieeyVHRI-GRTGR 534
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGR 131
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
422-500 4.02e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 40.52  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351  422 VEESDKrsflLDLLNAT-GKDSLTLVFVETKKGadsledfLyhegyactsIHGDRSQRDREEALHQFRSGKSPILVATAV 500
Cdd:PRK10917 481 IEESEK----LDLQSAEeTYEELQEAFPELRVG-------L---------LHGRMKPAEKDAVMAAFKAGEIDILVATTV 540
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
206-333 4.75e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 38.88  E-value: 4.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 206 VQKHAIP-IIKEKRDLMACAQTGSGKTAAFLLPILsqiysdgpgEALRAMKENGRYGRRKQYpislvLAPTRELAVQIYE 284
Cdd:cd18023   5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAIL---------RLLKERNPLPWGNRKVVY-----IAPIKALCSEKYD 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 87196351 285 EAR-KFsyrSRVRPCVVYGGADigQQIRDLE--RGCHLLVATPGRLvDMMER 333
Cdd:cd18023  71 DWKeKF---GPLGLSCAELTGD--TEMDDTFeiQDADIILTTPEKW-DSMTR 116
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
444-534 5.33e-03

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 38.38  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87196351 444 TLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDlpSDIE 523
Cdd:cd18790  30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107
                        90
                ....*....|....*...
gi 87196351 524 EY-------VHRIGRTGR 534
Cdd:cd18790 108 GFlrsetslIQTIGRAAR 125
 
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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