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Conserved domains on  [gi|1398331558|ref|NP_001351092|]
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ATP-dependent RNA helicase DDX24 isoform 2 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028649)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
204-552 3.04e-118

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: 358.09  E-value: 3.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQWhkmkappiprstgmppremrfgat 283
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdA 363
Cdd:cd17946    57 -------------------------------------------------------------------------------K 57
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 EQAGKLKqelcdqiaiykvhPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17946    58 SSNGVGG-------------KQKPLRALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVA 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 444 TPGRLWELVKEKHPHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQ--YNPSRQTLVFSATLTLVHQAPARIL 521
Cdd:cd17946   125 TPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEKGHFAELEKILELLNKDRagKKRKRQTFVFSATLTLDHQLPLKLN 204
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1398331558 522 HKKHVKKMDKTDKLDLLMQKVGMRGKPKVID 552
Cdd:cd17946   205 SKKKKKKKEKKQKLELLIEKVGFRKKPKVID 235
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
563-691 5.11e-45

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: 158.05  E-value: 5.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 563 LTETKIHCETDEKDLYLYYFLMQ--YPGRSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCV 640
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEklKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 641 LLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLI 691
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
204-552 3.04e-118

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: 358.09  E-value: 3.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQWhkmkappiprstgmppremrfgat 283
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdA 363
Cdd:cd17946    57 -------------------------------------------------------------------------------K 57
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 EQAGKLKqelcdqiaiykvhPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17946    58 SSNGVGG-------------KQKPLRALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVA 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 444 TPGRLWELVKEKHPHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQ--YNPSRQTLVFSATLTLVHQAPARIL 521
Cdd:cd17946   125 TPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEKGHFAELEKILELLNKDRagKKRKRQTFVFSATLTLDHQLPLKLN 204
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1398331558 522 HKKHVKKMDKTDKLDLLMQKVGMRGKPKVID 552
Cdd:cd17946   205 SKKKKKKKEKKQKLELLIEKVGFRKKPKVID 235
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
197-730 2.23e-92

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 297.44  E-value: 2.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 197 DLFVPKAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHsvlqwhkmkappiprstgmppr 276
Cdd:COG0513     6 DLGLSPPLLKALAELGYTTPTPIQAQAI-PLILAGRDVLGQAQTGTGKTAAFLLPLLQ---------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 277 emrfgatahlgspckdrtesgvlpeeaRIETEAQPsdsGVQAtpetsasasaqtllvcdddagegpssleekpvpkqned 356
Cdd:COG0513    63 ---------------------------RLDPSRPR---APQA-------------------------------------- 74
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 357 geekfdaeqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNR 436
Cdd:COG0513    75 ----------------------------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKR 120
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 437 HPEIVIATPGRLWELVKEKHphLsNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNdsqynPSRQTLVFSATLtlvhqa 516
Cdd:COG0513   121 GVDIVVATPGRLLDLIERGA--L-DLSGVETLVLDEADRMLDMGFIEDIERILKLLP-----KERQTLLFSATM------ 186
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 517 PARIlhKKHVKKMdktdkldllmqkvgMRgKPKVIDLTRNEGTVETLTETKIHCETDEKDLYLYYFLMQY-PGRSLVFAN 595
Cdd:COG0513   187 PPEI--RKLAKRY--------------LK-NPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEdPERAIVFCN 249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 596 SISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRS 675
Cdd:COG0513   250 TKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRI 329
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398331558 676 GRTARAASEGLSLMLIGPEDVINFKKIYKTLQKD---EDIPLF-PVQSKYMDVVKERIR 730
Cdd:COG0513   330 GRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKieeEELPGFePVEEKRLERLKPKIK 388
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
205-702 5.77e-48

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 176.67  E-value: 5.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 205 LRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQWhkmkappiPRSTGMPPREmrfgata 284
Cdd:PRK11192   13 LEALQDKGYTRPTAIQAEAIPPALDGR-DVLGSAPTGTGKTAAFLLPALQHLLDF--------PRRKSGPPRI------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 285 hlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdae 364
Cdd:PRK11192      --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 365 qagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIAT 444
Cdd:PRK11192   77 --------------------------LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVAT 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 445 PGRLWELVKEKHphlSNLRQLRCLVIDEADRMVEKGhFAELSQllEMLNDSQYNpsRQTLVFSATltlvhqapariLHKK 524
Cdd:PRK11192  131 PGRLLQYIKEEN---FDCRAVETLILDEADRMLDMG-FAQDIE--TIAAETRWR--KQTLLFSAT-----------LEGD 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 525 HVKKMDKtdklDLLMQKVGMRGKPkvidlTRNEgtvetltETKIH-----CETDEKDLYLYYFLMQYP--GRSLVFANSI 597
Cdd:PRK11192  192 AVQDFAE----RLLNDPVEVEAEP-----SRRE-------RKKIHqwyyrADDLEHKTALLCHLLKQPevTRSIVFVRTR 255
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 598 SCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGR 677
Cdd:PRK11192  256 ERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGR 335
                         490       500
                  ....*....|....*....|....*
gi 1398331558 678 TARAASEGLSLMLIGPEDVINFKKI 702
Cdd:PRK11192  336 TGRAGRKGTAISLVEAHDHLLLGKI 360
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
563-691 5.11e-45

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: 158.05  E-value: 5.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 563 LTETKIHCETDEKDLYLYYFLMQ--YPGRSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCV 640
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEklKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 641 LLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLI 691
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
217-511 5.04e-29

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: 113.88  E-value: 5.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 217 TPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVlqwhkmkappiprstgmppremrfgatahlgspckdrtes 296
Cdd:pfam00270   1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEAL---------------------------------------- 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 297 gvlpeearieteaQPSDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdaeqagklkqelcdq 376
Cdd:pfam00270  40 -------------DKLDNGPQA---------------------------------------------------------- 48
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 377 iaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLnRHPEIVIATPGRLWELVKEKH 456
Cdd:pfam00270  49 --------------LVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK 113
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 457 phlsNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:pfam00270 114 ----LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL-----PKKRQILLLSATLP 159
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
574-681 5.93e-25

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: 99.98  E-value: 5.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 574 EKDLYLYYFLMQYPG-RSLVFANSISCIKrLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLD 652
Cdd:pfam00271   1 EKLEALLELLKKERGgKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*....
gi 1398331558 653 IPKVQHVIHYQVPRTSEIYIHRSGRTARA 681
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRA 108
DEXDc smart00487
DEAD-like helicases superfamily;
376-511 4.48e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 4.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558  376 QIAIYKVHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQ-QRMLNRHPEIVIATPGRLWELVKE 454
Cdd:smart00487  43 LPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLEN 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398331558  455 KHPHLSNlrqLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:smart00487 123 DKLSLSN---VDLVILDEAHRLLDGGFGDQLEKLLKLL-----PKNVQLLLLSATPP 171
HELICc smart00490
helicase superfamily c-terminal domain;
601-681 2.79e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558  601 KRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTAR 680
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   .
gi 1398331558  681 A 681
Cdd:smart00490  81 A 81
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
621-683 6.67e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 59.74  E-value: 6.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 621 MHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQ-VPrtSEI-YIHRSGRTARAAS 683
Cdd:COG1111   395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVP--SEIrSIQRKGRTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
621-683 3.67e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.19  E-value: 3.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 621 MHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQ-VPrtSEI-YIHRSGRTARAAS 683
Cdd:PRK13766  407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVP--SEIrSIQRKGRTGRQEE 469
 
Name Accession Description Interval E-value
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
204-552 3.04e-118

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: 358.09  E-value: 3.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQWhkmkappiprstgmppremrfgat 283
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdA 363
Cdd:cd17946    57 -------------------------------------------------------------------------------K 57
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 EQAGKLKqelcdqiaiykvhPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17946    58 SSNGVGG-------------KQKPLRALILTPTRELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVA 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 444 TPGRLWELVKEKHPHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQ--YNPSRQTLVFSATLTLVHQAPARIL 521
Cdd:cd17946   125 TPGRLWELIQEGNEHLANLKSLRFLVLDEADRMLEKGHFAELEKILELLNKDRagKKRKRQTFVFSATLTLDHQLPLKLN 204
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1398331558 522 HKKHVKKMDKTDKLDLLMQKVGMRGKPKVID 552
Cdd:cd17946   205 SKKKKKKKEKKQKLELLIEKVGFRKKPKVID 235
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
197-730 2.23e-92

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 297.44  E-value: 2.23e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 197 DLFVPKAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHsvlqwhkmkappiprstgmppr 276
Cdd:COG0513     6 DLGLSPPLLKALAELGYTTPTPIQAQAI-PLILAGRDVLGQAQTGTGKTAAFLLPLLQ---------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 277 emrfgatahlgspckdrtesgvlpeeaRIETEAQPsdsGVQAtpetsasasaqtllvcdddagegpssleekpvpkqned 356
Cdd:COG0513    63 ---------------------------RLDPSRPR---APQA-------------------------------------- 74
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 357 geekfdaeqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNR 436
Cdd:COG0513    75 ----------------------------------LILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKR 120
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 437 HPEIVIATPGRLWELVKEKHphLsNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNdsqynPSRQTLVFSATLtlvhqa 516
Cdd:COG0513   121 GVDIVVATPGRLLDLIERGA--L-DLSGVETLVLDEADRMLDMGFIEDIERILKLLP-----KERQTLLFSATM------ 186
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 517 PARIlhKKHVKKMdktdkldllmqkvgMRgKPKVIDLTRNEGTVETLTETKIHCETDEKDLYLYYFLMQY-PGRSLVFAN 595
Cdd:COG0513   187 PPEI--RKLAKRY--------------LK-NPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEdPERAIVFCN 249
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 596 SISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRS 675
Cdd:COG0513   250 TKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRI 329
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1398331558 676 GRTARAASEGLSLMLIGPEDVINFKKIYKTLQKD---EDIPLF-PVQSKYMDVVKERIR 730
Cdd:COG0513   330 GRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKieeEELPGFePVEEKRLERLKPKIK 388
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
204-511 1.02e-51

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: 179.17  E-value: 1.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHsvlqwhkmkappiprstgmppremrfgat 283
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAI-PLILSGRDVIGQAQTGSGKTLAFLLPILE----------------------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeeaRIETEAQPSDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfda 363
Cdd:cd00268    51 --------------------KLLPEPKKKGRGPQA--------------------------------------------- 65
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd00268    66 ---------------------------LVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVG 118
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398331558 444 TPGRLWELVKEKHPHLSNlrqLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:cd00268   119 TPGRLLDLIERGKLDLSN---VKYLVLDEADRMLDMGFEEDVEKILSAL-----PKDRQTLLFSATLP 178
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
205-702 5.77e-48

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 176.67  E-value: 5.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 205 LRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQWhkmkappiPRSTGMPPREmrfgata 284
Cdd:PRK11192   13 LEALQDKGYTRPTAIQAEAIPPALDGR-DVLGSAPTGTGKTAAFLLPALQHLLDF--------PRRKSGPPRI------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 285 hlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdae 364
Cdd:PRK11192      --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 365 qagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIAT 444
Cdd:PRK11192   77 --------------------------LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVAT 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 445 PGRLWELVKEKHphlSNLRQLRCLVIDEADRMVEKGhFAELSQllEMLNDSQYNpsRQTLVFSATltlvhqapariLHKK 524
Cdd:PRK11192  131 PGRLLQYIKEEN---FDCRAVETLILDEADRMLDMG-FAQDIE--TIAAETRWR--KQTLLFSAT-----------LEGD 191
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 525 HVKKMDKtdklDLLMQKVGMRGKPkvidlTRNEgtvetltETKIH-----CETDEKDLYLYYFLMQYP--GRSLVFANSI 597
Cdd:PRK11192  192 AVQDFAE----RLLNDPVEVEAEP-----SRRE-------RKKIHqwyyrADDLEHKTALLCHLLKQPevTRSIVFVRTR 255
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 598 SCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGR 677
Cdd:PRK11192  256 ERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGR 335
                         490       500
                  ....*....|....*....|....*
gi 1398331558 678 TARAASEGLSLMLIGPEDVINFKKI 702
Cdd:PRK11192  336 TGRAGRKGTAISLVEAHDHLLLGKI 360
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
201-695 7.31e-47

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 174.22  E-value: 7.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 201 PKAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVlqwhkmkappiprstgmppremrf 280
Cdd:PRK11776   12 PPALLANLNELGYTEMTPIQAQSL-PAILAGKDVIAQAKTGSGKTAAFGLGLLQKL------------------------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 281 gatahlgspckdrtesgvlpeearieteaQPSDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeek 360
Cdd:PRK11776   67 -----------------------------DVKRFRVQA------------------------------------------ 75
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 361 fdaeqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGiNTAILV--GGMSTQKQQRMLNRHP 438
Cdd:PRK11776   76 ------------------------------LVLCPTRELADQVAKEIRRLARFIP-NIKVLTlcGGVPMGPQIDSLEHGA 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 439 EIVIATPGRLWElvkekhpHLS----NLRQLRCLVIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSATLtlvh 514
Cdd:PRK11776  125 HIIVGTPGRILD-------HLRkgtlDLDALNTLVLDEADRMLDMGFQDAIDAII-----RQAPARRQTLLFSATY---- 188
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 515 qaPARILHkkhvkkmdktdkldlLMQKVgMRgKPKVIdltrnegTVETLTE-TKI-----HCETDEKDLYLYYFLMQY-P 587
Cdd:PRK11776  189 --PEGIAA---------------ISQRF-QR-DPVEV-------KVESTHDlPAIeqrfyEVSPDERLPALQRLLLHHqP 242
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 588 GRSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRT 667
Cdd:PRK11776  243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
                         490       500
                  ....*....|....*....|....*...
gi 1398331558 668 SEIYIHRSGRTARAASEGLSLMLIGPED 695
Cdd:PRK11776  323 PEVHVHRIGRTGRAGSKGLALSLVAPEE 350
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
563-691 5.11e-45

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: 158.05  E-value: 5.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 563 LTETKIHCETDEKDLYLYYFLMQ--YPGRSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCV 640
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEklKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 641 LLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLI 691
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
193-708 2.50e-43

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 164.32  E-value: 2.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 193 SAWRDLFVPKAVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQwhkmkappiprstg 272
Cdd:PRK01297   87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGH-DAIGRAQTGTGKTAAFLISIINQLLQ-------------- 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 273 mppremrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleeKPVPK 352
Cdd:PRK01297  152 ---------------------------------------------------------------------------TPPPK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 353 QNEDGEekfdaeqagklkqelcdqiaiykvhPRrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQR 432
Cdd:PRK01297  157 ERYMGE-------------------------PR----ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLK 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 433 MLN-RHPEIVIATPGRLWELVKEKHPHLSnlrQLRCLVIDEADRMVEKGHFAELSQLLEMlndSQYNPSRQTLVFSATLT 511
Cdd:PRK01297  208 QLEaRFCDILVATPGRLLDFNQRGEVHLD---MVEVMVLDEADRMLDMGFIPQVRQIIRQ---TPRKEERQTLLFSATFT 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 512 lvhqaparilhkkhvkkmdkTDKLDLLMQKVgmrGKPKVIDLTRNEGTVETLTETKIHCETDEKDLYLYYFLMQYP-GRS 590
Cdd:PRK01297  282 --------------------DDVMNLAKQWT---TDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPwERV 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 591 LVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEI 670
Cdd:PRK01297  339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1398331558 671 YIHRSGRTARAASEGLSLMLIGPEDVINFKKIYKTLQK 708
Cdd:PRK01297  419 YVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGR 456
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
197-702 1.48e-41

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 157.83  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 197 DLFVPKAVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQwhkmkappiprstgmppr 276
Cdd:PRK04837   12 DFALHPQVVEALEKKGFHNCTPIQALALPLTLAGR-DVAGQAQTGTGKTMAFLTATFHYLLS------------------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 277 emrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleeKPVPKQNEd 356
Cdd:PRK04837   73 -----------------------------------------------------------------------HPAPEDRK- 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 357 geekfdaeqagklkqelcdqiaiyKVHPRrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNR 436
Cdd:PRK04837   81 ------------------------VNQPR----ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLES 132
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 437 HPEIVIATPGRLWELVKEKHPHLSNLRqlrCLVIDEADRMVEKGHFAELSQLLEMLNDSQynpSRQTLVFSATLTLVHQA 516
Cdd:PRK04837  133 GVDILIGTTGRLIDYAKQNHINLGAIQ---VVVLDEADRMFDLGFIKDIRWLFRRMPPAN---QRLNMLFSATLSYRVRE 206
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 517 PArilhkkhVKKMDKTDKLDLL-MQKVGMRgkpkvidltrnegtvetLTETKIHCETDEKDLYLYYFLMQ-YPGRSLVFA 594
Cdd:PRK04837  207 LA-------FEHMNNPEYVEVEpEQKTGHR-----------------IKEELFYPSNEEKMRLLQTLIEEeWPDRAIIFA 262
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 595 NSI-SCIKRLS---------GLLKVlDVMpltlhacmhQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQV 664
Cdd:PRK04837  263 NTKhRCEEIWGhlaadghrvGLLTG-DVA---------QKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1398331558 665 PRTSEIYIHRSGRTARAASEGLSLMLIGPEDVINFKKI 702
Cdd:PRK04837  333 PDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAI 370
PTZ00110 PTZ00110
helicase; Provisional
201-694 4.64e-40

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 156.09  E-value: 4.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 201 PKAVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIP-MIHsvlqwhkmkappiprstgmppremr 279
Cdd:PTZ00110  138 PDYILKSLKNAGFTEPTPIQVQGWPIALSGR-DMIGIAETGSGKTLAFLLPaIVH------------------------- 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 280 fgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasASAQTLLvcddDAGEGPssleekpvpkqnedgee 359
Cdd:PTZ00110  192 ----------------------------------------------INAQPLL----RYGDGP----------------- 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 360 kfdaeqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPE 439
Cdd:PTZ00110  205 -----------------------------IVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 440 IVIATPGRLWELVKEKhphLSNLRQLRCLVIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSATLTLVHQAPAR 519
Cdd:PTZ00110  256 ILIACPGRLIDFLESN---VTNLRRVTYLVLDEADRMLDMGFEPQIRKIV-----SQIRPDRQTLMWSATWPKEVQSLAR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 520 ILHKKHVKKMDktdkldllmqkVGMrgkpkvIDLTrnegTVETLTETKIHCETDEKDLYLYYFL---MQYPGRSLVFANS 596
Cdd:PTZ00110  328 DLCKEEPVHVN-----------VGS------LDLT----ACHNIKQEVFVVEEHEKRGKLKMLLqriMRDGDKILIFVET 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 597 ISCIKRLSGLLKvLDVMP-LTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRS 675
Cdd:PTZ00110  387 KKGADFLTKELR-LDGWPaLCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
                         490
                  ....*....|....*....
gi 1398331558 676 GRTARAASEGLSLMLIGPE 694
Cdd:PTZ00110  466 GRTGRAGAKGASYTFLTPD 484
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
195-511 5.32e-38

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: 140.91  E-value: 5.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 195 WRDLFVPKAVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLqwhkmkappiprstgmp 274
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGR-DIIGLAETGSGKTAAFALPILQALL----------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 275 premrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqn 354
Cdd:cd17954       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 355 edgeekfdaeqagklkqelcdqiaiykvHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRML 434
Cdd:cd17954    64 ----------------------------ENPQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIAL 115
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 435 NRHPEIVIATPGRLWElvkekhpHLSN-----LRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqynPS-RQTLVFSA 508
Cdd:cd17954   116 AKKPHVIVATPGRLVD-------HLENtkgfsLKSLKFLVMDEADRLLNMDFEPEIDKILKVI------PReRTTYLFSA 182

                  ...
gi 1398331558 509 TLT 511
Cdd:cd17954   183 TMT 185
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
203-739 1.30e-37

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 149.33  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 203 AVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQwhkmkappiprstgmppremrfga 282
Cdd:PRK04537   19 ALLAGLESAGFTRCTPIQALTLPVALPGG-DVAGQAQTGTGKTLAFLVAVMNRLLS------------------------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 283 tahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddageGPSSLEEKPvpkqnEDgeekfd 362
Cdd:PRK04537   74 ----------------------------------------------------------RPALADRKP-----ED------ 84
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 363 aeqagklkqelcdqiaiykvhPRrpllGLVLTPTRELAIQVrqHIDAVaKF---TGINTAILVGGMSTQKQQRMLNRHPE 439
Cdd:PRK04537   85 ---------------------PR----ALILAPTRELAIQI--HKDAV-KFgadLGLRFALVYGGVDYDKQRELLQQGVD 136
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 440 IVIATPGRLWELVKEkHPHLSnLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDsqyNPSRQTLVFSATLTlvHqapaR 519
Cdd:PRK04537  137 VIIATPGRLIDYVKQ-HKVVS-LHACEICVLDEADRMFDLGFIKDIRFLLRRMPE---RGTRQTLLFSATLS--H----R 205
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 520 ILHKKHvKKMDKTDKLdllmqkvgmrgkpkvidLTRNEGTVETLTETKIHCETDEKDLYLYYFLMQYP--GRSLVFANSI 597
Cdd:PRK04537  206 VLELAY-EHMNEPEKL-----------------VVETETITAARVRQRIYFPADEEKQTLLLGLLSRSegARTMVFVNTK 267
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 598 SCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGR 677
Cdd:PRK04537  268 AFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGR 347
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398331558 678 TARAASEGLSLMLIGPEDVINFKKIYKTLQkdEDIPLFPVQSKYMDVVKERIRLARQIEKAE 739
Cdd:PRK04537  348 TARLGEEGDAISFACERYAMSLPDIEAYIE--QKIPVEPVTAELLTPLPRPPRVPVEGEEAD 407
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
204-511 1.16e-36

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: 136.62  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLqwHKMKAPPIPRstgmppremrfgat 283
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGK-DICASAVTGSGKTAAFLLPILERLL--YRPKKKAATR-------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfda 363
Cdd:cd17947       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17947    64 --------------------------VLVLVPTRELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIA 117
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398331558 444 TPGRLWELVkekHPHLS-NLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDsqynpSRQTLVFSATLT 511
Cdd:cd17947   118 TPGRLIDHL---RNSPSfDLDSIEILVLDEADRMLEEGFADELKEILRLCPR-----TRQTMLFSATMT 178
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
385-713 3.84e-36

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 142.64  E-value: 3.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 385 RRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELvkeKHPHLSNLRQ 464
Cdd:PRK10590   73 RRPVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDL---EHQNAVKLDQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 465 LRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLTLVHQAPA-RILHK-----------------KHV 526
Cdd:PRK10590  150 VEILVLDEADRMLDMGFIHDIRRVLAKL-----PAKRQNLLFSATFSDDIKALAeKLLHNpleievarrntaseqvtQHV 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 527 KKMDKTDKLDLLMQKVGMRGKPKVIDLTRNEGTVETLTETKihcetdEKDlylyyflmqypgrslvfansiscikrlsgl 606
Cdd:PRK10590  225 HFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQL------NKD------------------------------ 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 607 lkvlDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGL 686
Cdd:PRK10590  269 ----GIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGE 344
                         330       340
                  ....*....|....*....|....*..
gi 1398331558 687 SLMLIGPEDVINFKKIYKTLQKdeDIP 713
Cdd:PRK10590  345 ALSLVCVDEHKLLRDIEKLLKK--EIP 369
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
197-511 1.87e-34

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: 130.81  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 197 DLFVPKAVLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSvlqwhkmkappiprstgmppr 276
Cdd:cd17955     3 DLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGR-DVIGGAKTGSGKTAAFALPILQR--------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 277 emrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssLEEKPVpkqned 356
Cdd:cd17955    61 --------------------------------------------------------------------LSEDPY------ 66
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 357 geekfdaeqagklkqelcdqiAIYkvhprrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNR 436
Cdd:cd17955    67 ---------------------GIF---------ALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSK 116
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 437 HPEIVIATPGRLWELVKEKHPHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:cd17955   117 RPHIVVATPGRLADHLRSSDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSAL-----PPKRQTLLFSATLT 186
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
202-510 3.45e-34

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: 130.12  E-value: 3.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 202 KAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHsvlqwhkmkappiprstgmppremrfg 281
Cdd:cd17959    10 PPLLRAIKKKGYKVPTPIQRKTI-PLILDGRDVVAMARTGSGKTAAFLIPMIE--------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 282 atahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekf 361
Cdd:cd17959       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 362 daeqagKLKQElcdqiaiykvHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIV 441
Cdd:cd17959    62 ------KLKAH----------SPTVGARALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDII 125
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398331558 442 IATPGRLWELVKEKHphlSNLRQLRCLVIDEADRMVEKGhFAElsQLLEMLndSQYNPSRQTLVFSATL 510
Cdd:cd17959   126 IATPGRLLHLLVEMN---LKLSSVEYVVFDEADRLFEMG-FAE--QLHEIL--SRLPENRQTLLFSATL 186
PTZ00424 PTZ00424
helicase 45; Provisional
340-710 1.59e-30

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 124.94  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 340 EGPSSLEEKPVpKQNEDGEEKFDAEQAGKLKQELCDQIAIYKVHPR-RPLLGLVLTPTRELAIQVRQHIDAVAKFTGINT 418
Cdd:PTZ00424   49 EKPSAIQQRGI-KPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDlNACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 419 AILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHPHLSNLRqlrCLVIDEADRMVEKGHFAELSQLLEMLNdsqyn 498
Cdd:PTZ00424  128 HACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLK---LFILDEADEMLSRGFKGQIYDVFKKLP----- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 499 PSRQTLVFSATLtlvhqaPARILHkkhvkkmdktdkldlLMQKVgMRgKPKVIDLTRNEGTVETLTETKIHCETDE---- 574
Cdd:PTZ00424  200 PDVQVALFSATM------PNEILE---------------LTTKF-MR-DPKRILVKKDELTLEGIRQFYVAVEKEEwkfd 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 575 --KDLYLYYFLMQypgrSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLD 652
Cdd:PTZ00424  257 tlCDLYETLTITQ----AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 653 IPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLIGPEDVINFKKI--YKTLQKDE 710
Cdd:PTZ00424  333 VQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIerHYNTQIEE 392
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
197-691 3.64e-30

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 126.89  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 197 DLFVPKAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQwhKMKAPPIprstgmppr 276
Cdd:PRK11634   10 DLGLKAPILEALNDLGYEKPSPIQAECI-PHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDP--ELKAPQI--------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 277 emrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqned 356
Cdd:PRK11634      --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 357 geekfdaeqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAK-FTGINTAILVGGMSTQKQQRMLN 435
Cdd:PRK11634   78 ----------------------------------LVLAPTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALR 123
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 436 RHPEIVIATPGRLWELVKEKHPHLSNLRQlrcLVIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSATLTlvhQ 515
Cdd:PRK11634  124 QGPQIVVGTPGRLLDHLKRGTLDLSKLSG---LVLDEADEMLRMGFIEDVETIM-----AQIPEGHQTALFSATMP---E 192
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 516 APARILhKKHVKkmdktDKLDLLMQKvGMRGKPkviDLTRNEGTVETLtetkihcetdEKDLYLYYFLmqypgRSLVFAN 595
Cdd:PRK11634  193 AIRRIT-RRFMK-----EPQEVRIQS-SVTTRP---DISQSYWTVWGM----------RKNEALVRFL-----EAEDFDA 247
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 596 SISCIKRLSGLLKVLDVMPLT------LHACMHQKQRLRNLEqfaRLQDC---VLLATDVAARGLDIPKVQHVIHYQVPR 666
Cdd:PRK11634  248 AIIFVRTKNATLEVAEALERNgynsaaLNGDMNQALREQTLE---RLKDGrldILIATDVAARGLDVERISLVVNYDIPM 324
                         490       500
                  ....*....|....*....|....*
gi 1398331558 667 TSEIYIHRSGRTARAASEGLSLMLI 691
Cdd:PRK11634  325 DSESYVHRIGRTGRAGRAGRALLFV 349
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
202-510 1.79e-29

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: 116.53  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 202 KAVLRALSFLGFSAPTPIQALTLAPAIRDKLDILGAAETGSGKTLAFAIPMIhsvlqwhkmkappiprstgmppremrfg 281
Cdd:cd17964     3 PSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAI---------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 282 atahlgspckdrtesgvlpeEARIETEAQPSDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeekf 361
Cdd:cd17964    55 --------------------QSLLNTKPAGRRSGVSA------------------------------------------- 71
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 362 daeqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKF-TGINTAILVGGMSTQKQ-QRMLNRHPE 439
Cdd:cd17964    72 -----------------------------LIISPTRELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAElNRLRRGRPD 122
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398331558 440 IVIATPGRLwelvkekHPHLSN------LRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQYNPsRQTLVFSATL 510
Cdd:cd17964   123 ILVATPGRL-------IDHLENpgvakaFTDLDYLVLDEADRLLDMGFRPDLEQILRHLPEKNADP-RQTLLFSATV 191
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
192-523 4.78e-29

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: 115.55  E-value: 4.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 192 VSAWRDLFVPKAVLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHsvlqwHKMKAPPIprst 271
Cdd:cd17953    11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQAL-PAIMSGRDVIGIAKTGSGKTLAFLLPMFR-----HIKDQRPV---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 272 gmppremrfgatahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcddDAGEGPssleekpvp 351
Cdd:cd17953    81 -----------------------------------------------------------------KPGEGP--------- 86
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 352 kqnedgeekfdaeqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQ 431
Cdd:cd17953    87 -------------------------------------IGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQI 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 432 RMLNRHPEIVIATPGRLWELVKEKHPHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEmlndsQYNPSRQTLVFSATL- 510
Cdd:cd17953   130 AELKRGAEIVVCTPGRMIDILTANNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVN-----NIRPDRQTVLFSATFp 204
                         330
                  ....*....|...
gi 1398331558 511 TLVHQAPARILHK 523
Cdd:cd17953   205 RKVEALARKVLHK 217
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
217-511 5.04e-29

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: 113.88  E-value: 5.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 217 TPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVlqwhkmkappiprstgmppremrfgatahlgspckdrtes 296
Cdd:pfam00270   1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALEAL---------------------------------------- 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 297 gvlpeearieteaQPSDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdaeqagklkqelcdq 376
Cdd:pfam00270  40 -------------DKLDNGPQA---------------------------------------------------------- 48
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 377 iaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLnRHPEIVIATPGRLWELVKEKH 456
Cdd:pfam00270  49 --------------LVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK 113
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 457 phlsNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:pfam00270 114 ----LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL-----PKKRQILLLSATLP 159
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
374-707 1.21e-28

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 121.05  E-value: 1.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 374 CDQIAIYKVHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVK 453
Cdd:PLN00206  183 CCTIRSGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLS 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 454 EkhpHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqynPSRQTLVFSATLTlvhqaparilhkKHVKKMDKTD 533
Cdd:PLN00206  263 K---HDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL------SQPQVLLFSATVS------------PEVEKFASSL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 534 KLDLLMQKVGMRGKPKvidltrnegtvETLTETKIHCETDEKDLYLYYFLM---QYPGRSLVFANSISCIKRLS-GLLKV 609
Cdd:PLN00206  322 AKDIILISIGNPNRPN-----------KAVKQLAIWVETKQKKQKLFDILKskqHFKPPAVVFVSSRLGADLLAnAITVV 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 610 LDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLM 689
Cdd:PLN00206  391 TGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIV 470
                         330
                  ....*....|....*...
gi 1398331558 690 LIGPEDVINFKKIYKTLQ 707
Cdd:PLN00206  471 FVNEEDRNLFPELVALLK 488
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
204-510 1.68e-28

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: 113.28  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIhsvlqWHKMKAPPIprstgmppremrfgat 283
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGR-DMIGIAKTGSGKTAAFIWPML-----VHIMDQREL---------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcddDAGEGPssleekpvpkqnedgeekfda 363
Cdd:cd17952    59 -----------------------------------------------------EKGEGP--------------------- 64
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17952    65 -------------------------IAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVA 119
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398331558 444 TPGRLWELVKEKhphLSNLRQLRCLVIDEADRMVEKGhFAelSQLLEMLNdsQYNPSRQTLVFSATL 510
Cdd:cd17952   120 TPGRLIDMVKKK---ATNLQRVTYLVLDEADRMFDMG-FE--YQVRSIVG--HVRPDRQTLLFSATF 178
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
204-511 1.73e-27

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: 111.26  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLQwhkmkAPPIPRSTGMppremrfgat 283
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNR-DIIGIAETGSGKTAAFLIPLLVYISR-----LPPLDEETKD---------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagEGPssleekpvpkqnedgeekfda 363
Cdd:cd17945    65 --------------------------------------------------------DGP--------------------- 67
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17945    68 -------------------------YALILAPTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIA 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 444 TPGRLWELVkEKhpHLSNLRQLRCLVIDEADRMVEKGhFAE-----LSQL-----------LEMLNDSQYNPSRQTLVFS 507
Cdd:cd17945   123 TPGRLLDCL-ER--RLLVLNQCTYVVLDEADRMIDMG-FEPqvtkiLDAMpvsnkkpdteeAEKLAASGKHRYRQTMMFT 198

                  ....
gi 1398331558 508 ATLT 511
Cdd:cd17945   199 ATMP 202
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
204-509 6.62e-27

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: 108.61  E-value: 6.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPmihsvlqwhkmkappiprstgmppremrfgAT 283
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGR-DMVGIAQTGSGKTLAFLLP------------------------------AI 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 AHLgspckdrtesgvlpeearieteaqpsdsgvqatpetsasaSAQTLLvcddDAGEGPssleekpvpkqnedgeekfda 363
Cdd:cd17966    50 VHI----------------------------------------NAQPPL----ERGDGP--------------------- 64
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIA 443
Cdd:cd17966    65 -------------------------IVLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIA 119
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398331558 444 TPGRLWELVKEKHphlSNLRQLRCLVIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSAT 509
Cdd:cd17966   120 TPGRLIDFLDQGK---TNLRRVTYLVLDEADRMLDMGFEPQIRKIV-----DQIRPDRQTLMWSAT 177
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
204-511 8.29e-26

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: 105.74  E-value: 8.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHSVLqwhkmkappiprstgmppremrfgat 283
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGK-DILARARTGSGKTAAYALPIIQKIL-------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfda 363
Cdd:cd17961       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagKLKQELCDQIAIYkvhprrpllGLVLTPTRELAIQVRQHIDAVAKFTG--INTAILVGGMSTQKQQRMLNRHPEIV 441
Cdd:cd17961    58 ----KAKAESGEEQGTR---------ALILVPTRELAQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIV 124
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 442 IATPGRLWELVKEKhpHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqynPSR-QTLVFSATLT 511
Cdd:cd17961   125 VSTPARLLSHLESG--SLLLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYL------PKNyQTFLMSATLS 187
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
212-510 1.14e-25

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: 106.03  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 212 GFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLqwhkMKAPPIPRSTGMPpremrfgatahlgspck 291
Cdd:cd17967    19 GYTKPTPVQKYAI-PIILAGRDLMACAQTGSGKTAAFLLPIISKLL----EDGPPSVGRGRRK----------------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 292 drtesgvlpeearieteAQPSdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdaeqagklkq 371
Cdd:cd17967    77 -----------------AYPS----------------------------------------------------------- 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 372 elcdqiaiykvhprrpllGLVLTPTRELAIQvrqhIDAVA-KF---TGINTAILVGGMSTQKQQRMLNRHPEIVIATPGR 447
Cdd:cd17967    81 ------------------ALILAPTRELAIQ----IYEEArKFsyrSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGR 138
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 448 LWELVKEkhpHLSNLRQLRCLVIDEADRMVEKGhFaeLSQLLEMLNDSQYNP--SRQTLVFSATL 510
Cdd:cd17967   139 LVDFIER---GRISLSSIKFLVLDEADRMLDMG-F--EPQIRKIVEHPDMPPkgERQTLMFSATF 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
574-681 5.93e-25

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: 99.98  E-value: 5.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 574 EKDLYLYYFLMQYPG-RSLVFANSISCIKrLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLD 652
Cdd:pfam00271   1 EKLEALLELLKKERGgKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*....
gi 1398331558 653 IPKVQHVIHYQVPRTSEIYIHRSGRTARA 681
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRA 108
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
205-511 3.58e-23

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: 98.13  E-value: 3.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 205 LRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIHS--VLQWhkmkappiprstgmppremrfga 282
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQGR-DILGAAKTGSGKTLAFLVPLLEKlyRERW----------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 283 tahlgspckdrtesgvlpeearieteaqpsdsgvqaTPEtsasasaqtllvcdddagegpssleekpvpkqneDGeekfd 362
Cdd:cd17941    58 ------------------------------------TPE----------------------------------DG----- 62
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 363 aeqagklkqelcdqiaiykvhprrplLG-LVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHpEIV 441
Cdd:cd17941    63 --------------------------LGaLIISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINRM-NIL 115
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 442 IATPGRLWELVKEKhPHLsNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:cd17941   116 VCTPGRLLQHMDET-PGF-DTSNLQMLVLDEADRILDMGFKETLDAIVENL-----PKSRQTLLFSATQT 178
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
391-529 3.81e-23

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: 98.16  E-value: 3.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKFTG---INTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKhphLSNLRQLRC 467
Cdd:cd17938    64 LILEPSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTG---KLDLSSVRF 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398331558 468 LVIDEADRMVEKGHFAELSQLLEMLNDSQYNPSR-QTLVFSATltlvhqapariLHKKHVKKM 529
Cdd:cd17938   141 FVLDEADRLLSQGNLETINRIYNRIPKITSDGKRlQVIVCSAT-----------LHSFEVKKL 192
DEXDc smart00487
DEAD-like helicases superfamily;
376-511 4.48e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 4.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558  376 QIAIYKVHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQ-QRMLNRHPEIVIATPGRLWELVKE 454
Cdd:smart00487  43 LPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQlRKLESGKTDILVTTPGRLLDLLEN 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1398331558  455 KHPHLSNlrqLRCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:smart00487 123 DKLSLSN---VDLVILDEAHRLLDGGFGDQLEKLLKLL-----PKNVQLLLLSATPP 171
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
204-510 7.37e-23

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: 97.41  E-value: 7.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQwHKMKAPPIPrstgmppremrfgat 283
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGL-PTILSGRDMIGIAFTGSGKTLVFTLPLIMFALE-QEKKLPFIK--------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddaGEGPssleekpvpkqnedgeekfda 363
Cdd:cd17951    64 -------------------------------------------------------GEGP--------------------- 67
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrplLGLVLTPTRELAIQVRQHIDAVAK------FTGINTAILVGGMSTQKQQRMLNRH 437
Cdd:cd17951    68 -------------------------YGLIVCPSRELARQTHEVIEYYCKalqeggYPQLRCLLCIGGMSVKEQLEVIRKG 122
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398331558 438 PEIVIATPGRLWELVKEKhphLSNLRQLRCLVIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSATL 510
Cdd:cd17951   123 VHIVVATPGRLMDMLNKK---KINLDICRYLCLDEADRMIDMGFEEDIRTIF-----SYFKGQRQTLLFSATM 187
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
390-511 1.79e-22

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: 96.11  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 390 GLVLTPTRELAIQVRQHIDAVAKFTG--INTAILVGGMSTQKQQRMLNRH-PEIVIATPGRLWELVKEKHpHLSNLRQLR 466
Cdd:cd17960    66 ALIISPTRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKA-DKVKVKSLE 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398331558 467 CLVIDEADRMVEKGHFAELSQLLEMLndsqynP-SRQTLVFSATLT 511
Cdd:cd17960   145 VLVLDEADRLLDLGFEADLNRILSKL------PkQRRTGLFSATQT 184
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
205-520 2.47e-22

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: 95.51  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 205 LRALSFLGFSAPTPIQALTLAPAIRDKlDILGAAETGSGKTLAFAIPMIhsvlqwhkmkappiprstgmppremrfgata 284
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGR-DVLGAAKTGSGKTLAFLIPAI------------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 285 hlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdae 364
Cdd:cd17942       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 365 qagklkqELcdqiaIYKVH--PRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVI 442
Cdd:cd17942    50 -------EL-----LYKLKfkPRNGTGVIIISPTRELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILV 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 443 ATPGRLWElvkekhpHLSN-----LRQLRCLVIDEADRMVEKGHFAELSQLLEMLndsqynPS-RQTLVFSATLTLVHQA 516
Cdd:cd17942   118 ATPGRLLD-------HLQNtkgflYKNLQCLIIDEADRILEIGFEEEMRQIIKLL------PKrRQTMLFSATQTRKVED 184

                  ....
gi 1398331558 517 PARI 520
Cdd:cd17942   185 LARI 188
HELICc smart00490
helicase superfamily c-terminal domain;
601-681 2.79e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558  601 KRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTAR 680
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   .
gi 1398331558  681 A 681
Cdd:smart00490  81 A 81
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
376-511 8.32e-22

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: 95.01  E-value: 8.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 376 QIAIYKVHPRrpLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMST--QKQQRMLNRH------PEIVIATPGR 447
Cdd:cd17956    59 QALSKRVVPR--LRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFkkEQKLLLVDTSgrylsrVDILVATPGR 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 448 LWELVKEKHPHlsNLRQLRCLVIDEADRMVEKGHFAELSQLLE-----------------MLNDSQYNPsrQTLVFSATL 510
Cdd:cd17956   137 LVDHLNSTPGF--TLKHLRFLVIDEADRLLNQSFQDWLETVMKalgrptapdlgsfgdanLLERSVRPL--QKLLFSATL 212

                  .
gi 1398331558 511 T 511
Cdd:cd17956   213 T 213
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
212-509 2.68e-21

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: 94.26  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 212 GFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIhsvlqwhkmkappiprsTGMppreMRFGATAhlgspck 291
Cdd:cd18052    62 GYEKPTPVQKYAI-PIILAGRDLMACAQTGSGKTAAFLLPVL-----------------TGM----MKEGLTA------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 292 drtesgvlpeearieteaqPSDSGVQaTPETsasasaqtllvcdddagegpssleekpvpkqnedgeekfdaeqagklkq 371
Cdd:cd18052   113 -------------------SSFSEVQ-EPQA------------------------------------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 372 elcdqiaiykvhprrpllgLVLTPTRELAIQVrqHIDAVaKF---TGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRL 448
Cdd:cd18052   124 -------------------LIVAPTRELANQI--FLEAR-KFsygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRL 181
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398331558 449 WELV-KEKhphlSNLRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQYNpSRQTLVFSAT 509
Cdd:cd18052   182 LDFIgRGK----ISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKE-DRQTLMFSAT 238
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
390-511 3.75e-21

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: 92.39  E-value: 3.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 390 GLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKhpHLSnLRQLRCLV 469
Cdd:cd17939    68 ALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRR--SLR-TDKIKMFV 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398331558 470 IDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:cd17939   145 LDEADEMLSRGFKDQIYDIFQFL-----PPETQVVLFSATMP 181
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
211-511 5.89e-21

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: 92.26  E-value: 5.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 211 LGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQwhkmKAPPIPRSTGmppremrfgatahlgspc 290
Cdd:cd17949     9 MGIEKPTAIQKLAI-PVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLS----LEPRVDRSDG------------------ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 291 kdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfdaeqagklk 370
Cdd:cd17949       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 371 qelcdqiaiykvhprrpLLGLVLTPTRELAIQVRQHIDAVAK-FTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLW 449
Cdd:cd17949    66 -----------------TLALVLVPTRELALQIYEVLEKLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLL 128
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 450 ElvkekhpHLSN-----LRQLRCLVIDEADRMVEKGHFAELSQLLEMLNDSQYN--------PSRQTLVFSATLT 511
Cdd:cd17949   129 D-------HLKNtqsfdVSNLRWLVLDEADRLLDMGFEKDITKILELLDDKRSKaggekskpSRRQTVLVSATLT 196
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
391-511 8.68e-20

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: 88.56  E-value: 8.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKF-TGINTAILVGGMSTQKQQRML-NRHPEIVIATPGRLWELVKEKHPHLSNLRQlrcL 468
Cdd:cd17950    74 LVICHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKH---F 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1398331558 469 VIDEADRMVEKghfaelsqlLEMLNDSQ-----YNPSRQTLVFSATLT 511
Cdd:cd17950   151 VLDECDKMLEQ---------LDMRRDVQeifraTPHDKQVMMFSATLS 189
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
204-511 1.81e-19

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: 87.26  E-value: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQWHKmkappiprstgmppremrfgat 283
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAI-PILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsDSGVQAtpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfda 363
Cdd:cd17957    58 -----------------------------KKGLRA--------------------------------------------- 63
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvhprrpllgLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMS-TQKQQRMLNRHPEIVI 442
Cdd:cd17957    64 ---------------------------LILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILV 116
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398331558 443 ATPGRLWELVKEKHPHLSNLRQlrcLVIDEADRMVEKGhFAElsQLLEMLNDSQyNPSRQTLVFSATLT 511
Cdd:cd17957   117 STPLRLVFLLKQGPIDLSSVEY---LVLDEADKLFEPG-FRE--QTDEILAACT-NPNLQRSLFSATIP 178
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
385-509 5.78e-19

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: 85.78  E-value: 5.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 385 RRPLLGLVLTPTRELAIQVRQHIDAVA-KFTGINTAILVGGMSTQKQQRMLNRhPEIVIATPGRLWELVKEkhpHLSNLR 463
Cdd:cd17943    56 RRHPQVLILAPTREIAVQIHDVFKKIGkKLEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIEL---GALNVS 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398331558 464 QLRCLVIDEADRMVEKGHFAELSQLLEMLNDsqynpSRQTLVFSAT 509
Cdd:cd17943   132 HVRLFVLDEADKLMEGSFQKDVNWIFSSLPK-----NKQVIAFSAT 172
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
204-542 9.94e-19

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: 86.27  E-value: 9.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQWHKMKAPPIPrstgmppremrfgat 283
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGI-PSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFN--------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 284 ahlgspckdrtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagegpssleekpvpkqnedgeekfda 363
Cdd:cd17948       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 364 eqagklkqelcdqiaiykvHPRrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGmstQKQQRMLNRH---PEI 440
Cdd:cd17948    65 -------------------APR----GLVITPSRELAEQIGSVAQSLTEGLGLKVKVITGG---RTKRQIRNPHfeeVDI 118
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 441 VIATPGRLWELVKEkhpHLSNLRQLRCLVIDEADRMVEKGHFAELSQLLE--------MLNDSQYNPSRQTLVFSATLtl 512
Cdd:cd17948   119 LVATPGALSKLLTS---RIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRrfplasrrSENTDGLDPGTQLVLVSATM-- 193
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1398331558 513 vhqaPAR---ILHKkhVKKMD-----KTDKLDLLMQKV 542
Cdd:cd17948   194 ----PSGvgeVLSK--VIDVDsietvTSDKLHRLMPHV 225
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
389-527 2.92e-18

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: 83.75  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 389 LGLVLTPTRELAIQV-RQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEkhpHLSNLRQLRC 467
Cdd:cd17962    60 SALILTPTRELAVQIeDQAKELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQ---SSVELDNIKI 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 468 LVIDEADRMVEKGHFAELSQLLEMLNDSQynpsrQTLVFSATLTLVHQAPARILHKKHVK 527
Cdd:cd17962   137 VVVDEADTMLKMGFQQQVLDILENISHDH-----QTILVSATIPRGIEQLAGQLLQNPVR 191
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
390-509 5.15e-18

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: 83.01  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 390 GLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNrhpEIVIATPGRLWELVKEKhphLSNLRQLRCLV 469
Cdd:cd17963    67 ALCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKR---QLDLKKIKILV 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398331558 470 IDEADRMVEKGHFAELSQ-LLEMLndsqyNPSRQTLVFSAT 509
Cdd:cd17963   141 LDEADVMLDTQGHGDQSIrIKRML-----PRNCQILLFSAT 176
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
391-509 5.45e-18

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: 83.91  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHphlSNLRQLRCLVI 470
Cdd:cd18049   101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK---TNLRRCTYLVL 177
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398331558 471 DEADRMVEKGHFAELSQLLEmlndsQYNPSRQTLVFSAT 509
Cdd:cd18049   178 DEADRMLDMGFEPQIRKIVD-----QIRPDRQTLMWSAT 211
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
391-509 9.01e-18

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: 84.29  E-value: 9.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHphlSNLRQLRCLVI 470
Cdd:cd18050   139 LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK---TNLRRCTYLVL 215
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1398331558 471 DEADRMVEKGHFAELSQLLEmlndsQYNPSRQTLVFSAT 509
Cdd:cd18050   216 DEADRMLDMGFEPQIRKIVD-----QIRPDRQTLMWSAT 249
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
386-511 4.43e-16

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: 77.51  E-value: 4.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 386 RPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHphlSNLRQL 465
Cdd:cd18045    66 RETQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRS---LRTRHI 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1398331558 466 RCLVIDEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLT 511
Cdd:cd18045   143 KMLVLDEADEMLNKGFKEQIYDVYRYL-----PPATQVVLVSATLP 183
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
390-509 6.04e-16

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: 77.34  E-value: 6.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 390 GLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHPHLSNLRQlrcLV 469
Cdd:cd17940    70 ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKT---LV 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1398331558 470 IDEADRMVEKghfaELSQLLEMLNDSqYNPSRQTLVFSAT 509
Cdd:cd17940   147 LDEADKLLSQ----DFQPIIEKILNF-LPKERQILLFSAT 181
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
204-509 6.32e-16

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: 77.12  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 204 VLRALSFLGFSAPTPIQAlTLAPAIRDKLDILGAAETGSGKTLAFAIP-MIHSVLQwhkmkapPIPRstgmppremrfga 282
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQS-QAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQ-------PIPR------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 283 tahlgspckdrtesgvlpeEARIeteaqpsdsgvqatpetsasasaqtllvcdddageGPSSLeekpvpkqnedgeekfd 362
Cdd:cd17958    60 -------------------EQRN-----------------------------------GPGVL----------------- 68
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 363 aeqagklkqelcdqiaiykvhprrpllglVLTPTRELAIQVRQHIDAVaKFTGINTAILVGGMSTQKQQRMLNRHPEIVI 442
Cdd:cd17958    69 -----------------------------VLTPTRELALQIEAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIII 118
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398331558 443 ATPGRLWELVKEkhpHLSNLRQLRCLVIDEADRMVEKGhFAelSQLLEMLNDSQynPSRQTLVFSAT 509
Cdd:cd17958   119 ATPGRLNDLQMN---NVINLKSITYLVLDEADRMLDMG-FE--PQIRKILLDIR--PDRQTIMTSAT 177
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
213-519 4.82e-15

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: 75.85  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 213 FSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQwhkmkappiprstgmppremrfgatahlgspckd 292
Cdd:cd18051    41 YTKPTPVQKHAI-PIIKSKRDLMACAQTGSGKTAAFLLPILSQIYE---------------------------------- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 293 rtesgvlpeearieteaqpsdsgvqatpetsasasaqtllvcdddagEGPssleekPVPKQNEDGeekfdaeQAGKLKQe 372
Cdd:cd18051    86 -----------------------------------------------QGP------GESLPSESG-------YYGRRKQ- 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 373 lcdqiaiykvHPrrplLGLVLTPTRELAIQVrqhIDAVAKFT---GINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLW 449
Cdd:cd18051   105 ----------YP----LALVLAPTRELASQI---YDEARKFAyrsRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLV 167
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398331558 450 ELVKEKHPHLSNLRQlrcLVIDEADRMVEKGHFAELSQLLEMLNdsqYNPS--RQTLVFSATLTLVHQAPAR 519
Cdd:cd18051   168 DMLERGKIGLDYCKY---LVLDEADRMLDMGFEPQIRRIVEQDT---MPPTgeRQTLMFSATFPKEIQMLAR 233
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
391-522 6.58e-15

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: 74.02  E-value: 6.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHPHLSNLRQlrcLVI 470
Cdd:cd18046    71 LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKM---FVL 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398331558 471 DEADRMVEKGHFAELSQLLEMLndsqyNPSRQTLVFSATLtlvhqaPARILH 522
Cdd:cd18046   148 DEADEMLSRGFKDQIYDIFQKL-----PPDTQVVLLSATM------PNDVLE 188
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
391-509 6.31e-14

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: 71.42  E-value: 6.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKftGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHPHLSNLRQLrclVI 470
Cdd:cd17944    68 LVLAPTRELANQVTKDFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHV---VL 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1398331558 471 DEADRMVEKGhFAElsQLLEMLN-----DSQYNPsrQTLVFSAT 509
Cdd:cd17944   143 DEVDQMLDMG-FAE--QVEEILSvsykkDSEDNP--QTLLFSAT 181
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
391-809 7.31e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 65.82  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQvrqhidAVAKFTGINTAILVGGmstqkqqRMLNRHPEIVIATPGRLWelvkeKHPHLSNLRQLRCLVI 470
Cdd:COG1061   131 LVLVPRRELLEQ------WAEELRRFLGDPLAGG-------GKKDSDAPITVATYQSLA-----RRAHLDELGDRFGLVI 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 471 -DEAdrmvekgHFAELSQLLEMLNdsqYNPSRQTLVFSATltlvhqaPARilhkkhvkkMDKTD-KLDLLMQKV------ 542
Cdd:COG1061   193 iDEA-------HHAGAPSYRRILE---AFPAAYRLGLTAT-------PFR---------SDGREiLLFLFDGIVyeyslk 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 543 -----GMRGKPKVI----DLTRNEGTVETLTET---KIHCETDEKDLYLYYFLMQYPG--RSLVFANSISCIKRLSGLLK 608
Cdd:COG1061   247 eaiedGYLAPPEYYgirvDLTDERAEYDALSERlreALAADAERKDKILRELLREHPDdrKTLVFCSSVDHAEALAELLN 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 609 VLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQvPRTSE-IYIHRSGRTARAASEG-- 685
Cdd:COG1061   327 EAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPrEFIQRLGRGLRPAPGKed 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 686 LSLMLIGPEDVINFKKIYKTLQKDE------------DIPLFPVQSKYMDVVKERIRLARQIEKAEYRNFQACLHNSWIE 753
Cdd:COG1061   406 ALVYDFVGNDVPVLEELAKDLRDLAgyrvefldeeesEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLL 485
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1398331558 754 QAAAALEIELEEEMYKGGKADQQEERRRQKQMKMLKQELRHLLSQPLFQENLKTRY 809
Cdd:COG1061   486 LELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLEL 541
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
391-509 4.82e-09

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: 55.87  E-value: 4.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKfTGINTAILVGGMSTQKQQRMLNRHPEIVIATPGRLWELVKEKHPHLsnLRQLRCLVI 470
Cdd:cd00046    34 LVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLF--LKDLKLIIV 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1398331558 471 DEADRMVEKGHFAELSQLLE---MLNDSqynpsrQTLVFSAT 509
Cdd:cd00046   111 DEAHALLIDSRGALILDLAVrkaGLKNA------QVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
621-683 6.67e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 59.74  E-value: 6.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 621 MHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQ-VPrtSEI-YIHRSGRTARAAS 683
Cdd:COG1111   395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVP--SEIrSIQRKGRTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
621-683 3.67e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.19  E-value: 3.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398331558 621 MHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQ-VPrtSEI-YIHRSGRTARAAS 683
Cdd:PRK13766  407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVP--SEIrSIQRKGRTGRQEE 469
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
621-680 2.76e-07

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: 50.43  E-value: 2.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 621 MHQKQRLRNLEQFARLQDCVLLATDVAARGLDIPKVQHVIHYQvPRTSEI-YIHRSGRTAR 680
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
640-685 4.43e-07

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: 48.08  E-value: 4.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1398331558 640 VLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEG 685
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
568-697 1.45e-06

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 51.68  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 568 IHCETDEKDLYLYYFLMQYPGRS-LVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATdV 646
Cdd:COG0514   210 VPKPPDDKLAQLLDFLKEHPGGSgIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-I 288
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1398331558 647 A-ARGLDIPKVQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLIGPEDVI 697
Cdd:COG0514   289 AfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVA 340
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
589-662 1.89e-06

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: 47.86  E-value: 1.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398331558 589 RSLVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDC--VLLATDVAARGLDIPKVQHVIHY 662
Cdd:cd18793    29 KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILY 104
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
621-690 5.61e-06

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: 46.82  E-value: 5.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 621 MHQKQRLRNLEQFaRLQDC-VLLATDVAARGLDIPKVQHVIHYQVPRTSEIYIHRSGRtARAASEGLSLML 690
Cdd:cd18802    74 MTQRKQKETLDKF-RDGELnLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYILMV 142
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
188-258 5.72e-06

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: 50.22  E-value: 5.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 188 QKADVSAWRDlFVPKAVLRALSFLGFSAPTPIQALTLApAIRDKLDILGAAETGSGKTLAFAIPMIHSVLQ 258
Cdd:COG1205    30 REARYAPWPD-WLPPELRAALKKRGIERLYSHQAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLE 98
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
572-680 6.38e-06

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: 46.43  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 572 TDEKDLYLYYFLMQYPGRS-LVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFARLQDCVLLATdVA-AR 649
Cdd:cd18794    14 KDEKLDLLKRIKVEHLGGSgIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGM 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1398331558 650 GLDIPKVQHVIHYQVPRTSEIYIHRSGRTAR 680
Cdd:cd18794    93 GIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
342-533 1.24e-05

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: 47.32  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 342 PSSLEEKPVPKQNEDGEEKFDAE-QAGKLKQE-----LCDQIAIYKVHPRrpllGLVLTPTRELAIQVRQHIDAVAKF-T 414
Cdd:cd18048    41 PSKIQENALPMMLADPPQNLIAQsQSGTGKTAafvlaMLSRVDALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFcV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 415 GINTAILVGGMSTQKQQRMlnrHPEIVIATPGRLWELVKEKHphLSNLRQLRCLVIDEADRMVEKGHFAELSQLLEmlnd 494
Cdd:cd18048   117 GIQVIYAIRGNRPGKGTDI---EAQIVIGTPGTVLDWCFKLR--LIDVTNISVFVLDEADVMINVQGHSDHSVRVK---- 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1398331558 495 sQYNPSR-QTLVFSATL-TLVHQAPARILHKKHVKKMDKTD 533
Cdd:cd18048   188 -RSMPKEcQMLLFSATFeDSVWAFAERIVPDPNIIKLKKEE 227
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
358-479 3.70e-05

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: 46.22  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 358 EEKFDAEQAGKLKQELCDqiaiyKVHPRrpllGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQRML-NR 436
Cdd:cd17965    89 QEQEPFEEAEEEYESAKD-----TGRPR----SVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLaFK 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1398331558 437 HP-EIVIATPGRLWELVKEKhphLSNLRQLRCLVIDEADRMVEK 479
Cdd:cd17965   160 GRiDILVTTPGKLASLAKSR---PKILSRVTHLVVDEADTLFDR 200
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
628-701 4.76e-05

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


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 44.60  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 628 RNLEQFARLQDCVLLAT----DVAARGLDIPK-VQHVIHYQVPRTSeiYIHRSGRTAR----AASEGLSLMLIGPEDVIN 698
Cdd:cd18798    63 KNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVPVTT--YIQASGRTSRlyagGLTKGLSVVLVDDPELFE 140

                  ...
gi 1398331558 699 FKK 701
Cdd:cd18798   141 ALK 143
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
579-696 2.15e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 579 LYYFLMQYPGRS-LVFANSISCIKRLSGLLKVLDVMPLTLHACMHQKQRLRNLEQFAR--LQdcVLLATDVAARGLDIPK 655
Cdd:PRK11057  227 LMRYVQEQRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRddLQ--IVVATVAFGMGINKPN 304
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398331558 656 VQHVIHYQVPRTSEIYIHRSGRTARAASEGLSLMLIGPEDV 696
Cdd:PRK11057  305 VRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADM 345
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
391-510 5.48e-04

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: 42.01  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKF-TGINTAILVGGMSTQKQQRMLNrhpEIVIATPGRLWE-LVKEKhphLSNLRQLRCL 468
Cdd:cd18047    75 LCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLK---FIDPKKIKVF 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1398331558 469 VIDEADRMV-EKGHFAELSQLLEMLNDSQynpsrQTLVFSATL 510
Cdd:cd18047   149 VLDEADVMIaTQGHQDQSIRIQRMLPRNC-----QMLLFSATF 186
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
391-510 5.67e-04

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: 41.86  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 391 LVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKQQrmlNRHPEIVIATPGRlWELVKEKHPHLsNLRQLRCLVI 470
Cdd:cd17921    50 VYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLL---LAEADILVATPEK-LDLLLRNGGER-LIQDVRLVVV 124
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398331558 471 DEAdRMVEKGHFAE-LSQLLEMLNdsQYNPSRQTLVFSATL 510
Cdd:cd17921   125 DEA-HLIGDGERGVvLELLLSRLL--RINKNARFVGLSATL 162
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
213-247 1.33e-03

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 42.40  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1398331558 213 FSAPTPIQALTLaPAIRDKLDILGAAETGSGKTLA 247
Cdd:COG1201    22 FGAPTPPQREAW-PAIAAGESTLLIAPTGSGKTLA 55
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
393-509 2.49e-03

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 40.00  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 393 LTPTRELaiqVRQHIDAVAKFTGI---NTAILVGgmSTQKQQRM-LNRHPEIVIATPGRLWELVKEkhpHLSNLRQLRCL 468
Cdd:cd18033    52 MAPTKPL---VSQQIEACYKITGIpssQTAELTG--SVPPTKRAeLWASKRVFFLTPQTLENDLKE---GDCDPKSIVCL 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1398331558 469 VIDEADRMVEKGHFAELSQLLemlndSQYNPSRQTLVFSAT 509
Cdd:cd18033   124 VIDEAHRATGNYAYCQVVREL-----MRYNSHFRILALTAT 159
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
376-510 7.80e-03

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 39.88  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 376 QIAIYKvHPRRPLLGLVLTPTRELAIQVRQHIDAVAKFTGINTAILVGGMSTQKqqRMLNRhPEIVIATPGRLWELVKEK 455
Cdd:COG1204    56 ELAILK-ALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNG 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398331558 456 HphlSNLRQLRCLVIDEA----DRmvEKGHFAE--LSQLLEMlndsqyNPSRQTLVFSATL 510
Cdd:COG1204   132 P---SWLRDVDLVVVDEAhlidDE--SRGPTLEvlLARLRRL------NPEAQIVALSATI 181
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
415-511 8.69e-03

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 38.28  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398331558 415 GINTAILVGGMSTQKQQRMLNRHPE----IVIATPGRLW-ELVKEKHPHLSNLRQLRCLVIDEADRMVEKGH-----FAE 484
Cdd:cd17920    76 GIRAAALNSTLSPEEKREVLLRIKNgqykLLYVTPERLLsPDFLELLQRLPERKRLALIVVDEAHCVSQWGHdfrpdYLR 155
                          90       100
                  ....*....|....*....|....*..
gi 1398331558 485 LSQLLEMLNDSqynpsrQTLVFSATLT 511
Cdd:cd17920   156 LGRLRRALPGV------PILALTATAT 176
 
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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