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Conserved domains on  [gi|21071032|ref|NP_057306|]
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probable ATP-dependent RNA helicase DDX41 isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028728)

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_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 192-397 4.84e-148

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: 425.98  E-value: 4.84e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEGPYGLIVCPSRELAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17951  81 QTHEVIEYYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 408-536 1.88e-57

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: 189.26  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 408 VIQEVEYVKEEAKMVYLLECL--QKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDV 485
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21071032 486 LVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 192-397 4.84e-148

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: 425.98  E-value: 4.84e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEGPYGLIVCPSRELAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17951  81 QTHEVIEYYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
180-562 4.01e-147

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 432.26  E-value: 4.01e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 180 IKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfcleqekRLPFSKREGPY 259
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ-------RLDPSRPRAPQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 260 GLIICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICR 339
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLG------LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 340 YLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEA 419
Cdd:COG0513 148 TLVLDEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 420 KMVYLLECLQKTPPP-VLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDF 498
Cdd:COG0513 228 KLELLRRLLRDEDPErAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071032 499 PAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFinkaCDESVLMDLKALLLEAKQKVPPV 562
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISL----VTPDERRLLRAIEKLIGQKIEEE 367
PTZ00110 PTZ00110
helicase; Provisional
 152-566 2.66e-123

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 375.65  E-value: 2.66e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  152 VLSMSEERHERVRKKYHI-LVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSG 230
Cdd:PTZ00110 100 VSALSSKEVDEIRKEKEItIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  231 KTLVFTLPVIMFCLEQEKrlpFSKREGPYGLIICPSRELARQthgILEyycRLLQEDSSPLLRCALCIGGMSVKEQMETI 310
Cdd:PTZ00110 180 KTLAFLLPAIVHINAQPL---LRYGDGPIVLVLAPTRELAEQ---IRE---QCNKFGASSKIRNTVAYGGVPKRGQIYAL 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  311 RHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSAL 390
Cdd:PTZ00110 251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLC 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  391 V-KPVTINVGRAG-AASLDVIQEVEYVKEEAKMVYLLECLQKTPPP---VLIFAEKKADVDAIHEYLLLKGVEAVAIHGG 465
Cdd:PTZ00110 331 KeEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdkILIFVETKKGADFLTKELRLDGWPALCIHGD 410

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  466 KDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFINKacDESVL 545
Cdd:PTZ00110 411 KKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP--DKYRL 488

                        410       420
                 ....*....|....*....|..
gi 21071032  546 M-DLKALLLEAKQKVPPVLQVL 566
Cdd:PTZ00110 489 ArDLVKVLREAKQPVPPELEKL 510
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 408-536 1.88e-57

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: 189.26  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 408 VIQEVEYVKEEAKMVYLLECL--QKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDV 485
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21071032 486 LVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 205-385 2.24e-50

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: 171.66  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   205 TPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFsKREGPYGLIICPSRELARQTHGILEYYCRLL 284
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPAL-------EALDK-LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   285 QedssplLRCALCIGGMSVKEQMETIRhGVHMMVATPGRLMDLLQKKmVSLDICRYLALDEADRMIDMGFEGDIRTIFSY 364
Cdd:pfam00270  73 G------LKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRR 144

                         170       180
                  ....*....|....*....|.
gi 21071032   365 FKGQRQTLLFSATMPKKIQNF 385
Cdd:pfam00270 145 LPKKRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
196-409 1.21e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.35  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    196 LKKKGIHHPTPIQIQGIPTILSG-RDMIGIAFTGSGKTLVFTLPVIMFcleqekrlpFSKREGPYGLIICPSRELARQTH 274
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA---------LKRGKGGRVLVLVPTRELAEQWA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    275 GILEYYCrllqedSSPLLRCALCIGGMSVKEQMETIRHGV-HMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMG 353
Cdd:smart00487  72 EELKKLG------PSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032    354 FEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVI 409
Cdd:smart00487 146 FGDQLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 419-527 5.81e-35

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: 127.71  E-value: 5.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   419 AKMVYLLECLQKTPPP-VLIFAEKKADVDAihEYLLLK-GVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGL 496
Cdd:pfam00271   1 EKLEALLELLKKERGGkVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 21071032   497 DFPAIQHVINYDMPEEIENYVHRIGRTGRSG 527
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
446-527 1.62e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 111.53  E-value: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    446 DAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGR 525
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 21071032    526 SG 527
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
420-527 4.02e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 82.09  E-value: 4.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 420 KMVYLLECLQKT-----PPPVLIFAEKKADVDAIHEYLLLKGVEAV-----AIHGGKD---QEERTKAIEAFREGKKDVL 486
Cdd:COG1111 336 KLSKLREILKEQlgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqASKEGDKgltQKEQIEILERFRAGEFNVL 415

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21071032 487 VATDVASKGLDFPAIQHVINYD-MPEEIEnYVHRIGRTGRSG 527
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKR 456
PRK13766 PRK13766
Hef nuclease; Provisional
 410-527 5.61e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 68.75  E-value: 5.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  410 QEVEYVKEEAKMVYLLECLQKTPPP-VLIFAEKKADVDAIHEYLLLKGVEAVAIHG--------GKDQEERTKAIEAFRE 480
Cdd:PRK13766 342 LDIEHPKLEKLREIVKEQLGKNPDSrIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRA 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 21071032  481 GKKDVLVATDVASKGLDFPAIQHVINYD-MPEEIENyVHRIGRTGRSG 527
Cdd:PRK13766 422 GEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGRQE 468
 
Name Accession Description Interval E-value
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 192-397 4.84e-148

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: 425.98  E-value: 4.84e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEGPYGLIVCPSRELAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17951  81 QTHEVIEYYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
180-562 4.01e-147

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 432.26  E-value: 4.01e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 180 IKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfcleqekRLPFSKREGPY 259
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ-------RLDPSRPRAPQ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 260 GLIICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICR 339
Cdd:COG0513  74 ALILAPTRELALQVAEELRKLAKYLG------LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 340 YLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEA 419
Cdd:COG0513 148 TLVLDEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 420 KMVYLLECLQKTPPP-VLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDF 498
Cdd:COG0513 228 KLELLRRLLRDEDPErAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDI 307

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071032 499 PAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFinkaCDESVLMDLKALLLEAKQKVPPV 562
Cdd:COG0513 308 DDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISL----VTPDERRLLRAIEKLIGQKIEEE 367
PTZ00110 PTZ00110
helicase; Provisional
 152-566 2.66e-123

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 375.65  E-value: 2.66e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  152 VLSMSEERHERVRKKYHI-LVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSG 230
Cdd:PTZ00110 100 VSALSSKEVDEIRKEKEItIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  231 KTLVFTLPVIMFCLEQEKrlpFSKREGPYGLIICPSRELARQthgILEyycRLLQEDSSPLLRCALCIGGMSVKEQMETI 310
Cdd:PTZ00110 180 KTLAFLLPAIVHINAQPL---LRYGDGPIVLVLAPTRELAEQ---IRE---QCNKFGASSKIRNTVAYGGVPKRGQIYAL 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  311 RHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSAL 390
Cdd:PTZ00110 251 RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLC 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  391 V-KPVTINVGRAG-AASLDVIQEVEYVKEEAKMVYLLECLQKTPPP---VLIFAEKKADVDAIHEYLLLKGVEAVAIHGG 465
Cdd:PTZ00110 331 KeEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDgdkILIFVETKKGADFLTKELRLDGWPALCIHGD 410

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  466 KDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFINKacDESVL 545
Cdd:PTZ00110 411 KKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP--DKYRL 488

                        410       420
                 ....*....|....*....|..
gi 21071032  546 M-DLKALLLEAKQKVPPVLQVL 566
Cdd:PTZ00110 489 ArDLVKVLREAKQPVPPELEKL 510
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 192-396 3.26e-87

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: 269.70  E-value: 3.26e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRlpfsKREGPYGLIICPSRELAR 271
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKK----KGRGPQALVLAPTRELAM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRllqedsSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd00268  77 QIAEVARKLGK------GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLD 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd00268 151 MGFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 181-537 3.29e-87

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 278.99  E-value: 3.29e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  181 KSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPfSKREGPYG 260
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL-------QKLD-VKRFRVQA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  261 LIICPSRELA-----------RQTHGIleyycRLLqedsspllrcALCiGGMSVKEQMETIRHGVHMMVATPGRLMDLLQ 329
Cdd:PRK11776  76 LVLCPTRELAdqvakeirrlaRFIPNI-----KVL----------TLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLR 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  330 KKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASldVI 409
Cdd:PRK11776 140 KGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP--AI 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  410 QEVEY-VKEEAKM--VYLLeCLQKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVL 486
Cdd:PRK11776 218 EQRFYeVSPDERLpaLQRL-LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVL 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21071032  487 VATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFIN 537
Cdd:PRK11776 297 VATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVA 347
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 182-560 6.34e-87

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 278.23  E-value: 6.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEkrlPFSKREGPY-G 260
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ---PHAKGRRPVrA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  261 LIICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRY 340
Cdd:PRK10590  79 LILTPTRELAAQIGENVRDYSKYLN------IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  341 LALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEAK 420
Cdd:PRK10590 153 LVLDEADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  421 MVYLLECLQKTP-PPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFP 499
Cdd:PRK10590 233 RELLSQMIGKGNwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21071032  500 AIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFInkACDE-SVLMDLKALLleaKQKVP 560
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLV--CVDEhKLLRDIEKLL---KKEIP 369
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 153-560 3.09e-79

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 260.11  E-value: 3.09e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  153 LSMSEERHERVRKKYHILVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKT 232
Cdd:PLN00206  93 SGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKT 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  233 LVFTLPVIMFCLEQEKRLPfSKREGPYGLIICPSRELARQThgileyycrllqEDSSPLL------RCALCIGGMSVKEQ 306
Cdd:PLN00206 173 ASFLVPIISRCCTIRSGHP-SEQRNPLAMVLTPTRELCVQV------------EDQAKVLgkglpfKTALVVGGDAMPQQ 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  307 METIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKgQRQTLLFSATMPKKIQNFA 386
Cdd:PLN00206 240 LYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFA 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  387 KSALVKPVTINVGRAGAASLDVIQEVEYVKEEAKMVYLLECL---QKTPPPVLIFAEKKADVDAIHEYL-LLKGVEAVAI 462
Cdd:PLN00206 319 SSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILkskQHFKPPAVVFVSSRLGADLLANAItVVTGLKALSI 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  463 HGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFINKAcDE 542
Cdd:PLN00206 399 HGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE-DR 477

                        410
                 ....*....|....*...
gi 21071032  543 SVLMDLKALLLEAKQKVP 560
Cdd:PLN00206 478 NLFPELVALLKSSGAAIP 495
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 183-536 3.04e-74

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 244.47  E-value: 3.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREgpygLI 262
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRI----LI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  263 ICPSRELARQTHGileyYCRLLQEDSSplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLA 342
Cdd:PRK11192  79 LTPTRELAMQVAD----QARELAKHTH--LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  343 LDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMP-KKIQNFAKSALVKPVTINVgragAASLdviqeveyvKEEAKM 421
Cdd:PRK11192 153 LDEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEA----EPSR---------RERKKI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  422 ---VY----------LLECLQKTPPP--VLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVL 486
Cdd:PRK11192 220 hqwYYraddlehktaLLCHLLKQPEVtrSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVL 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 21071032  487 VATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:PRK11192 300 VATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 177-535 2.73e-73

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 243.28  E-value: 2.73e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  177 PPPIKS-FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLE---QEKRLpf 252
Cdd:PRK01297  82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtppPKERY-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  253 skREGPYGLIICPSRELARQthgileyycrlLQEDSSPL-----LRCALCIGGMSVKEQMETI--RHgVHMMVATPGRLM 325
Cdd:PRK01297 160 --MGEPRALIIAPTRELVVQ-----------IAKDAAALtkytgLNVMTFVGGMDFDKQLKQLeaRF-CDILVATPGRLL 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  326 DLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSY--FKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGA 403
Cdd:PRK01297 226 DFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQtpRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENV 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  404 ASLDVIQEVEYVKEEAKMVYLLECLQKTP-PPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGK 482
Cdd:PRK01297 306 ASDTVEQHVYAVAGSDKYKLLYNLVTQNPwERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGK 385

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21071032  483 KDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTF 535
Cdd:PRK01297 386 IRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 182-402 1.30e-71

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: 230.07  E-value: 1.30e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREG--PY 259
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKayPS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 260 GLIICPSRELARQTHGILEYYCRllqeDSSplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICR 339
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSY----RSG--VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIK 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071032 340 YLALDEADRMIDMGFEGDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAG 402
Cdd:cd17967 155 FLVLDEADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 192-545 3.22e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 233.32  E-value: 3.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFtLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:PRK04837  19 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTATFHYLLSHPAPEDRKVNQPRALIMAPTRELAV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  272 QTHgileyycrllqEDSSPL-----LRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEA 346
Cdd:PRK04837  98 QIH-----------ADAEPLaqatgLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  347 DRMIDMGFEGDIRTIFSYF--KGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEAKMVYL 424
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  425 LECLQKT-PPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQH 503
Cdd:PRK04837 247 QTLIEEEwPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 21071032  504 VINYDMPEEIENYVHRIGRTGRSGNTGIATTFinkACDESVL 545
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISL---ACEEYAL 365
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 182-560 2.48e-68

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 232.53  E-value: 2.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFtLPVIMFCLEQEKRLPFSKREGPYGL 261
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAF-LVAVMNRLLSRPALADRKPEDPRAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  262 IICPSRELARQTHGileyycRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLL-QKKMVSLDICRY 340
Cdd:PRK04537  89 ILAPTRELAIQIHK------DAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  341 LALDEADRMIDMGFEGDIRTIFSYF--KGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEE 418
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  419 AKMVYLLECLQKTP-PPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLD 497
Cdd:PRK04537 243 EKQTLLLGLLSRSEgARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLH 322

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071032  498 FPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFinkACdESVLMDLKALLLEAKQKVP 560
Cdd:PRK04537 323 IDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF---AC-ERYAMSLPDIEAYIEQKIP 381
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 171-396 1.73e-67

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: 219.17  E-value: 1.73e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 171 VEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQekrL 250
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQ---R 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 251 PFSKREGPYGLIICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLL-- 328
Cdd:cd17953  79 PVKPGEGPIGLIMAPTRELALQIYVECKKFSKALG------LRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILta 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071032 329 -QKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17953 153 nNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 192-396 5.22e-65

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: 211.89  E-value: 5.22e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKrlpFSKREGPYGLIICPSRELAR 271
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRE---LEKGEGPIAVIVAPTRELAQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17952  78 QIYLEAKKFGKAYN------LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17952 152 MGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 166-402 4.81e-64

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: 211.75  E-value: 4.81e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 166 KY-HILVE--GDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMF 242
Cdd:cd18052  25 KYdEIPVEvtGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 243 CLEQEKRLP-FSKREGPYGLIICPSRELARQTHgiLEyyCRLLQEDSSplLRCALCIGGMSVKEQMETIRHGVHMMVATP 321
Cdd:cd18052 105 MMKEGLTASsFSEVQEPQALIVAPTRELANQIF--LE--ARKFSYGTC--IRPVVVYGGVSVGHQIRQIEKGCHILVATP 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 322 GRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL-VKPVTI 396
Cdd:cd18052 179 GRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFL 258


                ....*.
gi 21071032 397 NVGRAG 402
Cdd:cd18052 259 TVGRVG 264
PTZ00424 PTZ00424
helicase 45; Provisional
 180-536 5.01e-63

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 213.53  E-value: 5.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  180 IKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFSKReGPY 259
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-------QLIDYDLN-ACQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  260 GLIICPSRELARQTHGI---LEYYCRLlqedsspllRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLD 336
Cdd:PTZ00424  99 ALILAPTRELAQQIQKVvlaLGDYLKV---------RCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVD 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  337 ICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVgRAGAASLDVIQEVeYV- 415
Cdd:PTZ00424 170 DLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILV-KKDELTLEGIRQF-YVa 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  416 --KEEAKMVYLLECLQK-TPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVA 492
Cdd:PTZ00424 248 veKEEWKFDTLCDLYETlTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 21071032  493 SKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:PTZ00424 328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFV 371
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 192-396 8.89e-63

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 206.79  E-value: 8.89e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDGPYALILAPTRELAQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QthgILEYYCRLLQedssPL-LRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMI 350
Cdd:cd17945  81 Q---IEEETQKFAK----PLgIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032 351 DMGFEGDIRTIFSYF--------------------KGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17945 154 DMGFEPQVTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 182-536 2.66e-61

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 214.71  E-value: 2.66e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKrlpfskreGPYGL 261
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELK--------APQIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  262 IICPSRELARQTHGILEYYCRLLQEdssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYL 341
Cdd:PRK11634  79 VLAPTRELAVQVAEAMTDFSKHMRG-----VNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  342 ALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYV----KE 417
Cdd:PRK11634 154 VLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVwgmrKN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  418 EAkMVYLLEClqKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLD 497
Cdd:PRK11634 234 EA-LVRFLEA--EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLD 310

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 21071032  498 FPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:PRK11634 311 VERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 161-399 2.89e-61

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: 203.32  E-value: 2.89e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 161 ERVRKKYHILVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVI 240
Cdd:cd18049   4 EQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 241 MFCLEQekrlPFSKR-EGPYGLIICPSRELARQTHGILEYYCRLLQEDSSpllrcalCI-GGMSVKEQMETIRHGVHMMV 318
Cdd:cd18049  84 VHINHQ----PFLERgDGPICLVLAPTRELAQQVQQVAAEYGRACRLKST-------CIyGGAPKGPQIRDLERGVEICI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 319 ATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINV 398
Cdd:cd18049 153 ATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232


                .
gi 21071032 399 G 399
Cdd:cd18049 233 G 233
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 192-397 5.85e-59

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: 196.05  E-value: 5.85e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEkrlPFSKREGPYGLIICPSRELAR 271
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQP---PLERGDGPIVLVLAPTRELAQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17966  78 QIQQEANKFGGSSR------LRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17966 152 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 192-396 9.19e-58

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 192.85  E-value: 9.19e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFSKREGPY--GLIICPSREL 269
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL-------ERLLYRPKKKAAtrVLVLVPTREL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 270 ARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKM-VSLDICRYLALDEADR 348
Cdd:cd17947  74 AMQCFSVLQQLAQFTD------ITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADR 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21071032 349 MIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17947 148 MLEEGFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 152-399 1.29e-57

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: 195.23  E-value: 1.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 152 VLSMSEERHERVRKKYHILVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGK 231
Cdd:cd18050  33 VARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGK 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 232 TLVFTLPVIMFCLEQekrlPFSKR-EGPYGLIICPSRELARQTHGILEYYCRllqedsSPLLRCALCIGGMSVKEQMETI 310
Cdd:cd18050 113 TLAYLLPAIVHINHQ----PYLERgDGPICLVLAPTRELAQQVQQVADDYGK------SSRLKSTCIYGGAPKGPQIRDL 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 311 RHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSAL 390
Cdd:cd18050 183 ERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFL 262


                ....*....
gi 21071032 391 VKPVTINVG 399
Cdd:cd18050 263 RDYVQINIG 271
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 408-536 1.88e-57

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: 189.26  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 408 VIQEVEYVKEEAKMVYLLECL--QKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDV 485
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21071032 486 LVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFI 536
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 166-403 3.52e-57

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: 192.95  E-value: 3.52e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 166 KYH-ILVE--GDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVI-- 240
Cdd:cd18051   3 KYEdIPVEatGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsq 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 241 MF------CLEQEKRLPFSKREGPYGLIICPSRELARQthgILEYYCRLLQEDsspLLRCALCIGGMSVKEQMETIRHGV 314
Cdd:cd18051  83 IYeqgpgeSLPSESGYYGRRKQYPLALVLAPTRELASQ---IYDEARKFAYRS---RVRPCVVYGGADIGQQMRDLERGC 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 315 HMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSAL 390
Cdd:cd18051 157 HLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFL 236

                       250
                ....*....|...
gi 21071032 391 VKPVTINVGRAGA 403
Cdd:cd18051 237 DNYIFLAVGRVGS 249
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 182-397 2.37e-55

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: 186.74  E-value: 2.37e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqEKRLPFSKREGPYGL 261
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI------EKLKAHSPTVGARAL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 262 IICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYL 341
Cdd:cd17959  76 ILSPTRELALQTLKVTKELGKFTD------LRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYV 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032 342 ALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17959 150 VFDEADRLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 192-397 6.17e-54

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: 182.78  E-value: 6.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLpfsKREGPYGLIICPSRELAR 271
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANL---KKGQVGALIISPTRELAT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCrllqEDSSPLLRCALCIGGMSVKEQMETI-RHGVHMMVATPGRLMDLLQK-----KMVSLDIcryLALDE 345
Cdd:cd17960  78 QIYEVLQSFL----EHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRkadkvKVKSLEV---LVLDE 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21071032 346 ADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17960 151 ADRLLDLGFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 183-394 7.55e-52

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 177.03  E-value: 7.55e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLpfskREGPYG-- 260
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-------QRL----SEDPYGif 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 261 -LIICPSRELARQthgILEYYCRLlqedSSPL-LRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQ---KKMVSL 335
Cdd:cd17955  70 aLVLTPTRELAYQ---IAEQFRAL----GAPLgLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVL 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21071032 336 DICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPV 394
Cdd:cd17955 143 SRVKFLVLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 182-396 2.58e-51

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: 175.58  E-value: 2.58e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLpfskregpYGL 261
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF--------FAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 262 IICPSRELARQthgILEYYCRLlqeDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQK-KMVSLDICRY 340
Cdd:cd17954  73 VLAPTRELAQQ---ISEQFEAL---GSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKF 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032 341 LALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17954 147 LVMDEADRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 190-390 3.93e-51

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: 175.46  E-value: 3.93e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 190 AAILRGLKKKGIHHPTPIQIQGIPTILS-GRDMIGIAFTGSGKTLVFTLPVIMFCLeqeKRLPFSKREGPYGLIICPSRE 268
Cdd:cd17964   3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLL---NTKPAGRRSGVSALIISPTRE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 269 LARQthgILEYYCRLLQedSSPLLRCALCIGGMSVKEQM-ETIRHGVHMMVATPGRLMDLLQKKMV--SLDICRYLALDE 345
Cdd:cd17964  80 LALQ---IAAEAKKLLQ--GLRKLRVQSAVGGTSRRAELnRLRRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDE 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21071032 346 ADRMIDMGFEGDIRTIFSY----FKGQRQTLLFSATMPKKIQNFAKSAL 390
Cdd:cd17964 155 ADRLLDMGFRPDLEQILRHlpekNADPRQTLLFSATVPDEVQQIARLTL 203
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 205-385 2.24e-50

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: 171.66  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   205 TPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFsKREGPYGLIICPSRELARQTHGILEYYCRLL 284
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPAL-------EALDK-LDNGPQALVLAPTRELAEQIYEELKKLGKGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   285 QedssplLRCALCIGGMSVKEQMETIRhGVHMMVATPGRLMDLLQKKmVSLDICRYLALDEADRMIDMGFEGDIRTIFSY 364
Cdd:pfam00270  73 G------LKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRR 144

                         170       180
                  ....*....|....*....|.
gi 21071032   365 FKGQRQTLLFSATMPKKIQNF 385
Cdd:pfam00270 145 LPKKRQILLLSATLPRNLEDL 165
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 192-397 4.09e-49

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: 169.85  E-value: 4.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfclEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI----ELLYKLKFKPRNGTGVIIISPTRELAL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQEDsspllrCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQ-KKMVSLDICRYLALDEADRMI 350
Cdd:cd17942  77 QIYGVAKELLKYHSQT------FGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRIL 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21071032 351 DMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALV-KPVTIN 397
Cdd:cd17942 151 EIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKkKPLYVG 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 192-398 7.88e-49

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 169.01  E-value: 7.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVimfcLEQEKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPL----LEKLYRERWTPEDGLGALIISPTRELAM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILeyycRLLQEDSSplLRCALCIGGMSVKEQMETIrHGVHMMVATPGRLMDLLQKKmVSLDI--CRYLALDEADRM 349
Cdd:cd17941  77 QIFEVL----RKVGKYHS--FSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDET-PGFDTsnLQMLVLDEADRI 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21071032 350 IDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINV 398
Cdd:cd17941 149 LDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 192-396 2.33e-48

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: 167.64  E-value: 2.33e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEkrLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQP--IPREQRNGPGVLVLTPTRELAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHG-ILEYYCRLLQedsspllrcALCI-GGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRM 349
Cdd:cd17958  79 QIEAeCSKYSYKGLK---------SVCVyGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21071032 350 IDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17958 150 LDMGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 183-397 1.01e-47

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: 165.93  E-value: 1.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPvimfCLEQEKrlpfSKREGPYGLI 262
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP----ILEKID----PKKDVIQALI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 263 ICPSRELARQTHGIleyyCRLLQEdsSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLA 342
Cdd:cd17940  73 LVPTRELALQTSQV----CKELGK--HMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLV 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21071032 343 LDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTIN 397
Cdd:cd17940 147 LDEADKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 194-396 4.51e-46

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: 161.98  E-value: 4.51e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 194 RGLKKK-GIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRlpFSKREGPYGLIICPSRELARQ 272
Cdd:cd17949   3 SHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPR--VDRSDGTLALVLVPTRELALQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 273 THGILEyycRLLQedSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQK-KMVSLDICRYLALDEADRMID 351
Cdd:cd17949  81 IYEVLE---KLLK--PFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLD 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21071032 352 MGFEGDIRTIFSYFKGQ-------------RQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17949 156 MGFEKDITKILELLDDKrskaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEXDc smart00487
DEAD-like helicases superfamily;
196-409 1.21e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.35  E-value: 1.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    196 LKKKGIHHPTPIQIQGIPTILSG-RDMIGIAFTGSGKTLVFTLPVIMFcleqekrlpFSKREGPYGLIICPSRELARQTH 274
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA---------LKRGKGGRVLVLVPTRELAEQWA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    275 GILEYYCrllqedSSPLLRCALCIGGMSVKEQMETIRHGV-HMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMG 353
Cdd:smart00487  72 EELKKLG------PSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032    354 FEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVI 409
Cdd:smart00487 146 FGDQLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 192-399 2.99e-45

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: 159.29  E-value: 2.99e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfcleqeKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQ------KLGKPRKKKGLRALILAPTRELAS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEyycRLLQEDSsplLRCALCIGGMSVK-EQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMI 350
Cdd:cd17957  75 QIYRELL---KLSKGTG---LRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21071032 351 DMGFEGDIRTIFSYFKGQR-QTLLFSATMPKKIQNFAKSALVKPVTINVG 399
Cdd:cd17957 149 EPGFREQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 192-396 1.62e-44

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 156.94  E-value: 1.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEqekrlpfsKREGPYGLIICPSRELAR 271
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT--------EHRNPSALILTPTRELAV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLqedssPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17962  73 QIEDQAKELMKGL-----PPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17962 148 MGFQQQVLDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 192-388 7.34e-44

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: 156.63  E-value: 7.34e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIP-TILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQ-EKRLPFSKREGPYGLIICPSREL 269
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQkSSNGVGGKQKPLRALILTPTREL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 270 ARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKK---MVSLDICRYLALDEA 346
Cdd:cd17946  81 AVQVKDHLKAIAKYTN------IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21071032 347 DRMIDMG-FEgDIRTIFSYFKG-------QRQTLLFSATMPKKIQNFAKS 388
Cdd:cd17946 155 DRMLEKGhFA-ELEKILELLNKdragkkrKRQTFVFSATLTLDHQLPLKL 203
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 183-378 1.65e-41

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: 149.39  E-value: 1.65e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLeqekrlpfskregpyGLI 262
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV---------------ALI 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 263 ICPSRELARQTHGILEYYCRLLqedSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLA 342
Cdd:cd17938  66 LEPSRELAEQTYNCIENFKKYL---DNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFV 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21071032 343 LDEADRMIDMGFEGDIRTIFSYF-----KGQR-QTLLFSATM 378
Cdd:cd17938 143 LDEADRLLSQGNLETINRIYNRIpkitsDGKRlQVIVCSATL 184
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 192-396 9.31e-41

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: 147.35  E-value: 9.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLpfSKREGPYGLIICPSRELAR 271
Cdd:cd17961   5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAES--GEEQGTRALILVPTRELAQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILE---YYCRllqedssPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKK-MVSLDICRYLALDEAD 347
Cdd:cd17961  83 QVSKVLEqltAYCR-------KDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEAD 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21071032 348 RMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17961 156 LVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 185-396 5.75e-39

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


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 142.08  E-value: 5.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 185 EMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFSKREgPYGLIIC 264
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL-------QRIDTTVRE-TQALVLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 265 PSRELARQThgilEYYCRLLQEDSSplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALD 344
Cdd:cd17939  73 PTRELAQQI----QKVVKALGDYMG--VKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLD 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21071032 345 EADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17939 147 EADEMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 192-396 1.48e-38

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: 140.86  E-value: 1.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLeqekrlpfSKREGPYGLIICPSRELAR 271
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD--------LERRHPQVLILAPTREIAV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLQEdssplLRCALCIGGMSVKEQMETIRhGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMID 351
Cdd:cd17943  73 QIHDVFKKIGKKLEG-----LKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21071032 352 MGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17943 147 GSFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 183-396 1.38e-36

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: 135.65  E-value: 1.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPFSKREgPYGLI 262
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISIL-------QQIDTSLKA-TQALV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 263 ICPSRELARQTHGI---LEYYCRLlqedsspllRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICR 339
Cdd:cd18046  73 LAPTRELAQQIQKVvmaLGDYMGI---------KCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIK 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071032 340 YLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd18046 144 MFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 419-527 5.81e-35

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: 127.71  E-value: 5.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   419 AKMVYLLECLQKTPPP-VLIFAEKKADVDAihEYLLLK-GVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGL 496
Cdd:pfam00271   1 EKLEALLELLKKERGGkVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 21071032   497 DFPAIQHVINYDMPEEIENYVHRIGRTGRSG 527
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 183-396 1.25e-34

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: 130.28  E-value: 1.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfCLEqekrlpFSKREgPYGLI 262
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLD------IQVRE-TQALI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 263 ICPSRELARQTHGILEYYCRLLQedssplLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLA 342
Cdd:cd18045  73 LSPTRELAVQIQKVLLALGDYMN------VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLV 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21071032 343 LDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd18045 147 LDEADEMLNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 192-380 1.47e-34

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: 130.95  E-value: 1.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQeKRLPFSKREGPYGLIICPSRELAR 271
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRY-KLLAEGPFNAPRGLVITPSRELAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 272 QTHGILEYYCRLLqedssPLLrcALCIGGMSVKEQMETIRHG-VHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMI 350
Cdd:cd17948  80 QIGSVAQSLTEGL-----GLK--VKVITGGRTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21071032 351 DMGFEGDIRTIFSYF---KGQR----------QTLLFSATMPK 380
Cdd:cd17948 153 DDSFNEKLSHFLRRFplaSRRSentdgldpgtQLVLVSATMPS 195
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 189-396 1.85e-34

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: 129.62  E-value: 1.85e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 189 PAAILRGLKKKGIHHPTPIQIQGIPTILSG--RDMIGIAFTGSGKTLVFTLPviMFCleqekRLPFSKREgPYGLIICPS 266
Cdd:cd17963   2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLA--MLS-----RVDPTLKS-PQALCLAPT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 267 RELARQthgILEYYCRLLQEDSsplLRCALCIGGMSVKEQmETIRHgvHMMVATPGRLMDLLQKKMVSLDICRYLALDEA 346
Cdd:cd17963  74 RELARQ---IGEVVEKMGKFTG---VKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEA 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 21071032 347 DRMIDM-GFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd17963 145 DVMLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 196-387 1.13e-30

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 119.18  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 196 LKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCleQEKRLPFSKREGPYGLIICPSRELARQTHG 275
Cdd:cd17944   5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QEDQQPRKRGRAPKVLVLAPTRELANQVTK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 276 ILEyycrllqeDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFE 355
Cdd:cd17944  83 DFK--------DITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFA 154

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21071032 356 GDIRTIFS--YFKGQR---QTLLFSATMPKKIQNFAK 387
Cdd:cd17944 155 EQVEEILSvsYKKDSEdnpQTLLFSATCPDWVYNVAK 191
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 182-398 2.06e-30

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: 118.60  E-value: 2.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 182 SFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVimfcLEQEKRLPfskrEGPYGL 261
Cdd:cd17950   3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLST----LQQLEPVD----GQVSVL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 262 IICPSRELARQthgILEYYCRLLQedSSPLLRCALCIGGMSVKEQMETIRHGV-HMMVATPGRLMDLLQKKMVSLDICRY 340
Cdd:cd17950  75 VICHTRELAFQ---ISNEYERFSK--YMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKH 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21071032 341 LALDEADRMI-DMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINV 398
Cdd:cd17950 150 FVLDECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
HELICc smart00490
helicase superfamily c-terminal domain;
446-527 1.62e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 111.53  E-value: 1.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032    446 DAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGR 525
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 21071032    526 SG 527
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 192-385 7.89e-27

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 108.87  E-value: 7.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 192 ILRGLKKKGIHHPTPIQIQGIPTILSG---------RDMIGIAFTGSGKTLVFTLPVImfcleQEkrlpFSKREGP--YG 260
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA----LSKRVVPrlRA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 261 LIICPSRELARQTHGILEYYCRllqedSSPLLRCALCiGGMSVKEQMETIRHGVH--------MMVATPGRLMD-LLQKK 331
Cdd:cd17956  72 LIVVPTKELVQQVYKVFESLCK-----GTGLKVVSLS-GQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDhLNSTP 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071032 332 MVSLDICRYLALDEADRMIDMGFEG-------------------DIRTIFSYFKGQR-QTLLFSATM---PKKIQNF 385
Cdd:cd17956 146 GFTLKHLRFLVIDEADRLLNQSFQDwletvmkalgrptapdlgsFGDANLLERSVRPlQKLLFSATLtrdPEKLSSL 222
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
227-505 3.54e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 88.16  E-value: 3.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 227 TGSGKTLVFTLpvIMFCLEQEKRLpfskregpygLIICPSRELARQTHgilEYYCRLLQEDSSPLLRcalciggmsvkeq 306
Cdd:COG1061 109 TGTGKTVLALA--LAAELLRGKRV----------LVLVPRRELLEQWA---EELRRFLGDPLAGGGK------------- 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 307 metIRHGVHMMVATPGRLMDLLQKKMVSlDICRYLALDEADRMIDMGFegdiRTIFSYFKGQRqTLLFSAT------MPK 380
Cdd:COG1061 161 ---KDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgREI 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 381 KIQNFA-----------------KSALVKPVTINVGRAGAASLDVIQEVEYV---KEEAKMVYLLECLQKTPP--PVLIF 438
Cdd:COG1061 232 LLFLFDgivyeyslkeaiedgylAPPEYYGIRVDLTDERAEYDALSERLREAlaaDAERKDKILRELLREHPDdrKTLVF 311

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071032 439 AEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVI 505
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
208-535 7.38e-18

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 86.73  E-value: 7.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 208 QIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfcleqekrlpfskREGPyGLIIcpsrelarqthgileyycrllqed 287
Cdd:COG0514  22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL-------------LPGL-TLVV------------------------ 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 288 sSPLLrcAL----------------CI-GGMSVKEQMET---IRHG-VHMMVATPGRLM-----DLLQKKMVSLdicryL 341
Cdd:COG0514  64 -SPLI--ALmkdqvdalraagiraaFLnSSLSAEERREVlraLRAGeLKLLYVAPERLLnprflELLRRLKISL-----F 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 342 ALDEA--------D-----RMIdmgfeGDIRTIFsyfkGQRQTLLFSATMPKKIQN--FAKSALVKPVTINvgragaASL 406
Cdd:COG0514 136 AIDEAhcisqwghDfrpdyRRL-----GELRERL----PNVPVLALTATATPRVRAdiAEQLGLEDPRVFV------GSF 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 407 DV--IQ-EVEYVKEEAKMVYLLECLQKTPP-PVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGK 482
Cdd:COG0514 201 DRpnLRlEVVPKPPDDKLAQLLDFLKEHPGgSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDE 280

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 21071032 483 KDVLVATdVA-SKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTF 535
Cdd:COG0514 281 VDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 183-380 2.58e-16

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: 78.96  E-value: 2.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 183 FKEMK-FP---AAILRGLKKKGIH-----HPTPIQIQGIPtILSGRDMIGI-----------------AFTGSGKTLVFT 236
Cdd:cd17965   1 FDQLKlLPsvrEAIIKEILKGSNKtdeeiKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 237 LPVIMFCLEQEKRL---------PFSKREGPYGLIICPSRELARQTHGILE-------YYCRLLQEDSSPllrcalcigg 300
Cdd:cd17965  80 APLLDYLKRQEQEPfeeaeeeyeSAKDTGRPRSVILVPTHELVEQVYSVLKklshtvkLGIKTFSSGFGP---------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 301 mSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPK 380
Cdd:cd17965 150 -SYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK 228
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
420-527 4.02e-16

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 82.09  E-value: 4.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 420 KMVYLLECLQKT-----PPPVLIFAEKKADVDAIHEYLLLKGVEAV-----AIHGGKD---QEERTKAIEAFREGKKDVL 486
Cdd:COG1111 336 KLSKLREILKEQlgtnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqASKEGDKgltQKEQIEILERFRAGEFNVL 415

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21071032 487 VATDVASKGLDFPAIQHVINYD-MPEEIEnYVHRIGRTGRSG 527
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKR 456
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 419-521 1.11e-14

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: 70.97  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 419 AKMVYLLECLQKTPPP---VLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKD--VLVATDVAS 493
Cdd:cd18793  11 GKLEALLELLEELREPgekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGG 90

                        90       100       110
                ....*....|....*....|....*....|....
gi 21071032 494 KGLDFPAIQHVINYDMP------EEIENYVHRIG 521
Cdd:cd18793  91 VGLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 180-398 2.08e-14

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: 73.13  E-value: 2.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 180 IKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSG--RDMIGIAFTGSGKTLVFTLPVImfcleqeKRLPfSKREG 257
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML-------SRVD-ALKLY 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 258 PYGLIICPSRELARQTHGILEYYCRLlqedsspllrCAlcigGMSVKEQMETIRHG------VHMMVATPGRLMDLLQK- 330
Cdd:cd18048  89 PQCLCLSPTFELALQTGKVVEEMGKF----------CV----GIQVIYAIRGNRPGkgtdieAQIVIGTPGTVLDWCFKl 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071032 331 KMVSLDICRYLALDEADRMIDM-GFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINV 398
Cdd:cd18048 155 RLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 436-535 3.64e-13

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: 66.85  E-value: 3.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 436 LIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIEN 515
Cdd:cd18794  34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113

                        90       100
                ....*....|....*....|
gi 21071032 516 YVHRIGRTGRSGNTGIATTF 535
Cdd:cd18794 114 YYQESGRAGRDGLPSECILF 133
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 227-377 7.58e-13

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 66.27  E-value: 7.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 227 TGSGKTLVFTLPVIMFCLEQEKRLpfskregpygLIICPSRELARQTHgileyycRLLQEDSSPLLRCALCIGGMSVKEQ 306
Cdd:cd00046  10 TGSGKTLAALLAALLLLLKKGKKV----------LVLVPTKALALQTA-------ERLRELFGPGIRVAVLVGGSSAEER 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071032 307 METIRHGVHMMVATPGRL-MDLLQKKMVSLDICRYLALDEADRMIDMGFEGDI--RTIFSYFKGQRQTLLFSAT 377
Cdd:cd00046  73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 413-523 2.26e-12

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 69.87  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 413 EYVKEEAKMVYLLECLQKTPP---PVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGK--KDVLV 487
Cdd:COG0553 527 ELSGRSAKLEALLELLEELLAegeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLI 606

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 488 ATDVASKGLDFPAIQHVINYDMP-----EE-----IenyvHRIGRT 523
Cdd:COG0553 607 SLKAGGEGLNLTAADHVIHYDLWwnpavEEqaidrA----HRIGQT 648
PRK13766 PRK13766
Hef nuclease; Provisional
 410-527 5.61e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 68.75  E-value: 5.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  410 QEVEYVKEEAKMVYLLECLQKTPPP-VLIFAEKKADVDAIHEYLLLKGVEAVAIHG--------GKDQEERTKAIEAFRE 480
Cdd:PRK13766 342 LDIEHPKLEKLREIVKEQLGKNPDSrIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRA 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 21071032  481 GKKDVLVATDVASKGLDFPAIQHVINYD-MPEEIENyVHRIGRTGRSG 527
Cdd:PRK13766 422 GEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGRQE 468
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 181-396 1.51e-11

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: 63.97  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 181 KSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSG--RDMIGIAFTGSGKTLVFTLPVIMFCleqEKRLPFSKregp 258
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQ---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 259 yGLIICPSRELARQTHGILEYYCRLLqedssPLLRCALCIGGmsvkEQMET-IRHGVHMMVATPGRLMD-LLQKKMVSLD 336
Cdd:cd18047  74 -CLCLSPTYELALQTGKVIEQMGKFY-----PELKLAYAVRG----NKLERgQKISEQIVIGTPGTVLDwCSKLKFIDPK 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21071032 337 ICRYLALDEADRMIDMGFEGD--IRTIFSYFKGQrQTLLFSATMPKKIQNFAKSALVKPVTI 396
Cdd:cd18047 144 KIKVFVLDEADVMIATQGHQDqsIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDPNVI 204
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 466-522 4.14e-11

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: 61.07  E-value: 4.14e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071032 466 KDQEErtkAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGR 522
Cdd:cd18802  77 RKQKE---TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 436-527 1.04e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.27  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  436 LIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIEN 515
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319

                         90
                 ....*....|..
gi 21071032  516 YVHRIGRTGRSG 527
Cdd:PRK11057 320 YYQETGRAGRDG 331
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 420-525 4.02e-09

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 55.44  E-value: 4.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 420 KMVYLLECL----QKTPPP----VLIFAEKKADVDAIHEYLL--LKGVEAVAIHG--------GKDQEERTKAIEAFREG 481
Cdd:cd18801  10 KLEKLEEIVkehfKKKQEGsdtrVIIFSEFRDSAEEIVNFLSkiRPGIRATRFIGqasgksskGMSQKEQKEVIEQFRKG 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21071032 482 KKDVLVATDVASKGLDFPAIQHVINYD-MPEEIENyVHRIGRTGR 525
Cdd:cd18801  90 GYNVLVATSIGEEGLDIGEVDLIICYDaSPSPIRM-IQRMGRTGR 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 485-536 2.18e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 51.55  E-value: 2.18e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21071032 485 VLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNT-GIATTFI 536
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 189-532 1.05e-07

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: 55.23  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 189 PAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQekrlpfskrEGPYGLIICPSRE 268
Cdd:COG1205  42 PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED---------PGATALYLYPTKA 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 269 LAR-QTHGILEYYCRLLQEdssplLRCALCIGGMSVKEQmETIRHGVHMMVATPgrlmDllqkkMVSLDI---------- 337
Cdd:COG1205 113 LARdQLRRLRELAEALGLG-----VRVATYDGDTPPEER-RWIREHPDIVLTNP----D-----MLHYGLlphhtrwarf 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 338 ---CRYLALDEA---------------DRMidmgfegdiRTIFSYFKGQRQTLLFSATM--PKKiqnFAkSALV-KPVTI 396
Cdd:COG1205 178 frnLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIgnPAE---HA-ERLTgRPVTV 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 397 nVGRAGAAS-----------LDVIQEVEYVKEEAKMVyLLECLQ---KTpppvLIFAEKKADVDAIHEYL---LLKGVEA 459
Cdd:COG1205 245 -VDEDGSPRgertfvlwnppLVDDGIRRSALAEAARL-LADLVReglRT----LVFTRSRRGAELLARYArraLREPDLA 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 460 VAI---HGGKDQEERTKAIEAFREGKKDVLVAT-------DVAskGLDFpaiqhVINYDMPEEIENYVHRIGRTGRSGNT 529
Cdd:COG1205 319 DRVaayRAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQD 391


                ...
gi 21071032 530 GIA 532
Cdd:COG1205 392 SLV 394
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 457-528 4.69e-07

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 49.57  E-value: 4.69e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071032 457 VEAVAIHGGK-DQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGN 528
Cdd:cd18796  68 PDFIALHHGSlSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
189-527 9.37e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 48.74  E-value: 9.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 189 PAAILRGLKKKGIHHPTPIQIQGIP-TILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKrlpfskregpyGLIICPSR 267
Cdd:COG1204   8 LEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK-----------ALYIVPLR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 268 ELARQTHGILEyycRLLQEDSsplLRCALCIGGMSVKEQmETIRHGVhmMVATPGRLMDLLQKK---MVSLDicrYLALD 344
Cdd:COG1204  77 ALASEKYREFK---RDFEELG---IKVGVSTGDYDSDDE-WLGRYDI--LVATPEKLDSLLRNGpswLRDVD---LVVVD 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 345 EAdRMIDMGFEG----DIRTIFSYFKGQRQTLLFSATMPKkIQNFAK---SALVK----PVTINVGRAGAASLDVIQEVE 413
Cdd:COG1204 145 EA-HLIDDESRGptleVLLARLRRLNPEAQIVALSATIGN-AEEIAEwldAELVKsdwrPVPLNEGVLYDGVLRFDDGSR 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 414 YVKEEAkmVYLLECLQKTPPPVLIFAEKKADV---------------------------DAIHEY------------LLL 454
Cdd:COG1204 223 RSKDPT--LALALDLLEEGGQVLVFVSSRRDAeslakkladelkrrltpeereeleelaEELLEVseethtnekladCLE 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 455 KGVeavAIH-GGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAiQHVI--------NYDMP-EEIENYvhrIGRTG 524
Cdd:COG1204 301 KGV---AFHhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPA-RRVIirdtkrggMVPIPvLEFKQM---AGRAG 373


                ...
gi 21071032 525 RSG 527
Cdd:COG1204 374 RPG 376
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 435-502 1.52e-05

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 45.32  E-value: 1.52e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21071032 435 VLIFAEKKADVDAIHEYLLLKgveavAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFP----AIQ 502
Cdd:cd18789  52 IIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeanvAIQ 118
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 414-531 2.03e-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: 45.37  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 414 YVKEEAKMVYLLECLQKTPPPVLIFAEK---KADVDAIHEYLLLKGVEAVAIHggkdqEERTKAIEAFREGKKDVLVAT- 489
Cdd:cd18798   6 YIEDSDSLEKLLELVKKLGDGGLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVa 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21071032 490 ---DVASKGLDFPA-IQHVINYDMPeeIENYVHRIGRTGRSGNTGI 531
Cdd:cd18798  81 syyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLYAGGL 124
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 206-381 1.13e-04

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 43.78  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 206 PIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfcleqekrlpFSKREGPYGLIICPSRELARQthgileyycrllQ 285
Cdd:cd18018  15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----------LRRRGPGLTLVVSPLIALMKD------------Q 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 286 EDSSPLLRCALCIGGMSVKEQMET----IRHG-VHMMVATPGRLMD------LLQKKMVSLdicryLALDEADRMIDMG- 353
Cdd:cd18018  73 VDALPRAIKAAALNSSLTREERRRilekLRAGeVKILYVSPERLVNesfrelLRQTPPISL-----LVVDEAHCISEWSh 147

                       170       180       190
                ....*....|....*....|....*....|..
gi 21071032 354 -FEGDIRTIFSY---FKGQRQTLLFSATMPKK 381
Cdd:cd18018 148 nFRPDYLRLCRVlreLLGAPPVLALTATATKR 179
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
203-274 1.36e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.09  E-value: 1.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071032 203 HPTPIQIQGIPTILSGRDMIGIAFTGSGKTL-VFtLPVIMFCLEQEKrlPFSKREGPYGLIICPSRELARQTH 274
Cdd:COG1201  24 APTPPQREAWPAIAAGESTLLIAPTGSGKTLaAF-LPALDELARRPR--PGELPDGLRVLYISPLKALANDIE 93
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 205-379 1.98e-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: 42.63  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 205 TPIQIQGIPTI-LSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFskregpygliICPSRELARQThgileyyCRL 283
Cdd:cd17921   3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVY----------IAPTRALVNQK-------EAD 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 284 LQEDSSPL-LRCALCIGGMSVKEQMETIRHGVhmmVATPGRLMDLLQK-KMVSLDICRYLALDEAdRMIDMGFEGDI--R 359
Cdd:cd17921  66 LRERFGPLgKNVGLLTGDPSVNKLLLAEADIL---VATPEKLDLLLRNgGERLIQDVRLVVVDEA-HLIGDGERGVVleL 141

                       170       180
                ....*....|....*....|..
gi 21071032 360 TI--FSYFKGQRQTLLFSATMP 379
Cdd:cd17921 142 LLsrLLRINKNARFVGLSATLP 163
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 371-526 2.63e-04

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 43.71  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 371 TLLFSATMPKKIQNFAKSALVKPVTINV---GRAgaasLDVIQ---------EVEYVKEEAKMVYLLECLQKTPPPVLIF 438
Cdd:COG4098 250 LIYLTATPSKALQRQVKRGKLKVVKLPAryhGHP----LPVPKfkwlgnwkkRLRRGKLPRKLLKWLKKRLKEGRQLLIF 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 439 AEKKADVDAIHEYL--LLKGVEAVAIHGgKDqEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQ-HVINYDmpeeien 515
Cdd:COG4098 326 VPTIELLEQLVALLqkLFPEERIAGVHA-ED-PERKEKVQAFRDGEIPILVTTTILERGVTFPNVDvAVLGAD------- 396

                       170       180
                ....*....|....*....|.
gi 21071032 516 yvHRI----------GRTGRS 526
Cdd:COG4098 397 --HPVfteaalvqiaGRVGRS 415
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 444-527 3.56e-04

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 41.56  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 444 DVDAIHEYL--LLKGVEAVA-IHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFP-AIQHVInydmpEEIENY--- 516
Cdd:cd18811  46 AAVAMYEYLkeRFRPELNVGlLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPnATVMVI-----EDAERFgls 120

                        90
                ....*....|...
gi 21071032 517 -VHRI-GRTGRSG 527
Cdd:cd18811 121 qLHQLrGRVGRGD 133
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 200-527 4.16e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 43.73  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   200 GIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMfCleqekrlpfskreGPYGLIICPSRELarqthgILEY 279
Cdd:PLN03137  457 GNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALI-C-------------PGITLVISPLVSL------IQDQ 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   280 YCRLLQEDSSpllrCALCIGGMSVKEQMETIRH------GVHMMVATPGRLM--DLLQKKMVSLDICRYLA---LDEADR 348
Cdd:PLN03137  517 IMNLLQANIP----AASLSAGMEWAEQLEILQElsseysKYKLLYVTPEKVAksDSLLRHLENLNSRGLLArfvIDEAHC 592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   349 MIDMGFEgdirtifsyFKGQRQTLlfsATMPKKIQNFAKSALVKPVTINVGRagaaslDVIQEVEYVK--------EEAK 420
Cdd:PLN03137  593 VSQWGHD---------FRPDYQGL---GILKQKFPNIPVLALTATATASVKE------DVVQALGLVNcvvfrqsfNRPN 654

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   421 MVYLL-----ECLQKTPPPV---------LIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVL 486
Cdd:PLN03137  655 LWYSVvpktkKCLEDIDKFIkenhfdecgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINII 734

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 21071032   487 VATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSG 527
Cdd:PLN03137  735 CATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDG 775
PRK00254 PRK00254
ski2-like helicase; Provisional
 185-522 6.76e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 42.88  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  185 EMKFPAAILRGLKKKGIHHPTPIQIQGIPT-ILSGRDMIGIAFTGSGKTLVFTLPVIMFCLeqekrlpfskREGPYGLII 263
Cdd:PRK00254   5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLL----------REGGKAVYL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  264 CPSRELARQTHGILEYYCRLLqedssplLRCALCIGGMSVKEQMetiRHGVHMMVATPGRLMDLLQKKMVSLDICRYLAL 343
Cdd:PRK00254  75 VPLKALAEEKYREFKDWEKLG-------LRVAMTTGDYDSTDEW---LGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  344 DEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATM--PKKIQNFAKSALV----KPVTINVG------------------ 399
Cdd:PRK00254 145 DEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAEWLNAELVvsdwRPVKLRKGvfyqgflfwedgkierfp 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  400 -----------RAGAASL-----------------DVIQEVEYVKEEAKMVYLLECLQKTPPpvlifAEKKADVdaihey 451
Cdd:PRK00254 225 nsweslvydavKKGKGALvfvntrrsaekealelaKKIKRFLTKPELRALKELADSLEENPT-----NEKLKKA------ 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032  452 lLLKGVeaVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVI-------NYDMPE----EIENYVHRI 520
Cdd:PRK00254 294 -LRGGV--AFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIrdtkrysNFGWEDipvlEIQQMMGRA 370


                 ..
gi 21071032  521 GR 522
Cdd:PRK00254 371 GR 372
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 415-523 7.54e-04

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 42.87  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032   415 VKEEAKMVYL---LECLQKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAF-REG--KKDVLVA 488
Cdd:PLN03142  467 VENSGKMVLLdklLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGseKFVFLLS 546

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 21071032   489 TDVASKGLDFPAIQHVINYD------MPEEIENYVHRIGRT 523
Cdd:PLN03142  547 TRAGGLGINLATADIVILYDsdwnpqVDLQAQDRAHRIGQK 587
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 191-242 1.14e-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: 40.60  E-value: 1.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21071032 191 AILRglKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMF 242
Cdd:cd17920   2 QILK--EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL 51
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 227-346 1.57e-03

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 40.33  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 227 TGSGKTLVftlpVIMFCLEQEKRLPFSKREGPYGLIICPSRELARQTHGILEYYCrllqedsspLLRCALCIGGMSV--- 303
Cdd:cd18034  25 TGSGKTLI----AVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHT---------DLKVGEYSGEMGVdkw 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21071032 304 -----KEQMETIrhgvHMMVATPGRLMDLLQKKMVSLDICRYLALDEA 346
Cdd:cd18034  92 tkerwKEELEKY----DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 434-532 1.94e-03

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 39.07  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 434 PVLIFAEKKADVDAIHEYLLlkgveAVAI-HGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVIN----YD 508
Cdd:cd18795  45 PVLVFCSSRKECEKTAKDLA-----GIAFhHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYD 119

                        90       100       110
                ....*....|....*....|....*....|
gi 21071032 509 MPEEIE----NYVHRIGRTGRSG--NTGIA 532
Cdd:cd18795 120 GKGYRElsplEYLQMIGRAGRPGfdTRGEA 149
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 455-528 2.81e-03

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 38.78  E-value: 2.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21071032 455 KGVEAVAIH-GGKDQEERtKAIEA-FREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGN 528
Cdd:cd18797  64 PLASKVASYrAGYLAEDR-REIEAeLFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
SF2_C_suv3 cd18805
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ...
 456-535 5.18e-03

C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain]  Cd Length: 135  Bit Score: 37.54  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071032 456 GVEAVAIHGGKDQEERTKAIEAFREGKK--DVLVATDVASKGLDFPaIQHVINYDM------------PEEIENYVHRIG 521
Cdd:cd18805  42 GLKCAVIYGALPPETRRQQARLFNDPESgyDVLVASDAIGMGLNLN-IRRVIFSSLskfdgnemrplsPSEVKQIAGRAG 120

                        90
                ....*....|....
gi 21071032 522 RTGRSGNTGIATTF 535
Cdd:cd18805 121 RFGSHFPEGEVTTL 134
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 436-501 5.95e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 37.15  E-value: 5.95e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071032 436 LIFAEKKADVDAIHEYLLLKGVEAVAIHGG-KDQEERTKAIEAFREGKK--DVLVATDVASKGLDFPAI 501
Cdd:cd18799  10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDySDRERGDEALILLFFGELkpPILVTVDLLTTGVDIPEV 78
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
443-491 6.60e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 39.65  E-value: 6.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21071032 443 ADVDAIHEYL--LLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDV 491
Cdd:COG1200 488 QAAEETYEELreAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 448-499 7.13e-03

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 38.00  E-value: 7.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21071032 448 IHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFP 499
Cdd:cd18790  43 LTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLP 94
 
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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