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Conserved domains on  [gi|27469538|gb|AAH41801|]
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DEAD (Asp-Glu-Ala-Asp) box polypeptide 59 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00206 super family cl33426
DEAD-box ATP-dependent RNA helicase; Provisional
89-592 0e+00

DEAD-box ATP-dependent RNA helicase; Provisional


The actual alignment was detected with superfamily member PLN00206:

Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 549.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206  12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206  87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206 167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDcQTILVSATIPTSIEQLASQLLHN 401
Cdd:PLN00206 246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  402 PVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLFKPPVLVFVDCKLGADLLSEAVQKITGLKRISIHSEKSQ 481
Cdd:PLN00206 325 IILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  482 IERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIA 561
Cdd:PLN00206 405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
                        490       500       510
                 ....*....|....*....|....*....|..
gi 27469538  562 KRVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 592
Cdd:PLN00206 485 ALLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
 
Name Accession Description Interval E-value
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
89-592 0e+00

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 549.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206  12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206  87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206 167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDcQTILVSATIPTSIEQLASQLLHN 401
Cdd:PLN00206 246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  402 PVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLFKPPVLVFVDCKLGADLLSEAVQKITGLKRISIHSEKSQ 481
Cdd:PLN00206 325 IILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  482 IERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIA 561
Cdd:PLN00206 405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
                        490       500       510
                 ....*....|....*....|....*....|..
gi 27469538  562 KRVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 592
Cdd:PLN00206 485 ALLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
205-593 5.28e-129

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 385.65  E-value: 5.28e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFE-SKTPSALILTPTREL 283
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGF 363
Cdd:COG0513  84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 364 QQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLF 443
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 444 KppVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMP 523
Cdd:COG0513 243 R--AIVFCNTKRGADRLAEKLQK-RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 524 SSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRvkpTGSILPPQLLNSPYLHDQKRKEQQKDK 593
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIEEEELPGFEPVEEKRLERLKPK 386
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
214-406 1.42e-123

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: 363.02  E-value: 1.42e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKE 293
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 294 LMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILEN 373
Cdd:cd17962  81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 27469538 374 IPNDCQTILVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
227-394 1.78e-52

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: 177.43  E-value: 1.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   227 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLL 306
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   307 VGGLPLPPQLYRLqQHVKVIIATPGRLLDIIKQsSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSAT 386
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 27469538   387 IPTSIEQL 394
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
218-413 1.80e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.05  E-value: 1.80e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538    218 LKKSGYEVPTPIQMQMIPVGLLG-RDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAIQIERQAKELMS 296
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538    297 GLPRmKTVLLVGGLPLPPQLYRLQQHV-KVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIP 375
Cdd:smart00487  80 SLGL-KVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 27469538    376 NDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLP 413
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLE 196
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
378-554 9.80e-06

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 48.83  E-value: 9.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   378 CQTILVSATiPTSIE-QLASQLLHNPVRIiTGEKNlPCANVRQIILWVEDpakkkkLFEILNDKKLFKPPVLVFVDCKLG 456
Cdd:TIGR00631 384 NQVVYVSAT-PGPYElEQSGNVVEQIIRP-TGLLD-PEIEVRPTDGQVDD------LLSEIRQRVARNERVLVTTLTKKM 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   457 A----DLLSEAvqkitGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-----MPSSMD 527
Cdd:TIGR00631 455 AedltDYLKEL-----GIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSER 529
                         170       180
                  ....*....|....*....|....*..
gi 27469538   528 EYVHQIGRVGRlGQNGTAITFINNNSK 554
Cdd:TIGR00631 530 SLIQTIGRAAR-NVNGKVIMYADKITD 555
 
Name Accession Description Interval E-value
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
89-592 0e+00

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 549.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206  12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206  87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206 167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDcQTILVSATIPTSIEQLASQLLHN 401
Cdd:PLN00206 246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  402 PVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLFKPPVLVFVDCKLGADLLSEAVQKITGLKRISIHSEKSQ 481
Cdd:PLN00206 325 IILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  482 IERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIA 561
Cdd:PLN00206 405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
                        490       500       510
                 ....*....|....*....|....*....|..
gi 27469538  562 KRVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 592
Cdd:PLN00206 485 ALLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
205-593 5.28e-129

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 385.65  E-value: 5.28e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFE-SKTPSALILTPTREL 283
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGF 363
Cdd:COG0513  84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 364 QQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKKLF 443
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 444 KppVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMP 523
Cdd:COG0513 243 R--AIVFCNTKRGADRLAEKLQK-RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 524 SSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRvkpTGSILPPQLLNSPYLHDQKRKEQQKDK 593
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIEEEELPGFEPVEEKRLERLKPK 386
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
214-406 1.42e-123

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: 363.02  E-value: 1.42e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKE 293
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 294 LMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILEN 373
Cdd:cd17962  81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 27469538 374 IPNDCQTILVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
PTZ00110 PTZ00110
helicase; Provisional
168-590 3.86e-97

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 307.86  E-value: 3.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  168 YKEHPFILNLQEDQIENLKQQLGI-LVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILAS 246
Cdd:PTZ00110  94 YKEHPEVSALSSKEVDEIRKEKEItIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGI 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  247 ADTGSGKTAAFLLPVIMRALFESKT-----PSALILTPTRELAIQIERQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PTZ00110 174 AETGSGKTLAFLLPAIVHINAQPLLrygdgPIVLVLAPTRELAEQIREQCNKF-GASSKIRNTVAYGGVPKRGQIYALRR 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLL-H 400
Cdd:PTZ00110 253 GVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkE 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  401 NPVRIITGEKNL-PCANVRQIILWVEDPAKKKKLFEILndKKLFKP--PVLVFVDCKLGADLLSEAVqKITGLKRISIHS 477
Cdd:PTZ00110 333 EPVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLKMLL--QRIMRDgdKILIFVETKKGADFLTKEL-RLDGWPALCIHG 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  478 EKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLF 557
Cdd:PTZ00110 410 DKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLA 489
                        410       420       430
                 ....*....|....*....|....*....|...
gi 27469538  558 WDIAKRVKPTGSILPPQLLNSPYLHDQKRKEQQ 590
Cdd:PTZ00110 490 RDLVKVLREAKQPVPPELEKLSNERSNGTERRR 522
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
214-405 3.40e-85

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: 264.30  E-value: 3.40e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFES----KTPSALILTPTRELAIQIER 289
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 290 QAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLD 369
Cdd:cd00268  81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27469538 370 ILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
211-565 1.87e-77

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 253.58  E-value: 1.87e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  211 PEVLnHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS------ALILTPTRELA 284
Cdd:PRK10590  10 PDIL-RAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILTPTRELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:PRK10590  89 AQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVeDPAKKKKLFEILNDKKLFK 444
Cdd:PRK10590 168 HDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFV-DKKRKRELLSQMIGKGNWQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  445 pPVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPS 524
Cdd:PRK10590 247 -QVLVFTRTKHGANHLAEQLNK-DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPN 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 27469538  525 SMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRVK 565
Cdd:PRK10590 325 VPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
204-549 1.80e-74

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 244.85  E-value: 1.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  204 DFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAL-FESKTPSA---LILTP 279
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdFPRRKSGPpriLILTP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  280 TRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTML 359
Cdd:PRK11192  82 TRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  360 KMGFQQQVldilENIPNDC----QTILVSATIPTS-IEQLASQLLHNPVRIitgEKNLPCANVRQIILWVE--DPAKKKk 432
Cdd:PRK11192 161 DMGFAQDI----ETIAAETrwrkQTLLFSATLEGDaVQDFAERLLNDPVEV---EAEPSRRERKKIHQWYYraDDLEHK- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  433 lFEILndKKLFKPP----VLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRG 508
Cdd:PRK11192 233 -TALL--CHLLKQPevtrSIVFVRTRERVHELAGWLRK-AGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 27469538  509 LDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFI 549
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
204-550 4.13e-74

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 244.71  E-value: 4.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  204 DFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR---ALFEsktPSALILTPT 280
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKldvKRFR---VQALVLCPT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  281 RELAIQIERQAKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLK 360
Cdd:PRK11776  82 RELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  361 MGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNlpcanvrqiilwvEDPAKKKKLFEILNDK 440
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-------------DLPAIEQRFYEVSPDE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  441 KL---------FKP-PVLVF----VDCKLGADLLSEAvqkitGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLG 506
Cdd:PRK11776 229 RLpalqrlllhHQPeSCVVFcntkKECQEVADALNAQ-----GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 27469538  507 RGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFIN 550
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVA 347
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
222-596 2.45e-69

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 236.67  E-value: 2.45e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLPRM 301
Cdd:PRK11634  25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTI 381
Cdd:PRK11634 105 NVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  382 LVSATIPTSIEQLASQLLHNP--VRIITGEKNLPcaNVRQIILWVEDPAKKKKLFEILNDKKLfkPPVLVFVDCKLGADL 459
Cdd:PRK11634 185 LFSATMPEAIRRITRRFMKEPqeVRIQSSVTTRP--DISQSYWTVWGMRKNEALVRFLEAEDF--DAAIIFVRTKNATLE 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  460 LSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRL 539
Cdd:PRK11634 261 VAEALER-NGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRA 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27469538  540 GQNGTAITFINNNSKRLFWDIAKRVKPTgsiLPPQLLNSPYLHDQKRKEQQKDKQTQ 596
Cdd:PRK11634 340 GRAGRALLFVENRERRLLRNIERTMKLT---IPEVELPNAELLGKRRLEKFAAKVQQ 393
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
205-401 6.90e-67

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: 217.74  E-value: 6.90e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRaLFESK-----------TPS 273
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISK-LLEDGppsvgrgrrkaYPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 274 ALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVD 353
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27469538 354 EADTMLKMGFQQQVLDILE--NIP--NDCQTILVSATIPTSIEQLASQLLHN 401
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEhpDMPpkGERQTLMFSATFPREIQRLAADFLKN 211
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
200-548 7.17e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 223.29  E-value: 7.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  200 RPIID--FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR-----ALFESK-- 270
Cdd:PRK04537   4 KPLTDltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRllsrpALADRKpe 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  271 TPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSV-ELCGVKI 349
Cdd:PRK04537  84 DPRALILAPTRELAIQIHKDAVKFGADLG-LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  350 VVVDEADTMLKMGFQQQVLDILENIPNDC--QTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEDP 427
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  428 AKKKKLFEILNDKKLFKppVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGR 507
Cdd:PRK04537 243 EKQTLLLGLLSRSEGAR--TMVFVNTKAFVERVARTLER-HGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 27469538  508 GLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 548
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
222-405 1.36e-63

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: 207.88  E-value: 1.36e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALF---ESKTPSALILTPTRELAIQIERQAKELMSGL 298
Cdd:cd17947   9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYrpkKKAATRVLVLVPTRELAMQCFSVLQQLAQFT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 299 PrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPND 377
Cdd:cd17947  89 D-ITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEILRLCPRT 167
                       170       180
                ....*....|....*....|....*...
gi 27469538 378 CQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17947 168 RQTMLFSATMTDEVKDLAKLSLNKPVRV 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
205-548 6.37e-62

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 212.85  E-value: 6.37e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESK-------TPSALIL 277
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPpkerymgEPRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  278 TPTRELAIQIERQAKELM--SGLPRMKtvlLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:PRK01297 169 APTRELVVQIAKDAAALTkyTGLNVMT---FVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  355 ADTMLKMGFQQQVLDILENIP--NDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEDPAKKKK 432
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKL 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  433 LFEILNDKKLFKppVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLI 512
Cdd:PRK01297 326 LYNLVTQNPWER--VMVFANRKDEVRRIEERLVK-DGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 27469538  513 SVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 548
Cdd:PRK01297 403 GISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
214-408 3.71e-61

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: 201.66  E-value: 3.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR--ALFESKTPSALILTPTRELAIQIERQA 291
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKlgKPRKKKGLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 292 KELMSGLPrMKTVLLVGGL-PLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDI 370
Cdd:cd17957  81 LKLSKGTG-LRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27469538 371 LENIPNDC-QTILVSATIPTSIEQLASQLLHNPVRIITG 408
Cdd:cd17957 160 LAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
205-405 3.87e-59

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: 196.76  E-value: 3.87e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSL-PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS--ALILTPTR 281
Cdd:cd17959   3 FQSMGLsPPLLR-AIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGarALILSPTR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 282 ELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKM 361
Cdd:cd17959  82 ELALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27469538 362 GFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
193-406 5.16e-59

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: 196.83  E-value: 5.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 193 VQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI-----MRALF 267
Cdd:cd17953   2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 268 ESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSS---VEL 344
Cdd:cd17953  82 PGEGPIGLIMAPTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27469538 345 CGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
193-400 3.64e-58

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: 195.96  E-value: 3.64e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 193 VQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAL------ 266
Cdd:cd18052  33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkeglta 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 267 ---FESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVE 343
Cdd:cd18052 113 ssfSEVQEPQALIVAPTRELANQIFLEARKFSYGTC-IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27469538 344 LCGVKIVVVDEADTMLKMGFQQQVLDILE--NIP--NDCQTILVSATIPTSIEQLASQLLH 400
Cdd:cd18052 192 LSKLKYLILDEADRMLDMGFGPEIRKLVSepGMPskEDRQTLMFSATFPEEIQRLAAEFLK 252
PTZ00424 PTZ00424
helicase 45; Provisional
205-562 3.96e-58

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 200.44  E-value: 3.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:PTZ00424 110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLPCANVRQIILWVEdpaKKKKLFEILND--KKL 442
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE---KEEWKFDTLCDlyETL 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  443 FKPPVLVFVDCKLGADLLSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDM 522
Cdd:PTZ00424 266 TITQAIIYCNTRRKVDYLTKKMHE-RDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 27469538  523 PSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAK 562
Cdd:PTZ00424 345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
218-405 5.54e-57

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: 191.38  E-value: 5.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR-----ALFESKT---PSALILTPTRELAIQIER 289
Cdd:cd17945   5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYisrlpPLDEETKddgPYALILAPTRELAQQIEE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 290 QAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLD 369
Cdd:cd17945  85 ETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTK 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27469538 370 ILENIPNDC--------------------QTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17945 164 ILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
205-405 4.50e-55

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: 185.60  E-value: 4.50e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPvIMRALFESKTP-SALILTPTREL 283
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP-ILQALLENPQRfFALVLAPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSS-VELCGVKIVVVDEADTMLKMG 362
Cdd:cd17954  81 AQQISEQFEALGSSIG-LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMD 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 27469538 363 FQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
214-405 1.17e-53

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: 181.84  E-value: 1.17e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIM-----RALFESKTPSALILTPTRELAIQIE 288
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVhimdqRELEKGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 289 RQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVL 368
Cdd:cd17952  81 LEAKKF-GKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27469538 369 DILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
227-394 1.78e-52

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: 177.43  E-value: 1.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   227 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLL 306
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   307 VGGLPLPPQLYRLqQHVKVIIATPGRLLDIIKQsSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSAT 386
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 27469538   387 IPTSIEQL 394
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
218-399 6.62e-52

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: 177.39  E-value: 6.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGL-LGRDILASADTGSGKTAAFLLPVIMRAL-----FESKTPSALILTPTRELAIQIERQA 291
Cdd:cd17964   9 LTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLntkpaGRRSGVSALIISPTRELALQIAAEA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 292 KELMSGLPRMKTVLLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSV--ELCGVKIVVVDEADTMLKMGFQQQVL 368
Cdd:cd17964  89 KKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDMGFRPDLE 168
                       170       180       190
                ....*....|....*....|....*....|....*
gi 27469538 369 DILENIPN----DCQTILVSATIPTSIEQLASQLL 399
Cdd:cd17964 169 QILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
218-405 3.49e-51

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: 175.25  E-value: 3.49e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRA-----LFESKTPSALILTPTRELAIQIERQAK 292
Cdd:cd17966   5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHInaqppLERGDGPIVLVLAPTRELAQQIQQEAN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 293 ELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILE 372
Cdd:cd17966  85 KF-GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVD 163
                       170       180       190
                ....*....|....*....|....*....|...
gi 27469538 373 NIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17966 164 QIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
211-548 2.02e-49

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 177.47  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  211 PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT-------PSALILTPTREL 283
Cdd:PRK04837  17 PQVVE-ALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPedrkvnqPRALIMAPTREL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  284 AIQIERQAKEL--MSGLprmKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKM 361
Cdd:PRK04837  96 AVQIHADAEPLaqATGL---KLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  362 GFQQQVLDILENIPNDCQ--TILVSATIPTSIEQLASQLLHNPVRII------TGEknlpcaNVRQIILWVEDPAKKKKL 433
Cdd:PRK04837 173 GFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEvepeqkTGH------RIKEELFYPSNEEKMRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  434 FEILN----DKklfkppVLVFVDCK---------LGAD-----LLSEAV-QKitglKRISihseksqierknILKGLLEG 494
Cdd:PRK04837 247 QTLIEeewpDR------AIIFANTKhrceeiwghLAADghrvgLLTGDVaQK----KRLR------------ILEEFTRG 304
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 27469538  495 DYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 548
Cdd:PRK04837 305 DLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
168-408 2.17e-49

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: 172.89  E-value: 2.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 168 YKEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASA 247
Cdd:cd18050  27 YVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 248 DTGSGKTAAFLLPVIMRA-----LFESKTPSALILTPTRELAIQIERQAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQH 322
Cdd:cd18050 107 QTGSGKTLAYLLPAIVHInhqpyLERGDGPICLVLAPTRELAQQVQQVADDYGKS-SRLKSTCIYGGAPKGPQIRDLERG 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 323 VKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNP 402
Cdd:cd18050 186 VEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDY 265

                ....*.
gi 27469538 403 VRIITG 408
Cdd:cd18050 266 VQINIG 271
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
205-405 2.95e-49

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: 170.17  E-value: 2.95e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:cd17940  81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27469538 365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
195-401 3.10e-49

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: 171.76  E-value: 3.10e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 195 GQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPvIMRALFES----- 269
Cdd:cd18051  13 GENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLP-ILSQIYEQgpges 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 270 ------------KTPSALILTPTRELAIQIERQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDII 337
Cdd:cd18051  92 lpsesgyygrrkQYPLALVLAPTRELASQIYDEARKF-AYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27469538 338 KQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILE--NIP--NDCQTILVSATIPTSIEQLASQLLHN 401
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPptGERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
218-405 1.36e-48

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: 168.24  E-value: 1.36e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS----ALILTPTRELAIQIERQAKE 293
Cdd:cd17941   5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEVLRK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 294 LMSGlPRMKTVLLVGGLPLPPQLYRLQQhVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDEADTMLKMGFQQQVLDILE 372
Cdd:cd17941  85 VGKY-HSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
                       170       180       190
                ....*....|....*....|....*....|...
gi 27469538 373 NIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17941 163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
218-405 1.71e-48

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: 168.29  E-value: 1.71e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT--------PSALILTPTRELAIQ--- 286
Cdd:cd17951   5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpfikgegPYGLIVCPSRELARQthe 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 287 -IERQAKELM-SGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:cd17951  85 vIEYYCKALQeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFE 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27469538 365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17951 165 EDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEXDc smart00487
DEAD-like helicases superfamily;
218-413 1.80e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 168.05  E-value: 1.80e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538    218 LKKSGYEVPTPIQMQMIPVGLLG-RDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAIQIERQAKELMS 296
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538    297 GLPRmKTVLLVGGLPLPPQLYRLQQHV-KVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIP 375
Cdd:smart00487  80 SLGL-KVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 27469538    376 NDCQTILVSATIPTSIEQLASQLLHNPVRIITGEKNLP 413
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLE 196
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
181-408 3.81e-48

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: 168.26  E-value: 3.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 181 QIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLP 260
Cdd:cd18049   2 EVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 261 VIMRA-----LFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLD 335
Cdd:cd18049  82 AIVHInhqpfLERGDGPICLVLAPTRELAQQVQQVAAEYGRAC-RLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27469538 336 IIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIITG 408
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
205-403 3.73e-47

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: 164.70  E-value: 3.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAlfeSKTPS---ALILTPTR 281
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---SEDPYgifALVLTPTR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 282 ELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCG---VKIVVVDEADTM 358
Cdd:cd17955  78 ELAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDEADRL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27469538 359 LKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPV 403
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
218-403 4.24e-47

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 164.29  E-value: 4.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT------PSALILTPTRELAIQIERQA 291
Cdd:cd17961   9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqgTRALILVPTRELAQQVSKVL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 292 KELMSGL-PRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELC-GVKIVVVDEADTMLKMGFQQQVLD 369
Cdd:cd17961  89 EQLTAYCrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSYGYEEDLKS 168
                       170       180       190
                ....*....|....*....|....*....|....
gi 27469538 370 ILENIPNDCQTILVSATIPTSIEQLASQLLHNPV 403
Cdd:cd17961 169 LLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
217-405 9.90e-46

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: 160.32  E-value: 9.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 217 NLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT------PSALILTPTRELAIQIERQ 290
Cdd:cd17958   4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPreqrngPGVLVLTPTRELALQIEAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 291 -AKELMSGlprMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLD 369
Cdd:cd17958  84 cSKYSYKG---LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27469538 370 ILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
222-406 1.10e-45

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: 160.57  E-value: 1.10e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRM 301
Cdd:cd17939  16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYM-GV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTI 381
Cdd:cd17939  95 KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
                       170       180
                ....*....|....*....|....*
gi 27469538 382 LVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd17939 175 LFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
218-405 2.88e-44

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: 156.27  E-value: 2.88e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSG 297
Cdd:cd17943   5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 298 LPRMKTVLLVGGLPLPPQLYRLQQhVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPND 377
Cdd:cd17943  85 LEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKN 163
                       170       180
                ....*....|....*....|....*...
gi 27469538 378 CQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17943 164 KQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
222-403 6.56e-43

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: 152.86  E-value: 6.56e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVImralfesKTPSALILTPTRELAIQ----IERQAKELMSg 297
Cdd:cd17938  18 DWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELAEQtyncIENFKKYLDN- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 298 lPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIP-- 375
Cdd:cd17938  90 -PKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPki 168
                       170       180       190
                ....*....|....*....|....*....|...
gi 27469538 376 ----NDCQTILVSATI-PTSIEQLASQLLHNPV 403
Cdd:cd17938 169 tsdgKRLQVIVCSATLhSFEVKKLADKIMHFPT 201
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
218-405 3.88e-42

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: 150.80  E-value: 3.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI-----MRALFESKTPSALILTPTRELAIQIERQAK 292
Cdd:cd17960   5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeillkRKANLKKGQVGALIISPTRELATQIYEVLQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 293 ELMS-GLPRMKTVLLVGGLPLPPQLYRLQQH-VKVIIATPGRLLDIIKQSSVELCG--VKIVVVDEADTMLKMGFQQQVL 368
Cdd:cd17960  85 SFLEhHLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLDLGFEADLN 164
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27469538 369 DILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17960 165 RILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
417-549 6.88e-41

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: 144.96  E-value: 6.88e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 417 VRQIILWVEDPAKKKKLFEILnDKKLFKPPVLVFVDCKLGADLLSEAVQKItGLKRISIHSEKSQIERKNILKGLLEGDY 496
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEEL-GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 27469538 497 EVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFI 549
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
219-405 7.22e-41

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: 147.73  E-value: 7.22e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 219 KKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALfeSKTPS--------ALILTPTRELAIQIERQ 290
Cdd:cd17949   7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRvdrsdgtlALVLVPTRELALQIYEV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQ-SSVELCGVKIVVVDEADTMLKMGFQQQVLD 369
Cdd:cd17949  85 LEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27469538 370 ILE-------------NIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17949 165 ILEllddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
218-395 6.60e-40

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: 144.43  E-value: 6.60e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLP---VIMRALFESKTPSA-LILTPTRELAIQIERQAKE 293
Cdd:cd17942   5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNGTGvIIISPTRELALQIYGVAKE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 294 LMSGlpRMKTVLLV-GGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELC-GVKIVVVDEADTMLKMGFQQQVLDIL 371
Cdd:cd17942  85 LLKY--HSQTFGIViGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYkNLQCLIIDEADRILEIGFEEEMRQII 162
                       170       180
                ....*....|....*....|....
gi 27469538 372 ENIPNDCQTILVSATIPTSIEQLA 395
Cdd:cd17942 163 KLLPKRRQTMLFSATQTRKVEDLA 186
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
218-387 2.63e-39

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: 144.30  E-value: 2.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 218 LKKSGYEVPTPIQMQMIPVGLL-GRDILASADTGSGKTAAFLLPVIMRAL---------FESKTPSALILTPTRELAIQI 287
Cdd:cd17946   5 LADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLsqkssngvgGKQKPLRALILTPTRELAVQV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 288 ERQAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIV---VVDEADTMLKMGFQ 364
Cdd:cd17946  85 KDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEKGHF 163
                       170       180       190
                ....*....|....*....|....*....|
gi 27469538 365 QQVLDILENIPNDC-------QTILVSATI 387
Cdd:cd17946 164 AELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
205-406 9.34e-39

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: 141.45  E-value: 9.34e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:cd18045  81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27469538 365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
205-406 2.23e-38

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: 140.66  E-value: 2.23e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQ 364
Cdd:cd18046  81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27469538 365 QQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRII 406
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
214-397 1.59e-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: 1.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFES-------KTPSALILTPTRELAIQ 286
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpfNAPRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 287 IERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQ 366
Cdd:cd17948  81 IGSVAQSLTEGLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27469538 367 VLDILENIP-------------NDCQTILVSATIPTSIEQLASQ 397
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
211-405 2.06e-32

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: 123.99  E-value: 2.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 211 PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQ 290
Cdd:cd17950  11 PELLR-AIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLK-MGFQQQVL 368
Cdd:cd17950  90 YERFSKYMPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEqLDMRRDVQ 169
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27469538 369 DILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17950 170 EIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
211-405 5.05e-32

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: 122.68  E-value: 5.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 211 PEVLNHnLKKSGYEVPTPIQMQMIPVgLLG---RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQI 287
Cdd:cd17963   3 PELLKG-LYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 288 ERQAKELMSgLPRMKTVLLVGGLPLPPQlYRLQQHvkVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKM-GFQQQ 366
Cdd:cd17963  81 GEVVEKMGK-FTGVKVALAVPGNDVPRG-KKITAQ--IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQ 156
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27469538 367 VLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRI 405
Cdd:cd17963 157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
217-402 1.80e-30

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: 119.27  E-value: 1.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 217 NLKKSGYEVPTPIQMQMIP---------VGLLGRDILASADTGSGKTAAFLLPVImRALFESKTPS--ALILTPTRELAI 285
Cdd:cd17956   4 NLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRlrALIVVPTKELVQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 286 QIERQAKELMSGLPrMKTVLLVGG------LPLPPQLYRLQQHVKV--IIATPGRLLDIIKQ-SSVELCGVKIVVVDEAD 356
Cdd:cd17956  83 QVYKVFESLCKGTG-LKVVSLSGQksfkkeQKLLLVDTSGRYLSRVdiLVATPGRLVDHLNStPGFTLKHLRFLVIDEAD 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27469538 357 TMLKMGFQQ---QVLDILENIPND-----------------CQTILVSATIPTSIEQLASQLLHNP 402
Cdd:cd17956 162 RLLNQSFQDwleTVMKALGRPTAPdlgsfgdanllersvrpLQKLLFSATLTRDPEKLSSLKLHRP 227
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
217-399 9.09e-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: 116.49  E-value: 9.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 217 NLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR------ALFESKTPSALILTPTRELAIQIerq 290
Cdd:cd17944   4 LLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKlqedqqPRKRGRAPKVLVLAPTRELANQV--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDI 370
Cdd:cd17944  81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 27469538 371 L-----ENIPNDCQTILVSATIPTSIEQLASQLL 399
Cdd:cd17944 161 LsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
205-402 6.76e-23

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: 97.78  E-value: 6.76e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRE 282
Cdd:cd18048  20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 283 LAIQIERQAKELMSGLPRMKTVLLVGGlPLPPQLYRLQQhvKVIIATPGRLLD-IIKQSSVELCGVKIVVVDEADTMLKM 361
Cdd:cd18048 100 LALQTGKVVEEMGKFCVGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMINV 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27469538 362 -GFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNP 402
Cdd:cd18048 177 qGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
428-540 3.87e-22

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: 91.50  E-value: 3.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   428 AKKKKLFEILNDKKlfKPPVLVFvdCKLGADLLSEAVQKITGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGR 507
Cdd:pfam00271   1 EKLEALLELLKKER--GGKVLIF--SQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 27469538   508 GLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLG 540
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
458-540 1.60e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.11  E-value: 1.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538    458 DLLSEAVQKItGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVG 537
Cdd:smart00490   1 EELAELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 27469538    538 RLG 540
Cdd:smart00490  80 RAG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
212-407 3.37e-20

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: 90.51  E-value: 3.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 212 EVLNHNLKKSGYEVPTPIQMQMIPVgLLGRDI-----------------LASADTGSGKTAAFLLPvIMRALFE------ 268
Cdd:cd17965  17 EILKGSNKTDEEIKPSPIQTLAIKK-LLKTLMrkvtkqtsneepklevfLLAAETGSGKTLAYLAP-LLDYLKRqeqepf 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 269 ------------SKTPSALILTPTRELAIQIERQAKELMSGLP-RMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLD 335
Cdd:cd17965  95 eeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLAS 174
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27469538 336 IIKQSSVELCGVKIVVVDEADTMLKMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNPVRIIT 407
Cdd:cd17965 175 LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIAT 246
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
205-402 1.74e-19

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: 87.08  E-value: 1.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRE 282
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 283 LAIQIERQAKELMSGLPRMKTVLLVGGlplppqlYRLQQHVK----VIIATPGRLLD-IIKQSSVELCGVKIVVVDEADT 357
Cdd:cd18047  83 LALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQKiseqIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADV 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27469538 358 ML-KMGFQQQVLDILENIPNDCQTILVSATIPTSIEQLASQLLHNP 402
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
240-566 8.23e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 87.00  E-value: 8.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLpvIMRALFESKTpsALILTPTRELAIQIerqAKELMSGLPRmktVLLVGGlplppqlyRL 319
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALA--LAAELLRGKR--VLVLVPRRELLEQW---AEELRRFLGD---PLAGGG--------KK 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 320 QQHVKVIIATPGRLldiIKQSSVELCG--VKIVVVDE-----ADTmlkmgFQQqvldILENIPNDCqTILVSAT------ 386
Cdd:COG1061 162 DSDAPITVATYQSL---ARRAHLDELGdrFGLVIIDEahhagAPS-----YRR----ILEAFPAAY-RLGLTATpfrsdg 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 387 --IPTSI-----------EQLASQLLHNPVRII--------TGEKNLPCANVRQIILwVEDPAKKKKLFEILnDKKLFKP 445
Cdd:COG1061 229 reILLFLfdgivyeyslkEAIEDGYLAPPEYYGirvdltdeRAEYDALSERLREALA-ADAERKDKILRELL-REHPDDR 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 446 PVLVFVDCKLGADLLSEAVQKItGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSS 525
Cdd:COG1061 307 KTLVFCSSVDHAEALAELLNEA-GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGS 385
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 27469538 526 MDEYVHQIGRVGRLGQNGTAITFIN--NNSKRLFWDIAKRVKP 566
Cdd:COG1061 386 PREFIQRLGRGLRPAPGKEDALVYDfvGNDVPVLEELAKDLRD 428
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
240-386 1.31e-17

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: 79.75  E-value: 1.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLpvIMRALFESKTPSALILTPTRELAIQierQAKELMSGLPRMKTV-LLVGGLPLPPQLYR 318
Cdd:cd00046   1 GENVLITAPTGSGKTLAALL--AALLLLLKKGKKVLVLVPTKALALQ---TAERLRELFGPGIRVaVLVGGSSAEEREKN 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27469538 319 LQQHVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDEADTMLKMGFQ--QQVLDILENIPNDCQTILVSAT 386
Cdd:cd00046  76 KLGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGalILDLAVRKAGLKNAQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
240-557 2.43e-17

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: 86.04  E-value: 2.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLPVImRALFESKTPSALILTPTRELAI-QIERQAKELMSGLPRMKTVLLVGGLPlPPQLYR 318
Cdd:COG1205  71 GKNVVIATPTASGKSLAYLLPVL-EALLEDPGATALYLYPTKALARdQLRRLRELAEALGLGVRVATYDGDTP-PEERRW 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 319 LQQHVKVIIATPgrllDIIKQSSVE--------LCGVKIVVVDEADT-----------MLKmgfqqQVLDILENIPNDCQ 379
Cdd:COG1205 149 IREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAHTyrgvfgshvanVLR-----RLRRICRHYGSDPQ 219
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 380 TILVSATI--PtsiEQLASQLLHNPVRIIT------GEknlpcanvRQIILW----VEDPAKK------KKLFEILNDKK 441
Cdd:COG1205 220 FILASATIgnP---AEHAERLTGRPVTVVDedgsprGE--------RTFVLWnpplVDDGIRRsalaeaARLLADLVREG 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 442 LfkpPVLVFVDCKLGADLLSEAVQkitglKRISIHSEKSQI----------ERKNILKGLLEGDYEVVVSTGVLGRGLDL 511
Cdd:COG1205 289 L---RTLVFTRSRRGAELLARYAR-----RALREPDLADRVaayragylpeERREIERGLRSGELLGVVSTNALELGIDI 360
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27469538 512 ISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAI---------TFINNNSKRLF 557
Cdd:COG1205 361 GGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVlvagddpldQYYVRHPEELF 415
zf-HIT_DDX59 cd23022
zinc finger HIT (zf-HIT) found in DEAD box protein 59 (DDX59) and similar proteins; DDX59, ...
103-136 6.40e-17

zinc finger HIT (zf-HIT) found in DEAD box protein 59 (DDX59) and similar proteins; DDX59, also called zinc finger HIT domain-containing protein 5 (ZNHIT5), is a probable ATP-dependent RNA helicase (EC 3.6.4.13) that plays a role in nervous system development and function. It has an important role in lung cancer development through promoting DNA replication. Mutations in DDX59 implicate RNA helicase in the pathogenesis of oral-facial-digital syndrome (OFDS). DDX59 contains a zf-HIT domain which is characterized by a fold in "treble-clef" through interleaved CCCC and CCHC zinc finger motifs that both bind a zinc ion.


Pssm-ID: 467794  Cd Length: 35  Bit Score: 74.20  E-value: 6.40e-17
                        10        20        30
                ....*....|....*....|....*....|....
gi 27469538 103 PGEPICVVCGRYGEYICDKTDEDVCSLECKAKHL 136
Cdd:cd23022   1 GKEGWCVVCGRYANYYCDDTDDPVCSLECKRKHL 34
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
209-546 1.07e-13

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 73.78  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 209 SLPEVLNHnLKKSGYEVPTPIQMQMIPVGLL-GRDILASADTGSGKTA-AFLLpvIMRALFESKTpsALILTPTRELAIQ 286
Cdd:COG1204   7 PLEKVIEF-LKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTLiAELA--ILKALLNGGK--ALYIVPLRALASE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 287 IERQAKELMSGLPrMKTVLLVGGLPLPPqlYRLQQHvKVIIATPGRLLDIIKQSSVELCGVKIVVVDEAdtmlkmgfqQQ 366
Cdd:COG1204  82 KYREFKRDFEELG-IKVGVSTGDYDSDD--EWLGRY-DILVATPEKLDSLLRNGPSWLRDVDLVVVDEA---------HL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 367 VLD-----ILENI-------PNDCQTILVSATIPtSIEQLAsQLLHN--------PVRIITGeknlpcANVRQIILWVED 426
Cdd:COG1204 149 IDDesrgpTLEVLlarlrrlNPEAQIVALSATIG-NAEEIA-EWLDAelvksdwrPVPLNEG------VLYDGVLRFDDG 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 427 PAK-KKKLFEILNDKKLFKPPVLVFV----DCKLGADLLSEAVQKITG-------------LKRISIHSEKSQIERKNIL 488
Cdd:COG1204 221 SRRsKDPTLALALDLLEEGGQVLVFVssrrDAESLAKKLADELKRRLTpeereeleelaeeLLEVSEETHTNEKLADCLE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 489 KG--------------LLE-----GDYEVVVSTGVLGRGLDLISVRLVV-----NFDMP-SSMDeyVHQ-IGRVGRLGQN 542
Cdd:COG1204 301 KGvafhhaglpselrrLVEdafreGLIKVLVATPTLAAGVNLPARRVIIrdtkrGGMVPiPVLE--FKQmAGRAGRPGYD 378

                ....*.
gi 27469538 543 --GTAI 546
Cdd:COG1204 379 pyGEAI 384
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
227-388 5.03e-11

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: 61.89  E-value: 5.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 227 TPIQMQMIPVGLL-GRDILASADTGSGKTAAFLLpVIMRALFESKtPSALILTPTRELAIQIERQAKELMSglPRMKTVL 305
Cdd:cd17921   3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAEL-AILRALATSG-GKAVYIAPTRALVNQKEADLRERFG--PLGKNVG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 306 LVGGLP--LPPQLYRLQqhvkVIIATPGRLLDIIKQSSVELCG-VKIVVVDEADtMLKMGFQ----QQVLDILENIPNDC 378
Cdd:cd17921  79 LLTGDPsvNKLLLAEAD----ILVATPEKLDLLLRNGGERLIQdVRLVVVDEAH-LIGDGERgvvlELLLSRLLRINKNA 153
                       170
                ....*....|
gi 27469538 379 QTILVSATIP 388
Cdd:cd17921 154 RFVGLSATLP 163
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
240-398 3.21e-10

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 59.52  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAI-QIERQAKELMSGLPRMKTVLLVGGLPLPPQLYR 318
Cdd:cd17923  15 GRSVVVTTGTASGKSLCYQLP-ILEALLRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGDTPREERRAI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 319 LQQHVKVIIATPGRL-LDIIKQSSVE---LCGVKIVVVDEADTmLKMGFQQQV-------LDILENIPNDCQTILVSATI 387
Cdd:cd17923  94 IRNPPRILLTNPDMLhYALLPHHDRWarfLRNLRYVVLDEAHT-YRGVFGSHValllrrlRRLCRRYGADPQFILTSATI 172
                       170
                ....*....|.
gi 27469538 388 pTSIEQLASQL 398
Cdd:cd17923 173 -GNPAEHARTL 182
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
496-549 5.76e-10

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: 55.79  E-value: 5.76e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27469538 496 YEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQ-NGTAITFI 549
Cdd:cd18785  23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILFV 77
zf-HIT cd23020
zinc finger HIT (zf-HIT) domain; The zinc finger HIT (zf-HIT) is a novel zinc-binding domain ...
107-136 1.33e-09

zinc finger HIT (zf-HIT) domain; The zinc finger HIT (zf-HIT) is a novel zinc-binding domain with about 50 amino acids. It is characterized by a fold in "treble-clef" through interleaved CCCC and CCHC zinc finger motifs that both bind a zinc ion. zf-HIT domain may function as a protein-protein interaction domain. It is mainly found in nuclear proteins involved in gene regulation and chromatin remodeling. The zf-HIT family includes six proteins containing zf-HIT domain present in human and three in yeast proteome, all belonging to multimodular RNA/protein complexes.


Pssm-ID: 467792  Cd Length: 31  Bit Score: 53.66  E-value: 1.33e-09
                        10        20        30
                ....*....|....*....|....*....|.
gi 27469538 107 ICVVCGRY-GEYICDKTDEDVCSLECKAKHL 136
Cdd:cd23020   1 TCGICGGYpGKYKCPRCGVPYCSLECYRKHL 31
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
240-387 1.79e-08

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 54.13  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLPVIMRALFESKTPSALI-LTPTRELAIQIERqakelmsglpRMKTVLLVGGLPLP----- 313
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLyISPLKALINDQER----------RLEEPLDEIDLEIPvavrh 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 314 ---PQLYRLQQHVK---VIIATPGRL--LDIIKQSSVELCGVKIVVVDEADTML--KMGFQ-QQVLDILENIP-NDCQTI 381
Cdd:cd17922  71 gdtSQSEKAKQLKNppgILITTPESLelLLVNKKLRELFAGLRYVVVDEIHALLgsKRGVQlELLLERLRKLTgRPLRRI 150

                ....*.
gi 27469538 382 LVSATI 387
Cdd:cd17922 151 GLSATL 156
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
483-548 4.48e-08

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 52.21  E-value: 4.48e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27469538 483 ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 548
Cdd:cd18794  68 DRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
483-548 5.56e-08

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 55.53  E-value: 5.56e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27469538 483 ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 548
Cdd:COG0514 268 EREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
223-408 1.28e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.72  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 223 YEVPTPIQMQMIPVGLLGRDILASADTGSGKT-AAFlLPVIMRaLFESKTPSAL-----IL--TPTRELAIQIERQAKEL 294
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDE-LARRPRPGELpdglrVLyiSPLKALANDIERNLRAP 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 295 MSGLprmktvLLVGGLPLP-----------PQLYRLQQ-----HvkVIIATP-----------GRLLdiikqssveLCGV 347
Cdd:COG1201 100 LEEI------GEAAGLPLPeirvgvrtgdtPASERQRQrrrppH--ILITTPeslallltspdAREL---------LRGV 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27469538 348 KIVVVDE----ADTmlKMGFQQQV-LDILENI-PNDCQTILVSATI-PtsIEQLASQLLHN----PVRIITG 408
Cdd:COG1201 163 RTVIVDEihalAGS--KRGVHLALsLERLRALaPRPLQRIGLSATVgP--LEEVARFLVGYedprPVTIVDA 230
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
241-399 4.96e-07

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.11  E-value: 4.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 241 RDILASADTGSGKTAAFLLPVIMRAlfeSKTPSALILTPTRELAIQIERQAKELmsgLPRMKTVLLVGGlplppQLYRLQ 320
Cdd:cd17918  37 MDRLLSGDVGSGKTLVALGAALLAY---KNGKQVAILVPTEILAHQHYEEARKF---LPFINVELVTGG-----TKAQIL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 321 QHVKVIIATPGRLldiikQSSVELCGVKIVVVDEADtmlKMGFQQQvlDILENIPNdCQTILVSAT-IPTSIEQLASQLL 399
Cdd:cd17918 106 SGISLLVGTHALL-----HLDVKFKNLDLVIVDEQH---RFGVAQR--EALYNLGA-THFLEATATpIPRTLALALSGLL 174
zf-HIT pfam04438
HIT zinc finger; This presumed zinc finger contains up to 6 cysteine residues that could ...
105-132 1.05e-06

HIT zinc finger; This presumed zinc finger contains up to 6 cysteine residues that could coordinate zinc. The domain is named after the HIT protein. This domain is also found in the Thyroid receptor interacting protein 3 (TRIP-3) that specifically interact with the ligand binding domain of the thyroid receptor.


Pssm-ID: 461310  Cd Length: 30  Bit Score: 45.32  E-value: 1.05e-06
                          10        20
                  ....*....|....*....|....*...
gi 27469538   105 EPICVVCGRYGEYICDKTDEDVCSLECK 132
Cdd:pfam04438   2 RKLCSVCGNPSKYRCPRCGVRYCSLECY 29
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
477-541 3.61e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 50.11  E-value: 3.61e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27469538 477 SEKSQIErknILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-MPSSMdEYVHQIGRVGRLGQ 541
Cdd:COG1111 396 TQKEQIE---ILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGRKRE 457
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
447-546 4.48e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 47.24  E-value: 4.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 447 VLVFVDCKLGADLLSEAVQKItGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD----- 521
Cdd:cd18790  30 VLVTTLTKRMAEDLTEYLQEL-GVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkeg 108
                        90       100
                ....*....|....*....|....*
gi 27469538 522 MPSSMDEYVHQIGRVGRlGQNGTAI 546
Cdd:cd18790 109 FLRSETSLIQTIGRAAR-NVNGKVI 132
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
378-554 9.80e-06

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 48.83  E-value: 9.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   378 CQTILVSATiPTSIE-QLASQLLHNPVRIiTGEKNlPCANVRQIILWVEDpakkkkLFEILNDKKLFKPPVLVFVDCKLG 456
Cdd:TIGR00631 384 NQVVYVSAT-PGPYElEQSGNVVEQIIRP-TGLLD-PEIEVRPTDGQVDD------LLSEIRQRVARNERVLVTTLTKKM 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538   457 A----DLLSEAvqkitGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-----MPSSMD 527
Cdd:TIGR00631 455 AedltDYLKEL-----GIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSER 529
                         170       180
                  ....*....|....*....|....*..
gi 27469538   528 EYVHQIGRVGRlGQNGTAITFINNNSK 554
Cdd:TIGR00631 530 SLIQTIGRAAR-NVNGKVIMYADKITD 555
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
428-541 2.78e-05

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: 44.00  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 428 AKKKKLFEILndKKLFKPP--VLVFVDCKLGADLLSEAVQKItGLKRISIHSEKSQIERKNILKGLLEGDYEVV--VSTG 503
Cdd:cd18793  11 GKLEALLELL--EELREPGekVLIFSQFTDTLDILEEALRER-GIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflLSTK 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27469538 504 VLGRGLDLISVRLVVNFDMP--SSMDEyvhQ-IGRVGRLGQ 541
Cdd:cd18793  88 AGGVGLNLTAANRVILYDPWwnPAVEE---QaIDRAHRIGQ 125
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
460-548 3.77e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 46.63  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  460 LSEAVQKiTGLKRISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRL 539
Cdd:PRK11057 252 TAARLQS-RGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330

                 ....*....
gi 27469538  540 GQNGTAITF 548
Cdd:PRK11057 331 GLPAEAMLF 339
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
422-543 1.53e-04

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 42.24  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 422 LWVEDPAKKKKLFEIL-----NDKklfkppVLVFVDCKlgadllsEAVQKI-TGLKRISIHSEKSQIERKNILKGLLEGD 495
Cdd:cd18789  28 LAAMNPNKLRALEELLkrheqGDK------IIVFTDNV-------EALYRYaKRLLKPFITGETPQSEREEILQNFREGE 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27469538 496 YEVVVSTGVLGRGLDL--ISVRLVVNFdMPSSMDEYVHQIGRVGRLGQNG 543
Cdd:cd18789  95 YNTLVVSKVGDEGIDLpeANVAIQISG-HGGSRRQEAQRLGRILRPKKGG 143
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
480-538 1.54e-04

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: 42.34  E-value: 1.54e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27469538 480 SQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGR 538
Cdd:cd18801  75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
PRK13767 PRK13767
ATP-dependent helicase; Provisional
220-541 1.61e-04

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 44.88  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  220 KSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKT-AAFLlpVIMRALFE-------SKTPSALILTPTRELAIQIERQA 291
Cdd:PRK13767  27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL--AIIDELFRlgregelEDKVYCLYVSPLRALNNDIHRNL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  292 KELMSGLprmKTVLLVGGLPLPP----------QLYRLQQHVK----VIIATPgRLLDIIKQS---SVELCGVKIVVVDE 354
Cdd:PRK13767 105 EEPLTEI---REIAKERGEELPEirvairtgdtSSYEKQKMLKkpphILITTP-ESLAILLNSpkfREKLRTVKWVIVDE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  355 ----ADTmlKMGFQQQV-LDILENI-PNDCQTILVSATI-PtsIEQLASQLLHN-------PVRIITgeknlpcAN-VRQ 419
Cdd:PRK13767 181 ihslAEN--KRGVHLSLsLERLEELaGGEFVRIGLSATIeP--LEEVAKFLVGYeddgeprDCEIVD-------ARfVKP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  420 IILWVEDPAK----------KKKLFEILndKKLFKP--PVLVFVDCKLGADLLSEAVQKITGlKRISI------HSEKSQ 481
Cdd:PRK13767 250 FDIKVISPVDdlihtpaeeiSEALYETL--HELIKEhrTTLIFTNTRSGAERVLYNLRKRFP-EEYDEdnigahHSSLSR 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27469538  482 IERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVG-RLGQ 541
Cdd:PRK13767 327 EVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGhRLGE 387
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
429-535 1.68e-04

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: 42.19  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 429 KKKKLFEILNDKKLFKPPV--LVFVD----CKLGADLLSEAVQKITGLK-------------RISIHSEKSQIErknILK 489
Cdd:cd18802   8 KLQKLIEILREYFPKTPDFrgIIFVErratAVVLSRLLKEHPSTLAFIRcgfligrgnssqrKRSLMTQRKQKE---TLD 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 27469538 490 GLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGR 535
Cdd:cd18802  85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
398-546 1.86e-04

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: 41.86  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 398 LLHNPVRIITGEKNLpcanvrqiilwVEDPAKKKKLFEILNDKKLfkpPVLVFVDCKLGADLLSEAVQ-----KITGLKR 472
Cdd:cd18797   3 VLWNPPLLDRKDGER-----------GSARREAARLFADLVRAGV---KTIVFCRSRKLAELLLRYLKarlveEGPLASK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 473 ISIH------SEKSQIERKnilkgLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAI 546
Cdd:cd18797  69 VASYragylaEDRREIEAE-----LFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
240-394 2.29e-04

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 42.66  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 240 GRDILASADTGSGKTAAFLLPVImrALFESKTPSALILT-PTRELAIQIERQAKELMSGLPRMKTVLLV----------- 307
Cdd:cd17930   1 PGLVILEAPTGSGKTEAALLWAL--KLAARGGKRRIIYAlPTRATINQMYERIREILGRLDDEDKVLLLhskaalelles 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 308 ----GGLPLPPQLYRLQQ----HVKVIIATPGRLLD-IIKQSSVE-----LCGvKIVVVDEA----DTMLKMgFQQQVLD 369
Cdd:cd17930  79 deepDDDPVEAVDWALLLkrswLAPIVVTTIDQLLEsLLKYKHFErrlhgLAN-SVVVLDEVqaydPEYMAL-LLKALLE 156
                       170       180
                ....*....|....*....|....*
gi 27469538 370 ILENIpnDCQTILVSATIPTSIEQL 394
Cdd:cd17930 157 LLGEL--GGPVVLMTATLPALLRDE 179
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
249-355 3.81e-04

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 41.92  E-value: 3.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 249 TGSGKTaaFLLPVIMRALFESkTPSALI--LTPTRELAIQiERQAKELMSGLPRMKTVLLVGGLPlPPQLYRLQQHVKVI 326
Cdd:cd18033  25 TGLGKT--FIAAVVMLNYYRW-FPKGKIvfMAPTKPLVSQ-QIEACYKITGIPSSQTAELTGSVP-PTKRAELWASKRVF 99
                        90       100
                ....*....|....*....|....*....
gi 27469538 327 IATPGRLLDIIKQSSVELCGVKIVVVDEA 355
Cdd:cd18033 100 FLTPQTLENDLKEGDCDPKSIVCLVIDEA 128
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
241-355 4.56e-04

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: 41.87  E-value: 4.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 241 RDILASADTGSGKT-AAFLLPVIMRALFESKTPS---ALILTPTRELAIQierQAKELmsglpRMKTVLLVG------GL 310
Cdd:cd18034  17 RNTIVVLPTGSGKTlIAVMLIKEMGELNRKEKNPkkrAVFLVPTVPLVAQ---QAEAI-----RSHTDLKVGeysgemGV 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 27469538 311 PLPPQLYRLQ--QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEA 355
Cdd:cd18034  89 DKWTKERWKEelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
222-408 4.59e-04

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: 41.75  E-value: 4.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPvimrALFESKTpsALILTPTreLAIQierqaKELMSGLPRM 301
Cdd:cd17920   9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP----ALLLDGV--TLVVSPL--ISLM-----QDQVDRLQQL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 302 --KTVLLVGGLPLPPQLYRLQQH----VKVIIATPGRL-----LDIIkQSSVELCGVKIVVVDEADT-----------ML 359
Cdd:cd17920  76 giRAAALNSTLSPEEKREVLLRIkngqYKLLYVTPERLlspdfLELL-QRLPERKRLALIVVDEAHCvsqwghdfrpdYL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 27469538 360 KMGfqqQVLDILENIPndcqTILVSAT-IPTSIEQLASQL-LHNPVRIITG 408
Cdd:cd17920 155 RLG---RLRRALPGVP----ILALTATaTPEVREDILKRLgLRNPVIFRAS 198
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
229-355 4.75e-04

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 41.35  E-value: 4.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 229 IQMQMIPVGLLGRDILASADTGSGKTAAFLLpvIMRALFESKTPSALILTPTRELAIQIERQAKELMSglPRMKTVLLVG 308
Cdd:cd18035   5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAIL--VAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLN--IPDKITSLTG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 27469538 309 GLPlPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEA 355
Cdd:cd18035  81 EVK-PEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
228-408 9.53e-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: 40.70  E-value: 9.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 228 PIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVImraLFESKTPS-ALILTPTRELaiqIERQakelMSGLPR-MKTVL 305
Cdd:cd18018  15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL---LLRRRGPGlTLVVSPLIAL---MKDQ----VDALPRaIKAAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 306 LVGGLPLPPQLYRLQQ----HVKVIIATPGRLLD-----IIKQSSvelcGVKIVVVDEADTMLKMGFQ-----QQVLDIL 371
Cdd:cd18018  85 LNSSLTREERRRILEKlragEVKILYVSPERLVNesfreLLRQTP----PISLLVVDEAHCISEWSHNfrpdyLRLCRVL 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27469538 372 ENIPNDCQTILVSATIPTS-IEQLASQLLHNPVRIITG 408
Cdd:cd18018 161 RELLGAPPVLALTATATKRvVEDIASHLGIPESGVVRG 198
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
103-135 9.70e-04

HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.


Pssm-ID: 467791  Cd Length: 43  Bit Score: 37.21  E-value: 9.70e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 27469538 103 PGEPICVVCGRYGEYICDKTDEDVCSLECKAKH 135
Cdd:cd21437   5 PPRKFCSVCGYWGKYTCVRCGARYCSLKCLETH 37
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
219-399 1.24e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 40.39  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 219 KKSGYEvPTPIQMQMIPVGLLGRDILASADTGSGKTAaFLLpvIMRALFESKTPSALILTPTRELAIQIERQAKElMSGL 298
Cdd:cd17924  12 KKTGFP-PWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGL--ATSLYLASKGKRSYLIFPTKSLVKQAYERLSK-YAEK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 299 PRMKTVLLV--GGLPLPPQ---LYRLQQ-HVKVIIATPGRL---LDIIKQSSVELcgvkiVVVDEADTMLKMGfqqQVLD 369
Cdd:cd17924  87 AGVEVKILVyhSRLKKKEKeelLEKIEKgDFDILVTTNQFLsknFDLLSNKKFDF-----VFVDDVDAVLKSS---KNID 158
                       170       180       190
                ....*....|....*....|....*....|.
gi 27469538 370 ILENIPNDCQTILVSATI-PTSIEQLASQLL 399
Cdd:cd17924 159 RLLKLLGFGQLVVSSATGrPRGIRPLLFREL 189
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
240-308 1.54e-03

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.54e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27469538 240 GRDILASADTGSGKTAAFLLPVIMRALFESKTpsALILTPTRELAIQI-ERQAKELMSGLPR-MKTVLLVG 308
Cdd:COG1199  33 GRHLLIEAGTGTGKTLAYLVPALLAARETGKK--VVISTATKALQEQLvEKDLPLLRKALGLpLRVALLKG 101
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
226-355 4.03e-03

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 38.95  E-value: 4.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 226 PTPIQMQMIPVGLLGRDILASADTGSGKTaaFLLPVIMRALFESKTPS----ALILTPTRELAIQIERQAKELMsGLPRM 301
Cdd:cd17927   3 PRNYQLELAQPALKGKNTIICLPTGSGKT--FVAVLICEHHLKKFPAGrkgkVVFLANKVPLVEQQKEVFRKHF-ERPGY 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27469538 302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQ-SSVELCGVKIVVVDEA 355
Cdd:cd17927  80 KVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDEC 134
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
405-549 4.48e-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: 38.30  E-value: 4.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 405 IITGEKNLPCANVRQIILWVEDPAKKKKLFEILNDKklfkpPVLVFVDCKLGADLLSeavQKITGlkrISI-HSEKSQIE 483
Cdd:cd18795   9 VLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGK-----PVLVFCSSRKECEKTA---KDLAG---IAFhHAGLTRED 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27469538 484 RKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVN----FDmPSSMDEY----VHQ-IGRVGRLGQN--GTAITFI 549
Cdd:cd18795  78 RELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYD-GKGYRELspleYLQmIGRAGRPGFDtrGEAIIMT 153
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
422-539 5.32e-03

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: 38.05  E-value: 5.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 422 LWVEDPAKKKKLFEILndkKLFKPPVLVFVDCKLGADLLSEAVQKitgLKRISIHSEKSQIERKNILKGLLEGDYEVVV- 500
Cdd:cd18798   5 VYIEDSDSLEKLLELV---KKLGDGGLIFVSIDYGKEYAEELKEF---LERHGIKAELALSSTEKNLEKFEEGEIDVLIg 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 27469538 501 ---STGVLGRGLDL-ISVRLVVNFDMPssMDEYVHQIGRVGRL 539
Cdd:cd18798  79 vasYYGVLVRGIDLpERIKYAIFYGVP--VTTYIQASGRTSRL 119
PRK13766 PRK13766
Hef nuclease; Provisional
249-355 5.33e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.86  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538  249 TGSGKTAAFLLpVIMRAL--FESKtpsALILTPTRELAIQIERQAKELMSgLPRMKTVLLVGGLPlPPQLYRLQQHVKVI 326
Cdd:PRK13766  38 TGLGKTAIALL-VIAERLhkKGGK---VLILAPTKPLVEQHAEFFRKFLN-IPEEKIVVFTGEVS-PEKRAELWEKAKVI 111
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 27469538  327 IATP---------GRlldiIKQSSVELCgvkivVVDEA 355
Cdd:PRK13766 112 VATPqviendliaGR----ISLEDVSLL-----IFDEA 140
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
248-354 6.54e-03

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 38.67  E-value: 6.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27469538 248 DTGSGKTA-AFLlpvIMRALFESKTPSALiLTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ----H 322
Cdd:cd17992  74 DVGSGKTVvAAL---AMLAAVENGYQVAL-MAPTEILAEQHYDSLKKLLEPLG-IRVALLTGSTKAKEKREILEKiasgE 148
                        90       100       110
                ....*....|....*....|....*....|..
gi 27469538 323 VKVIIATPGrlldIIkQSSVELCGVKIVVVDE 354
Cdd:cd17992 149 IDIVIGTHA----LI-QEDVEFHNLGLVIIDE 175
 
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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