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Conserved domains on  [gi|1168720088|ref|NP_001336732|]
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probable ATP-dependent RNA helicase DDX59 isoform 6 [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
89-508 2.85e-151

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: 443.08  E-value: 2.85e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206   12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206   87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206  167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE----------------------------------------------- 354
Cdd:PLN00206  246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEvdcmlergfrdqvmqifqalsqpqvllfsatvspevekfasslakdi 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 ---------------------------DKKLF---------KPPVLVFVDCKLGADLLSEAVQKITGLKSISIHSEKSQI 398
Cdd:PLN00206  326 ilisignpnrpnkavkqlaiwvetkqkKQKLFdilkskqhfKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSMK 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 399 ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAK 478
Cdd:PLN00206  406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1168720088 479 RVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 508
Cdd:PLN00206  486 LLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
 
Name Accession Description Interval E-value
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
89-508 2.85e-151

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 443.08  E-value: 2.85e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206   12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206   87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206  167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE----------------------------------------------- 354
Cdd:PLN00206  246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEvdcmlergfrdqvmqifqalsqpqvllfsatvspevekfasslakdi 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 ---------------------------DKKLF---------KPPVLVFVDCKLGADLLSEAVQKITGLKSISIHSEKSQI 398
Cdd:PLN00206  326 ilisignpnrpnkavkqlaiwvetkqkKQKLFdilkskqhfKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSMK 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 399 ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAK 478
Cdd:PLN00206  406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1168720088 479 RVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 508
Cdd:PLN00206  486 LLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
214-360 5.98e-89

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: 271.73  E-value: 5.98e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKE 293
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168720088 294 LMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFK 360
Cdd:cd17962    81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK 147
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
205-509 1.14e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 271.25  E-value: 1.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFE-SKTPSALILTPTREL 283
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-D------- 355
Cdd:COG0513    84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEaDrmldmgf 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 356 --------------------------------KKLFKPPV---------------------------------------- 363
Cdd:COG0513   163 iedierilkllpkerqtllfsatmppeirklaKRYLKNPVrievapenataetieqryylvdkrdklellrrllrdedpe 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 364 --LVFVDCKLGADLLSEAVQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSS 441
Cdd:COG0513   243 raIVFCNTKRGADRLAEKLQK-RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 442 MDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRvkpTGSILPPQLLNSPYLHDQKRKEQQKDK 509
Cdd:COG0513   322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIEEEELPGFEPVEEKRLERLKPK 386
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
227-354 7.21e-37

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: 133.91  E-value: 7.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 227 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLL 306
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1168720088 307 VGGLPLPPQLYRLqQHVKVIIATPGRLLDIIKQsSVELCGVKIVVVDE 354
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDE 125
DEXDc smart00487
DEAD-like helicases superfamily;
218-354 2.05e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 2.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  218 LKKSGYEVPTPIQMQMIPVGLLG-RDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAIQIERQAKELMS 296
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088  297 GLPRmKTVLLVGGLPLPPQLYRLQQHV-KVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:smart00487  80 SLGL-KVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
314-470 7.31e-05

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: 45.36  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 314 PQLYRLQQHVKVI--IATPGRLLD---IIKQSS--VE-LCGVKIVVVDEDKKlfkppVLVFVDCKLGA----DLLSEAvq 381
Cdd:TIGR00631 393 PGPYELEQSGNVVeqIIRPTGLLDpeiEVRPTDgqVDdLLSEIRQRVARNER-----VLVTTLTKKMAedltDYLKEL-- 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 382 kitGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-----MPSSMDEYVHQIGRVGRlG 456
Cdd:TIGR00631 466 ---GIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSERSLIQTIGRAAR-N 541
                         170
                  ....*....|....
gi 1168720088 457 QNGTAITFINNNSK 470
Cdd:TIGR00631 542 VNGKVIMYADKITD 555
 
Name Accession Description Interval E-value
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
89-508 2.85e-151

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 443.08  E-value: 2.85e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  89 EPVKSFSKTQRWAEPGEPICVVCGRYGEYICDKTDEDVCSLECKAKHLLQVKEKEEKSKLSNPQKADSEPESplnasYVY 168
Cdd:PLN00206   12 DVVKERSIEQREALPGEPKCVVCGRYGEYICDETDDDICSLECKQALLRRVAKSRVAVGAPKPKRLPATDEC-----FYV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 169 KEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASAD 248
Cdd:PLN00206   87 RDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSAD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 249 TGSGKTAAFLLPVIMRA-------LFESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PLN00206  167 TGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE----------------------------------------------- 354
Cdd:PLN00206  246 GVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEvdcmlergfrdqvmqifqalsqpqvllfsatvspevekfasslakdi 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 ---------------------------DKKLF---------KPPVLVFVDCKLGADLLSEAVQKITGLKSISIHSEKSQI 398
Cdd:PLN00206  326 ilisignpnrpnkavkqlaiwvetkqkKQKLFdilkskqhfKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSMK 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 399 ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAK 478
Cdd:PLN00206  406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1168720088 479 RVKPTGSILPPQLLNSPYL-HDQKRKEQQKD 508
Cdd:PLN00206  486 LLKSSGAAIPRELANSRYLgSGRKRKKKRRY 516
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
214-360 5.98e-89

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: 271.73  E-value: 5.98e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKE 293
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168720088 294 LMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFK 360
Cdd:cd17962    81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK 147
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
205-509 1.14e-85

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 271.25  E-value: 1.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFE-SKTPSALILTPTREL 283
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTREL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-D------- 355
Cdd:COG0513    84 ALQVAEELRKLAKYLG-LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEaDrmldmgf 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 356 --------------------------------KKLFKPPV---------------------------------------- 363
Cdd:COG0513   163 iedierilkllpkerqtllfsatmppeirklaKRYLKNPVrievapenataetieqryylvdkrdklellrrllrdedpe 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 364 --LVFVDCKLGADLLSEAVQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSS 441
Cdd:COG0513   243 raIVFCNTKRGADRLAEKLQK-RGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 442 MDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRvkpTGSILPPQLLNSPYLHDQKRKEQQKDK 509
Cdd:COG0513   322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL---IGQKIEEEELPGFEPVEEKRLERLKPK 386
PTZ00110 PTZ00110
helicase; Provisional
168-506 8.18e-64

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 217.33  E-value: 8.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 168 YKEHPFILNLQEDQIENLKQQLGI-LVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILAS 246
Cdd:PTZ00110   94 YKEHPEVSALSSKEVDEIRKEKEItIIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGI 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 247 ADTGSGKTAAFLLPVIMRALFESKT-----PSALILTPTRELAIQIERQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQ 321
Cdd:PTZ00110  174 AETGSGKTLAFLLPAIVHINAQPLLrygdgPIVLVLAPTRELAEQIREQCNKF-GASSKIRNTVAYGGVPKRGQIYALRR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 322 HVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL---FKP------------------------------------ 361
Cdd:PTZ00110  253 GVEILIACPGRLIDFLESNVTNLRRVTYLVLDEaDRMLdmgFEPqirkivsqirpdrqtlmwsatwpkevqslardlcke 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 362 ----------------------------------------------PVLVFVDCKLGADLLSEAVqKITGLKSISIHSEK 395
Cdd:PTZ00110  333 epvhvnvgsldltachnikqevfvveehekrgklkmllqrimrdgdKILIFVETKKGADFLTKEL-RLDGWPALCIHGDK 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 396 SQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWD 475
Cdd:PTZ00110  412 KQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARD 491
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1168720088 476 IAKRVKPTGSILPPQLLNSPYLHDQKRKEQQ 506
Cdd:PTZ00110  492 LVKVLREAKQPVPPELEKLSNERSNGTERRR 522
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
214-354 2.63e-57

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: 189.58  E-value: 2.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFES----KTPSALILTPTRELAIQIER 289
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168720088 290 QAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd00268    81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDE 144
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
204-465 6.96e-54

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 188.23  E-value: 6.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 204 DFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAL-FESKTPSA---LILTP 279
Cdd:PRK11192    2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdFPRRKSGPpriLILTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 280 TRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL 358
Cdd:PRK11192   82 TRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEaDRML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 359 ---FKP-------------------------------------PVLVFVD----------------------CKLGADLL 376
Cdd:PRK11192  161 dmgFAQdietiaaetrwrkqtllfsatlegdavqdfaerllndPVEVEAEpsrrerkkihqwyyraddlehkTALLCHLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 377 S--------------EAVQKITG-LKSISIHS-----EKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNF 436
Cdd:PRK11192  241 KqpevtrsivfvrtrERVHELAGwLRKAGINCcylegEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
                         330       340
                  ....*....|....*....|....*....
gi 1168720088 437 DMPSSMDEYVHQIGRVGRLGQNGTAITFI 465
Cdd:PRK11192  321 DMPRSADTYLHRIGRTGRAGRKGTAISLV 349
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
205-361 1.31e-50

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: 172.67  E-value: 1.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRaLFESK-----------TPS 273
Cdd:cd17967     2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISK-LLEDGppsvgrgrrkaYPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 274 ALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVD 353
Cdd:cd17967    81 ALILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
                         170
                  ....*....|..
gi 1168720088 354 E-DKKL---FKP 361
Cdd:cd17967   160 EaDRMLdmgFEP 171
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
211-481 1.23e-49

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 177.31  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 211 PEVLnHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS------ALILTPTRELA 284
Cdd:PRK10590   10 PDIL-RAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILTPTRELA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DK------- 356
Cdd:PRK10590   89 AQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEaDRmldmgfi 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 357 --------------------------------KLFKPP------------------------------------------ 362
Cdd:PRK10590  168 hdirrvlaklpakrqnllfsatfsddikalaeKLLHNPleievarrntaseqvtqhvhfvdkkrkrellsqmigkgnwqq 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 363 VLVFVDCKLGADLLSEAVQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSM 442
Cdd:PRK10590  248 VLVFTRTKHGANHLAEQLNK-DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1168720088 443 DEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAKRVK 481
Cdd:PRK10590  327 EDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
222-512 4.79e-45

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 168.10  E-value: 4.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLPRM 301
Cdd:PRK11634   25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE--------------------------- 354
Cdd:PRK11634  105 NVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEademlrmgfiedvetimaqipeghqta 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 -------------DKKLFKPP------------------------------------------VLVFVDCKLGADLLSEA 379
Cdd:PRK11634  185 lfsatmpeairriTRRFMKEPqevriqssvttrpdisqsywtvwgmrknealvrfleaedfdaAIIFVRTKNATLEVAEA 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 380 VQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNG 459
Cdd:PRK11634  265 LER-NGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAG 343
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1168720088 460 TAITFINNNSKRLFWDIAKRVKPTgsiLPPQLLNSPYLHDQKRKEQQKDKQTQ 512
Cdd:PRK11634  344 RALLFVENRERRLLRNIERTMKLT---IPEVELPNAELLGKRRLEKFAAKVQQ 393
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
214-361 7.86e-45

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 156.60  E-value: 7.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR--ALFESKTPSALILTPTRELAIQIERQA 291
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKlgKPRKKKGLRALILAPTRELASQIYREL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 292 KELMSGLPrMKTVLLVGGL-PLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFKP 361
Cdd:cd17957    81 LKLSKGTG-LRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEP 150
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
193-361 6.82e-44

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: 156.28  E-value: 6.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 193 VQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAL------ 266
Cdd:cd18052    33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkeglta 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 267 ---FESKTPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVE 343
Cdd:cd18052   113 ssfSEVQEPQALIVAPTRELANQIFLEARKFSYGTC-IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
                         170       180
                  ....*....|....*....|..
gi 1168720088 344 LCGVKIVVVDE-DKKL---FKP 361
Cdd:cd18052   192 LSKLKYLILDEaDRMLdmgFGP 213
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
204-466 5.46e-43

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 159.20  E-value: 5.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 204 DFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR---ALFEsktPSALILTPT 280
Cdd:PRK11776    5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKldvKRFR---VQALVLCPT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 281 RELAIQIERQAKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE------ 354
Cdd:PRK11776   82 RELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEadrmld 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 -----------------------------------------------------------------DKKL---------FK 360
Cdd:PRK11776  162 mgfqdaidaiirqaparrqtllfsatypegiaaisqrfqrdpvevkvesthdlpaieqrfyevspDERLpalqrlllhHQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 361 P-PVLVF----VDCKLGADLLSEAvqkitGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVN 435
Cdd:PRK11776  242 PeSCVVFcntkKECQEVADALNAQ-----GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1168720088 436 FDMPSSMDEYVHQIGRVGRLGQNGTAITFIN 466
Cdd:PRK11776  317 YELARDPEVHVHRIGRTGRAGSKGLALSLVA 347
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
222-358 1.28e-41

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: 148.17  E-value: 1.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALF---ESKTPSALILTPTRELAIQIERQAKELMSGL 298
Cdd:cd17947     9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYrpkKKAATRVLVLVPTRELAMQCFSVLQQLAQFT 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 299 PrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDEDKKL 358
Cdd:cd17947    89 D-ITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRM 148
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
200-464 3.09e-41

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 156.26  E-value: 3.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 200 RPIID--FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR-----ALFESK-- 270
Cdd:PRK04537    4 KPLTDltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRllsrpALADRKpe 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 271 TPSALILTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSS-VELCGVKI 349
Cdd:PRK04537   84 DPRALILAPTRELAIQIHKDAVKFGADLG-LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKvVSLHACEI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 350 VVVDEDKKLF---------------------------------------------------------------------- 359
Cdd:PRK04537  163 CVLDEADRMFdlgfikdirfllrrmpergtrqtllfsatlshrvlelayehmnepeklvvetetitaarvrqriyfpade 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 360 -KPPVL-------------VFVDCKLGADLLSEAVQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGL 425
Cdd:PRK04537  243 eKQTLLlgllsrsegartmVFVNTKAFVERVARTLER-HGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGL 321
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1168720088 426 DLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 464
Cdd:PRK04537  322 HIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
205-359 7.20e-41

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: 146.30  E-value: 7.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSL-PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS--ALILTPTR 281
Cdd:cd17959     3 FQSMGLsPPLLR-AIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGarALILSPTR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 282 ELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLF 359
Cdd:cd17959    82 ELALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
218-378 7.56e-41

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: 146.70  E-value: 7.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR-----ALFESKT---PSALILTPTRELAIQIER 289
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYisrlpPLDEETKddgPYALILAPTRELAQQIEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 290 QAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL---FKPPVLV 365
Cdd:cd17945    85 ETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEaDRMIdmgFEPQVTK 163
                         170
                  ....*....|...
gi 1168720088 366 FVDcKLGADLLSE 378
Cdd:cd17945   164 ILD-AMPVSNKKP 175
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
205-361 2.12e-39

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: 142.46  E-value: 2.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPvIMRALFESKTP-SALILTPTREL 283
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP-ILQALLENPQRfFALVLAPTREL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088 284 AIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSS-VELCGVKIVVVDEDKKLFKP 361
Cdd:cd17954    81 AQQISEQFEALGSSIG-LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNM 158
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
193-359 3.07e-38

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: 139.82  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 193 VQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI-----MRALF 267
Cdd:cd17953     2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 268 ESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSS---VEL 344
Cdd:cd17953    82 PGEGPIGLIMAPTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNL 160
                         170
                  ....*....|....*
gi 1168720088 345 CGVKIVVVDEDKKLF 359
Cdd:cd17953   161 RRVTYVVLDEADRMF 175
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
348-465 1.06e-37

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: 134.94  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 348 KIVVVDEDKKLFK-----------PPVLVFVDCKLGADLLSEAVQKItGLKSISIHSEKSQIERKNILKGLLEGDYEVVV 416
Cdd:cd18787     4 LYVVVEEEEKKLLlllllleklkpGKAIIFVNTKKRVDRLAELLEEL-GIKVAALHGDLSQEERERALKKFRSGKVRVLV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1168720088 417 STGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFI 465
Cdd:cd18787    83 ATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
227-354 7.21e-37

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: 133.91  E-value: 7.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 227 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLL 306
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1168720088 307 VGGLPLPPQLYRLqQHVKVIIATPGRLLDIIKQsSVELCGVKIVVVDE 354
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDE 125
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
211-464 5.03e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 138.95  E-value: 5.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 211 PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT-------PSALILTPTREL 283
Cdd:PRK04837   17 PQVVE-ALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPedrkvnqPRALIMAPTREL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 284 AIQIERQAKEL--MSGLprmKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFKp 361
Cdd:PRK04837   96 AVQIHADAEPLaqATGL---KLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFD- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 362 pvLVFV-DCKLGADLLSEAVQKITGLKSISI-------------HSEKSQIE---------------------------- 399
Cdd:PRK04837  172 --LGFIkDIRWLFRRMPPANQRLNMLFSATLsyrvrelafehmnNPEYVEVEpeqktghrikeelfypsneekmrllqtl 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 400 --------------------------------------------RKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVN 435
Cdd:PRK04837  250 ieeewpdraiifantkhrceeiwghlaadghrvglltgdvaqkkRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFN 329
                         330       340
                  ....*....|....*....|....*....
gi 1168720088 436 FDMPSSMDEYVHQIGRVGRLGQNGTAITF 464
Cdd:PRK04837  330 YDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
205-464 6.01e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 140.05  E-value: 6.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESK-------TPSALIL 277
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPpkerymgEPRALII 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 278 TPTRELAIQIERQAKEL--MSGLPRMKtvlLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:PRK01297  169 APTRELVVQIAKDAAALtkYTGLNVMT---FVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 DKKL----FKP--------------------------------------PVLVFVDC---------------------KL 371
Cdd:PRK01297  246 ADRMldmgFIPqvrqiirqtprkeerqtllfsatftddvmnlakqwttdPAIVEIEPenvasdtveqhvyavagsdkyKL 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 372 GADLLSE--------------AVQKI------TGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVR 431
Cdd:PRK01297  326 LYNLVTQnpwervmvfanrkdEVRRIeerlvkDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1168720088 432 LVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITF 464
Cdd:PRK01297  406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
205-358 2.18e-35

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: 131.27  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168720088 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKL 358
Cdd:cd17940    81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKL 153
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
214-359 5.15e-35

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: 130.23  E-value: 5.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIM-----RALFESKTPSALILTPTRELAIQIE 288
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVhimdqRELEKGEGPIAVIVAPTRELAQQIY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 289 RQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLF 359
Cdd:cd17952    81 LEAKKF-GKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF 150
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
168-368 7.06e-35

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: 132.06  E-value: 7.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 168 YKEHPFILNLQEDQIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASA 247
Cdd:cd18050    27 YVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 248 DTGSGKTAAFLLPVIMRA-----LFESKTPSALILTPTRELAIQIERQAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQH 322
Cdd:cd18050   107 QTGSGKTLAYLLPAIVHInhqpyLERGDGPICLVLAPTRELAQQVQQVADDYGKS-SRLKSTCIYGGAPKGPQIRDLERG 185
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1168720088 323 VKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKL----FKPPVLVFVD 368
Cdd:cd18050   186 VEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMldmgFEPQIRKIVD 235
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
218-354 1.30e-34

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: 129.63  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGL-LGRDILASADTGSGKTAAFLLPVIMRAL-----FESKTPSALILTPTRELAIQIERQA 291
Cdd:cd17964     9 LTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLntkpaGRRSGVSALIISPTRELALQIAAEA 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168720088 292 KELMSGLPRMKTVLLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSV--ELCGVKIVVVDE 354
Cdd:cd17964    89 KKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDE 154
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
195-361 4.12e-34

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: 129.39  E-value: 4.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 195 GQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPvIMRALFES----- 269
Cdd:cd18051    13 GENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLP-ILSQIYEQgpges 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 270 ------------KTPSALILTPTRELAIQIERQAKELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDII 337
Cdd:cd18051    92 lpsesgyygrrkQYPLALVLAPTRELASQIYDEARKF-AYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
                         170       180
                  ....*....|....*....|....*...
gi 1168720088 338 KQSSVELCGVKIVVVDE-DKKL---FKP 361
Cdd:cd18051   171 ERGKIGLDYCKYLVLDEaDRMLdmgFEP 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
205-354 4.37e-34

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 127.73  E-value: 4.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRAlfeSKTPS---ALILTPTR 281
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---SEDPYgifALVLTPTR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168720088 282 ELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCG---VKIVVVDE 354
Cdd:cd17955    78 ELAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDE 152
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
218-368 9.04e-34

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: 126.72  E-value: 9.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRA-----LFESKTPSALILTPTRELAIQIERQAK 292
Cdd:cd17966     5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHInaqppLERGDGPIVLVLAPTRELAQQIQQEAN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 293 ELmSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL---FKPPVLVFVD 368
Cdd:cd17966    85 KF-GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEaDRMLdmgFEPQIRKIVD 163
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
181-368 2.05e-33

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: 127.05  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 181 QIENLKQQLGILVQGQEVTRPIIDFEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLP 260
Cdd:cd18049     2 EVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 261 VIMRA-----LFESKTPSALILTPTRELAIQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLD 335
Cdd:cd18049    82 AIVHInhqpfLERGDGPICLVLAPTRELAQQVQQVAAEYGRAC-RLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1168720088 336 IIKQSSVELCGVKIVVVDEDKKL----FKPPVLVFVD 368
Cdd:cd18049   161 FLEAGKTNLRRCTYLVLDEADRMldmgFEPQIRKIVD 197
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
218-354 2.35e-33

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: 126.97  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLL-GRDILASADTGSGKTAAFLLPVIMRAL---------FESKTPSALILTPTRELAIQI 287
Cdd:cd17946     5 LADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLsqkssngvgGKQKPLRALILTPTRELAVQV 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 288 ERQAKELMSGlPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIV---VVDE 354
Cdd:cd17946    85 KDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDE 153
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
218-354 4.12e-33

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: 125.14  E-value: 4.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT--------PSALILTPTRELAIQ--- 286
Cdd:cd17951     5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpfikgegPYGLIVCPSRELARQthe 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 287 -IERQAKELM-SGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd17951    85 vIEYYCKALQeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDE 154
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
222-358 5.08e-33

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: 124.74  E-value: 5.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVImralfesKTPSALILTPTRELAIQ----IERQAKELMSg 297
Cdd:cd17938    18 DWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELAEQtyncIENFKKYLDN- 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 298 lPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKL 358
Cdd:cd17938    90 -PKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
218-358 6.43e-33

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: 124.30  E-value: 6.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSG 297
Cdd:cd17943     5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKK 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 298 LPRMKTVLLVGGLPLPPQLYRLQQhVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKL 358
Cdd:cd17943    85 LEGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144
DEXDc smart00487
DEAD-like helicases superfamily;
218-354 2.05e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 2.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  218 LKKSGYEVPTPIQMQMIPVGLLG-RDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAIQIERQAKELMS 296
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLP-ALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088  297 GLPRmKTVLLVGGLPLPPQLYRLQQHV-KVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:smart00487  80 SLGL-KVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDE 137
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
218-354 1.72e-30

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: 118.07  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT------PSALILTPTRELAIQIERQA 291
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqgTRALILVPTRELAQQVSKVL 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168720088 292 KELMSGL-PRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELC-GVKIVVVDE 354
Cdd:cd17961    89 EQLTAYCrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDE 153
PTZ00424 PTZ00424
helicase 45; Provisional
205-478 1.06e-29

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 120.70  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:PTZ00424   30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE---------- 354
Cdd:PTZ00424  110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEademlsrgfk 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 355 ------------------------------DKKLFKPPVLVFV--------------------DCKLgaDLLSEAVQKIT 384
Cdd:PTZ00424  189 gqiydvfkklppdvqvalfsatmpneilelTTKFMRDPKRILVkkdeltlegirqfyvavekeEWKF--DTLCDLYETLT 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 385 GLKSI------------------------SIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPS 440
Cdd:PTZ00424  267 ITQAIiycntrrkvdyltkkmherdftvsCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1168720088 441 SMDEYVHQIGRVGRLGQNGTAITFINNNSKRLFWDIAK 478
Cdd:PTZ00424  347 SPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
218-363 5.11e-29

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: 113.54  E-value: 5.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPS----ALILTPTRELAIQIERQAKE 293
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEVLRK 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168720088 294 LMSGlPRMKTVLLVGGLPLPPQLYRLQQhVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDE-DKKL---FKPPV 363
Cdd:cd17941    85 VGKY-HSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEaDRILdmgFKETL 157
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
217-363 6.12e-29

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: 113.33  E-value: 6.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 217 NLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKT------PSALILTPTRELAIQIERQ 290
Cdd:cd17958     4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPreqrngPGVLVLTPTRELALQIEAE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 291 -AKELMSGlprMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL---FKPPV 363
Cdd:cd17958    84 cSKYSYKG---LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEaDRMLdmgFEPQI 158
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
218-354 4.93e-27

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: 108.05  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI-----MRALFESKTPSALILTPTRELAIQIERQAK 292
Cdd:cd17960     5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeillkRKANLKKGQVGALIISPTRELATQIYEVLQ 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168720088 293 ELMS-GLPRMKTVLLVGGLPLPPQLYRLQQH-VKVIIATPGRLLDIIKQSSVELCG--VKIVVVDE 354
Cdd:cd17960    85 SFLEhHLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVKVksLEVLVLDE 150
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
218-354 8.71e-27

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: 107.45  E-value: 8.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 218 LKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLP---VIMRALFESKTPSA-LILTPTRELAIQIERQAKE 293
Cdd:cd17942     5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNGTGvIIISPTRELALQIYGVAKE 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168720088 294 LMSGlpRMKTVLLV-GGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELC-GVKIVVVDE 354
Cdd:cd17942    85 LLKY--HSQTFGIViGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYkNLQCLIIDE 145
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
222-360 1.51e-25

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: 103.94  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 222 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQAKELMSGLpRM 301
Cdd:cd17939    16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYM-GV 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088 302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFK 360
Cdd:cd17939    95 KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLS 153
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
211-358 9.28e-25

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: 102.04  E-value: 9.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 211 PEVLNhNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQIERQ 290
Cdd:cd17950    11 PELLR-AIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNE 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQ-QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE-DKKL 358
Cdd:cd17950    90 YERFSKYMPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDEcDKML 159
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
214-361 4.40e-24

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: 100.52  E-value: 4.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 214 LNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRaLFESK--------TPSALILTPTRELAI 285
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQR-LLRYKllaegpfnAPRGLVITPSRELAE 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168720088 286 QIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLFKP 361
Cdd:cd17948    80 QIGSVAQSLTEGLG-LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDD 154
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
219-404 1.54e-23

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: 98.81  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 219 KKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALfeSKTPS--------ALILTPTRELAIQIERQ 290
Cdd:cd17949     7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLL--SLEPRvdrsdgtlALVLVPTRELALQIYEV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQ-SSVELCGVKIVVVDEDKKLfkppvlvfVDC 369
Cdd:cd17949    85 LEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRL--------LDM 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1168720088 370 KLGADlLSEAVQKITGLKSISIHSEKSQIERKNIL 404
Cdd:cd17949   157 GFEKD-ITKILELLDDKRSKAGGEKSKPSRRQTVL 190
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
217-354 3.85e-23

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: 98.09  E-value: 3.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 217 NLKKSGYEVPTPIQMQMIP---------VGLLGRDILASADTGSGKTAAFLLPVImRALFESKTPS--ALILTPTRELAI 285
Cdd:cd17956     4 NLQNNGITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVPRlrALIVVPTKELVQ 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 286 QIERQAKELMSGLPrMKTVLLVGG------LPLPPQLYRLQQHVKV--IIATPGRLLDIIKQ-SSVELCGVKIVVVDE 354
Cdd:cd17956    83 QVYKVFESLCKGTG-LKVVSLSGQksfkkeQKLLLVDTSGRYLSRVdiLVATPGRLVDHLNStPGFTLKHLRFLVIDE 159
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
350-456 1.55e-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: 92.27  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 350 VVVDEDKKLFKPPVLVFvdCKLGADLLSEAVQKITGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLIS 429
Cdd:pfam00271   5 ALLELLKKERGGKVLIF--SQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
                          90       100
                  ....*....|....*....|....*..
gi 1168720088 430 VRLVVNFDMPSSMDEYVHQIGRVGRLG 456
Cdd:pfam00271  83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
374-456 1.49e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.81  E-value: 1.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088  374 DLLSEAVQKItGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVG 453
Cdd:smart00490   1 EELAELLKEL-GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 1168720088  454 RLG 456
Cdd:smart00490  80 RAG 82
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
205-354 1.31e-20

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: 89.83  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd18045    81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDE 149
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
205-354 4.57e-20

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: 88.27  E-value: 4.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELA 284
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 285 IQIERQAKELMSGLpRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd18046    81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
217-359 1.00e-19

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: 87.60  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 217 NLKKSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIMR------ALFESKTPSALILTPTRELAIQIerq 290
Cdd:cd17944     4 LLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKlqedqqPRKRGRAPKVLVLAPTRELANQV--- 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088 291 AKELMSGLPRMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDEDKKLF 359
Cdd:cd17944    81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML 149
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
211-354 7.51e-19

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: 84.55  E-value: 7.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 211 PEVLNHnLKKSGYEVPTPIQMQMIPVgLLG---RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRELAIQI 287
Cdd:cd17963     3 PELLKG-LYAMGFNKPSKIQETALPL-ILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168720088 288 ERQAKELMSgLPRMKTVLLVGGLPLPPQlYRLQQHvkVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd17963    81 GEVVEKMGK-FTGVKVALAVPGNDVPRG-KKITAQ--IVIGTPGTVLDWLKKRQLDLKKIKILVLDE 143
zf-HIT_DDX59 cd23022
zinc finger HIT (zf-HIT) found in DEAD box protein 59 (DDX59) and similar proteins; DDX59, ...
103-136 5.87e-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: 5.87e-17
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1168720088 103 PGEPICVVCGRYGEYICDKTDEDVCSLECKAKHL 136
Cdd:cd23022     1 GKEGWCVVCGRYANYYCDDTDDPVCSLECKRKHL 34
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
205-354 3.22e-13

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: 69.28  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRE 282
Cdd:cd18048    20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168720088 283 LAIQIERQAKELMSGLPRMKTVLLVGGlPLPPQLYRLQQhvKVIIATPGRLLD-IIKQSSVELCGVKIVVVDE 354
Cdd:cd18048   100 LALQTGKVVEEMGKFCVGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDE 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
240-482 7.84e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.82  E-value: 7.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 240 GRDILASADTGSGKTAAFLLpvIMRALFESKTpsALILTPTRELAIQIERQAKELMSGLPRMK---------TVLLVGGL 310
Cdd:COG1061   100 GGRGLVVAPTGTGKTVLALA--LAAELLRGKR--VLVLVPRRELLEQWAEELRRFLGDPLAGGgkkdsdapiTVATYQSL 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 311 PLPPQLYRLQQHVKVII----------------------------ATPGR----------LLDIIKQSSVE-------LC 345
Cdd:COG1061   176 ARRAHLDELGDRFGLVIideahhagapsyrrileafpaayrlgltATPFRsdgreillflFDGIVYEYSLKeaiedgyLA 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 346 GVKIVVVDED-----------------------------------KKLFKPPVLVFVDCKLGADLLSEAVQKItGLKSIS 390
Cdd:COG1061   256 PPEYYGIRVDltderaeydalserlrealaadaerkdkilrellrEHPDDRKTLVFCSSVDHAEALAELLNEA-GIRAAV 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 391 IHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQNGTAITFIN--NN 468
Cdd:COG1061   335 VTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDfvGN 414
                         330
                  ....*....|....
gi 1168720088 469 SKRLFWDIAKRVKP 482
Cdd:COG1061   415 DVPVLEELAKDLRD 428
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
240-354 8.90e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 65.89  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 240 GRDILASADTGSGKTAAFLLpvIMRALFESKTPSALILTPTRELAIQierQAKELMSGLPRMKTV-LLVGGLPLPPQLYR 318
Cdd:cd00046     1 GENVLITAPTGSGKTLAALL--AALLLLLKKGKKVLVLVPTKALALQ---TAERLRELFGPGIRVaVLVGGSSAEEREKN 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1168720088 319 LQQHVKVIIATPGRLLDIIKQS-SVELCGVKIVVVDE 354
Cdd:cd00046    76 KLGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDE 112
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
209-354 4.91e-11

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 64.92  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 209 SLPEVLNHnLKKSGYEVPTPIQMQMIPVGLL-GRDILASADTGSGKTA-AFLLpvIMRALFESKTpsALILTPTRELAIQ 286
Cdd:COG1204     7 PLEKVIEF-LKERGIEELYPPQAEALEAGLLeGKNLVVSAPTASGKTLiAELA--ILKALLNGGK--ALYIVPLRALASE 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168720088 287 IERQAKELMSGLPrMKTVLLVGGLPLPPqlYRLQQHvKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:COG1204    82 KYREFKRDFEELG-IKVGVSTGDYDSDD--EWLGRY-DILVATPEKLDSLLRNGPSWLRDVDLVVVDE 145
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
240-473 2.92e-10

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 62.93  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 240 GRDILASADTGSGKTAAFLLPVImRALFESKTPSALILTPTRELAI-QIERQAKELMSGLPRMKTVLLVGGLPlPPQLYR 318
Cdd:COG1205    71 GKNVVIATPTASGKSLAYLLPVL-EALLEDPGATALYLYPTKALARdQLRRLRELAEALGLGVRVATYDGDTP-PEERRW 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 319 LQQHVKVIIATP------------------------------------G--------RLLDII----------------- 337
Cdd:COG1205   149 IREHPDIVLTNPdmlhygllphhtrwarffrnlryvvideahtyrgvfGshvanvlrRLRRICrhygsdpqfilasatig 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 338 --KQSSVELCGVKIVVVDED-----KK---LFKPPV---------------------------LVFVDCKLGADLLSEAV 380
Cdd:COG1205   229 npAEHAERLTGRPVTVVDEDgsprgERtfvLWNPPLvddgirrsalaeaarlladlvreglrtLVFTRSRRGAELLARYA 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 381 QK--ITGLKSISIHSEKSQI---ERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRL 455
Cdd:COG1205   309 RRalREPDLADRVAAYRAGYlpeERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRR 388
                         330       340
                  ....*....|....*....|....*..
gi 1168720088 456 GQNGTAI---------TFINNNSKRLF 473
Cdd:COG1205   389 GQDSLVVlvagddpldQYYVRHPEELF 415
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
412-465 4.95e-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: 4.95e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1168720088 412 YEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRLGQ-NGTAITFI 465
Cdd:cd18785    23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKdEGEVILFV 77
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
205-354 6.48e-10

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: 58.96  E-value: 6.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 205 FEHCSLPEVLNHNLKKSGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIMRALFESKTPSALILTPTRE 282
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168720088 283 LAIQIERQAKELMSGLPRMKTVLLVGGlplppqlYRLQQHVK----VIIATPGRLLD-IIKQSSVELCGVKIVVVDE 354
Cdd:cd18047    83 LALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQKiseqIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDE 152
zf-HIT cd23020
zinc finger HIT (zf-HIT) domain; The zinc finger HIT (zf-HIT) is a novel zinc-binding domain ...
107-136 1.21e-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: 53.27  E-value: 1.21e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1168720088 107 ICVVCGRY-GEYICDKTDEDVCSLECKAKHL 136
Cdd:cd23020     1 TCGICGGYpGKYKCPRCGVPYCSLECYRKHL 31
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
212-359 4.81e-09

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: 57.00  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 212 EVLNHNLKKSGYEVPTPIQMQMIPVgLLGRDI-----------------LASADTGSGKTAAFLLPvIMRALFE------ 268
Cdd:cd17965    17 EILKGSNKTDEEIKPSPIQTLAIKK-LLKTLMrkvtkqtsneepklevfLLAAETGSGKTLAYLAP-LLDYLKRqeqepf 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 269 ------------SKTPSALILTPTRELAIQIERQAKELMSGLP-RMKTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLD 335
Cdd:cd17965    95 eeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLAS 174
                         170       180
                  ....*....|....*....|....
gi 1168720088 336 IIKQSSVELCGVKIVVVDEDKKLF 359
Cdd:cd17965   175 LAKSRPKILSRVTHLVVDEADTLF 198
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
227-354 1.33e-08

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: 54.58  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 227 TPIQMQMIPVGLL-GRDILASADTGSGKTAAFLLpVIMRALFESKtPSALILTPTRELAIQIERQAKELMSglPRMKTVL 305
Cdd:cd17921     3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAEL-AILRALATSG-GKAVYIAPTRALVNQKEADLRERFG--PLGKNVG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1168720088 306 LVGGLP--LPPQLYRLQqhvkVIIATPGRLLDIIKQSSVELCG-VKIVVVDE 354
Cdd:cd17921    79 LLTGDPsvNKLLLAEAD----ILVATPEKLDLLLRNGGERLIQdVRLVVVDE 126
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
373-464 2.01e-08

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 56.69  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 373 ADLLSEAvqkitGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRV 452
Cdd:COG0514   247 AEWLREA-----GIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
                          90
                  ....*....|..
gi 1168720088 453 GRLGQNGTAITF 464
Cdd:COG0514   322 GRDGLPAEALLL 333
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
373-464 3.31e-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: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 373 ADLLSEAVQKItGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRV 452
Cdd:cd18794    43 CEQVAARLQSK-GISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRA 121
                          90
                  ....*....|..
gi 1168720088 453 GRLGQNGTAITF 464
Cdd:cd18794   122 GRDGLPSECILF 133
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
240-354 2.68e-07

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: 50.66  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 240 GRDILASADTGSGKTAAFLLPVIMRALFESKTPSALI-LTPTRELAIQIERqakelmsglpRMKTVLLVGGLPLP----- 313
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLyISPLKALINDQER----------RLEEPLDEIDLEIPvavrh 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1168720088 314 ---PQLYRLQQHVK---VIIATPGRL--LDIIKQSSVELCGVKIVVVDE 354
Cdd:cd17922    71 gdtSQSEKAKQLKNppgILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
240-354 3.19e-07

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 50.66  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 240 GRDILASADTGSGKTAAFLLPvIMRALFESKTPSALILTPTRELAI-QIERQAKELMSGLPRMKTVLLVGGLPLPPQLYR 318
Cdd:cd17923    15 GRSVVVTTGTASGKSLCYQLP-ILEALLRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGDTPREERRAI 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1168720088 319 LQQHVKVIIATPGRL-LDIIKQSSVE---LCGVKIVVVDE 354
Cdd:cd17923    94 IRNPPRILLTNPDMLhYALLPHHDRWarfLRNLRYVVLDE 133
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
363-462 8.65e-07

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: 49.17  E-value: 8.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 363 VLVFVDCKLGADLLSEAVQKItGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD----- 437
Cdd:cd18790    30 VLVTTLTKRMAEDLTEYLQEL-GVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkeg 108
                          90       100
                  ....*....|....*....|....*
gi 1168720088 438 MPSSMDEYVHQIGRVGRlGQNGTAI 462
Cdd:cd18790   109 FLRSETSLIQTIGRAAR-NVNGKVI 132
zf-HIT pfam04438
HIT zinc finger; This presumed zinc finger contains up to 6 cysteine residues that could ...
105-132 9.37e-07

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: 9.37e-07
                          10        20
                  ....*....|....*....|....*...
gi 1168720088 105 EPICVVCGRYGEYICDKTDEDVCSLECK 132
Cdd:pfam04438   2 RKLCSVCGNPSKYRCPRCGVRYCSLECY 29
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
223-289 9.66e-07

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.64  E-value: 9.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168720088 223 YEVPTPIQMQMIPVGLLGRDILASADTGSGKT-AAFlLPVIMRaLFESKTPSAL-----IL--TPTRELAIQIER 289
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDE-LARRPRPGELpdglrVLyiSPLKALANDIER 94
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
241-309 1.09e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 48.95  E-value: 1.09e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088 241 RDILASADTGSGKTAAFLLPVIMRAlfeSKTPSALILTPTRELAIQIERQAKELmsgLPRMKTVLLVGG 309
Cdd:cd17918    37 MDRLLSGDVGSGKTLVALGAALLAY---KNGKQVAILVPTEILAHQHYEEARKF---LPFINVELVTGG 99
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
393-457 3.05e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 50.11  E-value: 3.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168720088 393 SEKSQIErknILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-MPSSMdEYVHQIGRVGRLGQ 457
Cdd:COG1111   396 TQKEQIE---ILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSIQRKGRTGRKRE 457
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
319-465 6.15e-06

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: 46.39  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 319 LQQHVKVI--IATPGRLLDIIKQSSVELCGVKIVVVDEDKklfkpPVLVFVDCKLGADLLSeavQKITGlksISI-HSEK 395
Cdd:cd18795     5 LEEYVLGFngLGIKLRVDVMNKFDSDIIVLLKIETVSEGK-----PVLVFCSSRKECEKTA---KDLAG---IAFhHAGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 396 SQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVN----FDmPSSMDEY----VHQ-IGRVGRLGQN--GTAITF 464
Cdd:cd18795    74 TREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYD-GKGYRELspleYLQmIGRAGRPGFDtrGEAIIM 152

                  .
gi 1168720088 465 I 465
Cdd:cd18795   153 T 153
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
342-457 1.05e-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: 45.16  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 342 VELCGVKIVVVDED-KKLFKPP--VLVFVDCKLGADLLSEAVQKItGLKSISIHSEKSQIERKNILKGLLEGDYEVV--V 416
Cdd:cd18793     6 EEVVSGKLEALLELlEELREPGekVLIFSQFTDTLDILEEALRER-GIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflL 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1168720088 417 STGVLGRGLDLISVRLVVNFDMP--SSMDEyvhQ-IGRVGRLGQ 457
Cdd:cd18793    85 STKAGGVGLNLTAANRVILYDPWwnPAVEE---QaIDRAHRIGQ 125
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
376-464 1.65e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.40  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 376 LSEAVQKiTGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGRL 455
Cdd:PRK11057  252 TAARLQS-RGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330

                  ....*....
gi 1168720088 456 GQNGTAITF 464
Cdd:PRK11057  331 GLPAEAMLF 339
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
314-470 7.31e-05

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: 45.36  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 314 PQLYRLQQHVKVI--IATPGRLLD---IIKQSS--VE-LCGVKIVVVDEDKKlfkppVLVFVDCKLGA----DLLSEAvq 381
Cdd:TIGR00631 393 PGPYELEQSGNVVeqIIRPTGLLDpeiEVRPTDgqVDdLLSEIRQRVARNER-----VLVTTLTKKMAedltDYLKEL-- 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 382 kitGLKSISIHSEKSQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD-----MPSSMDEYVHQIGRVGRlG 456
Cdd:TIGR00631 466 ---GIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSERSLIQTIGRAAR-N 541
                         170
                  ....*....|....
gi 1168720088 457 QNGTAITFINNNSK 470
Cdd:TIGR00631 542 VNGKVIMYADKITD 555
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
396-454 1.23e-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: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168720088 396 SQIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFDMPSSMDEYVHQIGRVGR 454
Cdd:cd18801    75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
103-135 8.38e-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: 8.38e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1168720088 103 PGEPICVVCGRYGEYICDKTDEDVCSLECKAKH 135
Cdd:cd21437     5 PPRKFCSVCGYWGKYTCVRCGARYCSLKCLETH 37
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
241-354 9.51e-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: 40.71  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 241 RDILASADTGSGKT-AAFLLPVIMRALFESKTPS---ALILTPTRELAIQierQAKELmsglpRMKTVLLVG------GL 310
Cdd:cd18034    17 RNTIVVLPTGSGKTlIAVMLIKEMGELNRKEKNPkkrAVFLVPTVPLVAQ---QAEAI-----RSHTDLKVGeysgemGV 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1168720088 311 PLPPQLYRLQ--QHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd18034    89 DKWTKERWKEelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDE 134
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
364-462 9.59e-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: 39.55  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 364 LVFVDCKLGADLLSEAVQKI---TGLKSISIHSEKS---QIERKNILKGLLEGDYEVVVSTGVLGRGLDLISVRLVVNFD 437
Cdd:cd18797    39 IVFCRSRKLAELLLRYLKARlveEGPLASKVASYRAgylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
                          90       100
                  ....*....|....*....|....*
gi 1168720088 438 MPSSMDEYVHQIGRVGRLGQNGTAI 462
Cdd:cd18797   119 YPGSLASLWQQAGRAGRRGKDSLVI 143
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
240-308 1.26e-03

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.45  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168720088 240 GRDILASADTGSGKTAAFLLPVIMRALFESKTpsALILTPTRELAIQI-ERQAKELMSGLPR-MKTVLLVG 308
Cdd:COG1199    33 GRHLLIEAGTGTGKTLAYLVPALLAARETGKK--VVISTATKALQEQLvEKDLPLLRKALGLpLRVALLKG 101
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
229-354 1.27e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 39.81  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 229 IQMQMIPVGLLGRDILASADTGSGKTAAFLLpvIMRALFESKTPSALILTPTRELAIQIERQAKELMSglPRMKTVLLVG 308
Cdd:cd18035     5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAIL--VAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLN--IPDKITSLTG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1168720088 309 GLPlPPQLYRLQQHVKVIIATPGRLLDIIKQSSVELCGVKIVVVDE 354
Cdd:cd18035    81 EVK-PEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDE 125
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
364-451 1.29e-03

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: 39.11  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 364 LVFVD----CKLGADLLSEAVQKITGLKS-------------ISIHSEKSQIErknILKGLLEGDYEVVVSTGVLGRGLD 426
Cdd:cd18802    29 IIFVErratAVVLSRLLKEHPSTLAFIRCgfligrgnssqrkRSLMTQRKQKE---TLDKFRDGELNLLIATSVLEEGID 105
                          90       100
                  ....*....|....*....|....*
gi 1168720088 427 LISVRLVVNFDMPSSMDEYVHQIGR 451
Cdd:cd18802   106 VPACNLVIRFDLPKTLRSYIQSRGR 130
PRK13767 PRK13767
ATP-dependent helicase; Provisional
220-354 1.97e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 41.02  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 220 KSGYEVPTPIQMQMIPVGLLGRDILASADTGSGKT-AAFLlpVIMRALFE-------SKTPSALILTPTRELAIQIERQA 291
Cdd:PRK13767   27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL--AIIDELFRlgregelEDKVYCLYVSPLRALNNDIHRNL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 292 KELMSGLprmKTVLLVGGLPLPP----------QLYRLQQHVK----VIIATPgRLLDIIKQS---SVELCGVKIVVVDE 354
Cdd:PRK13767  105 EEPLTEI---REIAKERGEELPEirvairtgdtSSYEKQKMLKkpphILITTP-ESLAILLNSpkfREKLRTVKWVIVDE 180
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
248-354 4.01e-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: 39.05  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 248 DTGSGKTA-AFLlpvIMRALFESKTPSALiLTPTRELAIQIERQAKELMSGLPrMKTVLLVGGLPLPPQLYRLQQ----H 322
Cdd:cd17992    74 DVGSGKTVvAAL---AMLAAVENGYQVAL-MAPTEILAEQHYDSLKKLLEPLG-IRVALLTGSTKAKEKREILEKiasgE 148
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1168720088 323 VKVIIATPGrlldIIkQSSVELCGVKIVVVDE 354
Cdd:cd17992   149 IDIVIGTHA----LI-QEDVEFHNLGLVIIDE 175
PRK13766 PRK13766
Hef nuclease; Provisional
249-330 4.73e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.86  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 249 TGSGKTAAFLLpVIMRAL--FESKtpsALILTPTRELAIQIERQAKELMSgLPRMKTVLLVGGLPlPPQLYRLQQHVKVI 326
Cdd:PRK13766   38 TGLGKTAIALL-VIAERLhkKGGK---VLILAPTKPLVEQHAEFFRKFLN-IPEEKIVVFTGEVS-PEKRAELWEKAKVI 111

                  ....
gi 1168720088 327 IATP 330
Cdd:PRK13766  112 VATP 115
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
226-354 6.18e-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: 38.18  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168720088 226 PTPIQMQMIPVGLLGRDILASADTGSGKTaaFLLPVIMRALFESKTPS----ALILTPTRELAIQIERQAKELMsGLPRM 301
Cdd:cd17927     3 PRNYQLELAQPALKGKNTIICLPTGSGKT--FVAVLICEHHLKKFPAGrkgkVVFLANKVPLVEQQKEVFRKHF-ERPGY 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168720088 302 KTVLLVGGLPLPPQLYRLQQHVKVIIATPGRLLDIIKQ-SSVELCGVKIVVVDE 354
Cdd:cd17927    80 KVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDE 133
 
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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