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Conserved domains on  [gi|351065690|emb|CCD61680|]
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RNA helicase [Caenorhabditis elegans]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

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

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
88-504 5.24e-132

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 391.43  E-value: 5.24e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  88 TKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYG-IYALILTPT 166
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 167 RELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdTIakVFKKIQFFVLDEADR 246
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERG--AL--DLSGVETLVLDEADR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 247 MLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEdkGKDDESTVDRLEQKYVVCPVAVKDAYLVY 326
Cdd:COG0513  157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--VAPENATAETIEQRYYLVDKRDKLELLRR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 327 VVKNYSEKnpksSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHV 406
Cdd:COG0513  235 LLRDEDPE----RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 407 DLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKLDELKV-SPKHVTKYVTQVLVAKKEAE 485
Cdd:COG0513  311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELpGFEPVEEKRLERLKPKIKEK 390
                        410
                 ....*....|....*....
gi 351065690 486 LKLENQKFGEKKEINRRKE 504
Cdd:COG0513  391 LKGKKAGRGGRPGPKGERK 409
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
88-504 5.24e-132

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 391.43  E-value: 5.24e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  88 TKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYG-IYALILTPT 166
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 167 RELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdTIakVFKKIQFFVLDEADR 246
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERG--AL--DLSGVETLVLDEADR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 247 MLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEdkGKDDESTVDRLEQKYVVCPVAVKDAYLVY 326
Cdd:COG0513  157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--VAPENATAETIEQRYYLVDKRDKLELLRR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 327 VVKNYSEKnpksSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHV 406
Cdd:COG0513  235 LLRDEDPE----RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 407 DLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKLDELKV-SPKHVTKYVTQVLVAKKEAE 485
Cdd:COG0513  311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELpGFEPVEEKRLERLKPKIKEK 390
                        410
                 ....*....|....*....
gi 351065690 486 LKLENQKFGEKKEINRRKE 504
Cdd:COG0513  391 LKGKKAGRGGRPGPKGERK 409
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
91-295 5.80e-109

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: 324.18  E-value: 5.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELA 170
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIaKVFKKIQFFVLDEADRMLEG 250
Cdd:cd17955   81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTT-KVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 351065690 251 QYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFE 295
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
86-461 1.47e-79

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 257.42  E-value: 1.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  86 MTTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTP 165
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 166 TRELAFQIAEQFTALGKPI-TLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKVfkkiQFFVLDEA 244
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDAL----NTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 245 DRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEDKGKDDESTVdrlEQKYVVCPVAVKDAYL 324
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAI---EQRFYEVSPDERLPAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 325 VYVVKNYsekNPKSSVmIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIP 404
Cdd:PRK11776 234 QRLLLHH---QPESCV-VFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 351065690 405 HVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKLD 461
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
113-283 8.63e-59

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: 192.84  E-value: 8.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  113 TPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIV 192
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  193 GGRSLIHQARELsERPHVVVATPGRLADLIEsdpdtIAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLL 272
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 351065690  273 SATITNNINML 283
Cdd:pfam00270 155 SATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
104-311 4.79e-46

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.74  E-value: 4.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690   104 LQTMQIKTATPVQAACIPKILEG-SDILGCARTGTGKTLAFAIPILQKLSVDPyGIYALILTPTRELAFQIAEQFTALGK 182
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690   183 PITLKCSVIVGGRSLIHQAREL-SERPHVVVATPGRLADLIESDPdtiaKVFKKIQFFVLDEADRMLEGQYNDQLKPIFE 261
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDK----LSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 351065690   262 SISEKRQTLLLSATITNNINMLHRVSTRKPYFFedkgKDDESTVDRLEQK 311
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI----DVGFTPLEPIEQF 201
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
328-505 9.77e-03

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: 38.82  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  328 VKNYSEKNPKssVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVD 407
Cdd:TIGR00631 435 IRQRVARNER--VLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  408 LV--VNHNVPQCPKTY---IHRVGRSARAGRfGSALSF---VTQYDVELLQAVEQVIGKKLD---ELKVSPKHVTKYVTQ 476
Cdd:TIGR00631 513 LVaiLDADKEGFLRSErslIQTIGRAARNVN-GKVIMYadkITDSMQKAIEETERRRKIQMAyneEHGITPQTIRKPIRD 591
                         170       180       190
                  ....*....|....*....|....*....|
gi 351065690  477 VLVAK-KEAELKLENQKFGEKKEINRRKEL 505
Cdd:TIGR00631 592 ILDIElKEKEDAAKKKKKGEDLSDLSKKEL 621
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
88-504 5.24e-132

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 391.43  E-value: 5.24e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  88 TKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYG-IYALILTPT 166
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 167 RELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdTIakVFKKIQFFVLDEADR 246
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERG--AL--DLSGVETLVLDEADR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 247 MLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEdkGKDDESTVDRLEQKYVVCPVAVKDAYLVY 326
Cdd:COG0513  157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--VAPENATAETIEQRYYLVDKRDKLELLRR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 327 VVKNYSEKnpksSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHV 406
Cdd:COG0513  235 LLRDEDPE----RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 407 DLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKLDELKV-SPKHVTKYVTQVLVAKKEAE 485
Cdd:COG0513  311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELpGFEPVEEKRLERLKPKIKEK 390
                        410
                 ....*....|....*....
gi 351065690 486 LKLENQKFGEKKEINRRKE 504
Cdd:COG0513  391 LKGKKAGRGGRPGPKGERK 409
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
91-295 5.80e-109

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: 324.18  E-value: 5.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELA 170
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIaKVFKKIQFFVLDEADRMLEG 250
Cdd:cd17955   81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTT-KVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 351065690 251 QYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFE 295
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
86-461 1.47e-79

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 257.42  E-value: 1.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  86 MTTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTP 165
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 166 TRELAFQIAEQFTALGKPI-TLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKVfkkiQFFVLDEA 244
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDAL----NTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 245 DRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEDKGKDDESTVdrlEQKYVVCPVAVKDAYL 324
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAI---EQRFYEVSPDERLPAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 325 VYVVKNYsekNPKSSVmIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIP 404
Cdd:PRK11776 234 QRLLLHH---QPESCV-VFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 351065690 405 HVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKLD 461
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
100-291 1.88e-74

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: 235.03  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY----GIYALILTPTRELAFQIAE 175
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgrGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 176 QFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYNDQ 255
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG----KLDLSNVKYLVLDEADRMLDMGFEED 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 351065690 256 LKPIFESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd00268  157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNP 192
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
91-291 7.44e-74

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: 233.75  E-value: 7.44e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELA 170
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIEsdpDTIAKVFKKIQFFVLDEADRMLEG 250
Cdd:cd17954   82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLE---NTKGFSLKSLKFLVMDEADRLLNM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 351065690 251 QYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17954  159 DFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
104-503 9.56e-67

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 222.90  E-value: 9.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLsVD-------PYGIyaLILTPTRELAFQIAEQ 176
Cdd:PRK11192  16 LQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL-LDfprrksgPPRI--LILTPTRELAMQVADQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 177 FTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPdtiakvF--KKIQFFVLDEADRMLEGQYnd 254
Cdd:PRK11192  93 ARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN------FdcRAVETLILDEADRMLDMGF-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 255 qlKPIFESIS-EKR---QTLLLSATITNN--INMLHRVSTrKPYFFedkgkddESTVDRLEQK------YVVCPVAVKDA 322
Cdd:PRK11192 165 --AQDIETIAaETRwrkQTLLFSATLEGDavQDFAERLLN-DPVEV-------EAEPSRRERKkihqwyYRADDLEHKTA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 323 YLVYVVKnysEKNPKSSVmIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLD 402
Cdd:PRK11192 235 LLCHLLK---QPEVTRSI-VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 403 IPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKL-----DELKVSPKHVTKYVTQV 477
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLkarviDELRPKTKAPSEKKTGK 390
                        410       420
                 ....*....|....*....|....*.
gi 351065690 478 LVAKKEAELKLENQKFGEKKEINRRK 503
Cdd:PRK11192 391 PSKKVLAKRAEKKEKEKEKPKVKKRH 416
PTZ00424 PTZ00424
helicase 45; Provisional
115-474 4.91e-62

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 209.68  E-value: 4.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 115 VQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGG 194
Cdd:PTZ00424  54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 195 RSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSA 274
Cdd:PTZ00424 134 TVVRDDINKLKAGVHMVVGTPGRVYDMIDKR----HLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSA 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 275 TITNNINMLHRVSTRKPYFFedKGKDDESTVDRLEQKYVVCPvavKDAYLVYVVKNYSEKNPKSSVMIFAQTCRECQALA 354
Cdd:PTZ00424 210 TMPNEILELTTKFMRDPKRI--LVKKDELTLEGIRQFYVAVE---KEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLT 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 355 YMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRF 434
Cdd:PTZ00424 285 KKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRK 364
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 351065690 435 GSALSFVTQYDVELLQAVEQVIGKKLDELkvsPKHVTKYV 474
Cdd:PTZ00424 365 GVAINFVTPDDIEQLKEIERHYNTQIEEM---PMEVADYL 401
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
75-476 5.76e-62

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 211.31  E-value: 5.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  75 TPKPIQ-------ISEDNMTTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPI 147
Cdd:PRK01297  66 KPKPASlwkledfVVEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISI 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 148 LQKLSVDPYG-------IYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSER-PHVVVATPGRLA 219
Cdd:PRK01297 146 INQLLQTPPPkerymgePRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 220 DLIESdpdtiAKV-FKKIQFFVLDEADRMLEGQYNDQLKPIFESISEK--RQTLLLSATITNNINMLHRVSTRKPYFFED 296
Cdd:PRK01297 226 DFNQR-----GEVhLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEI 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 297 KGKDDEStvDRLEQKyvVCPVAVKDAY-LVYvvkNYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQ 375
Cdd:PRK01297 301 EPENVAS--DTVEQH--VYAVAGSDKYkLLY---NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHK 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 376 RLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQV 455
Cdd:PRK01297 374 RIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEEL 453
                        410       420
                 ....*....|....*....|.
gi 351065690 456 IGKKLDeLKVSPKHVTKYVTQ 476
Cdd:PRK01297 454 LGRKIS-CEMPPAELLKPVPR 473
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
91-460 1.90e-59

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 204.27  E-value: 1.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYG------IYALILT 164
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 165 PTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEA 244
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN----AVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 245 DRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEDKGKDDEStvDRLEQKYVVCPVAVKDAYL 324
Cdd:PRK10590 159 DRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAS--EQVTQHVHFVDKKRKRELL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 325 VYVVKnyseKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIP 404
Cdd:PRK10590 237 SQMIG----KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 351065690 405 HVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKL 460
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
113-283 8.63e-59

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: 192.84  E-value: 8.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  113 TPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIV 192
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  193 GGRSLIHQARELsERPHVVVATPGRLADLIEsdpdtIAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLL 272
Cdd:pfam00270  81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-----ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 351065690  273 SATITNNINML 283
Cdd:pfam00270 155 SATLPRNLEDL 165
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
100-308 6.98e-58

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: 193.22  E-value: 6.98e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKIL-EGSDILGCARTGTGKTLAFAIPILQKL-----SVDPYGI----YALILTPTREL 169
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKqkplRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 170 AFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKvFKKIQFFVLDEADRMLE 249
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAN-LKSLRFLVLDEADRMLE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351065690 250 GQYNDQLKPIFESI-------SEKRQTLLLSATITNNINMLHRVSTRKPYFFEDKGKDDESTVDRL 308
Cdd:cd17946  160 KGHFAELEKILELLnkdragkKRKRQTFVFSATLTLDHQLPLKLNSKKKKKKKEKKQKLELLIEKV 225
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
91-456 7.09e-58

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 203.93  E-value: 7.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELA 170
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPI-TLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAkvfkKIQFFVLDEADRMLE 249
Cdd:PRK11634  88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLS----KLSGLVLDEADEMLR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 250 GQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYffEDKGKDDESTVDRLEQKYVVCPVAVKDAYLVyvvk 329
Cdd:PRK11634 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQ--EVRIQSSVTTRPDISQSYWTVWGMRKNEALV---- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 330 NYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLV 409
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 351065690 410 VNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVI 456
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTM 364
PTZ00110 PTZ00110
helicase; Provisional
74-463 7.46e-58

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 202.31  E-value: 7.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  74 DTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSV 153
Cdd:PTZ00110 124 NVPKPVV---------SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 154 DPY-----GIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDT 228
Cdd:PTZ00110 195 QPLlrygdGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTN 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 229 IAKVfkkiQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKPYFFEDKGKDDESTVDRL 308
Cdd:PTZ00110 275 LRRV----TYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDLTACHNI 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 309 EQKYVVCPVAVKDAYLVYVVKNYSEKNPKssVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTL 388
Cdd:PTZ00110 351 KQEVFVVEEHEKRGKLKMLLQRIMRDGDK--ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKS 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 389 QVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVT--QYD-----VELLQAVEQVIGKKLD 461
Cdd:PTZ00110 429 PIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTpdKYRlardlVKVLREAKQPVPPELE 508

                 ..
gi 351065690 462 EL 463
Cdd:PTZ00110 509 KL 510
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
104-291 3.61e-56

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: 187.08  E-value: 3.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY---GIYALILTPTRELAFQIAEQFTAL 180
Cdd:cd17947    5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKkkaATRVLVLVPTRELAMQCFSVLQQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 181 GKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPdtiAKVFKKIQFFVLDEADRMLEGQYNDQLKPIF 260
Cdd:cd17947   85 AQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSP---SFDLDSIEILVLDEADRMLEEGFADELKEIL 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 351065690 261 ESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17947  162 RLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
81-460 2.58e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 190.55  E-value: 2.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  81 ISEDNMTTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL-------SV 153
Cdd:PRK04537   1 MSDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 154 DPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiaKV- 232
Cdd:PRK04537  81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH-----KVv 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 233 -FKKIQFFVLDEADRMLEGQYNDQLKPIFESISEK--RQTLLLSATITNNINMLHRVSTRKPyffEDKGKDDES-TVDRL 308
Cdd:PRK04537 156 sLHACEICVLDEADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEP---EKLVVETETiTAARV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 309 EQKyVVCPVAVKDAYLVYVVKNYSEKnpkSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTL 388
Cdd:PRK04537 233 RQR-IYFPADEEKQTLLLGLLSRSEG---ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351065690 389 QVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIGKKL 460
Cdd:PRK04537 309 EILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI 380
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
110-291 5.05e-53

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: 179.42  E-value: 5.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 110 KTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL--SVDPYGIYALILTPTRELAFQIAEQFTALGKPITLK 187
Cdd:cd17959   22 KVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkaHSPTVGARALILSPTRELALQTLKVTKELGKFTDLR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 188 CSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIakvfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKR 267
Cdd:cd17959  102 TALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKL----SSVEYVVFDEADRLFEMGFAEQLHEILSRLPENR 177
                        170       180
                 ....*....|....*....|....
gi 351065690 268 QTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17959  178 QTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
104-293 5.11e-53

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: 179.02  E-value: 5.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY----GIYALILTPTRELAFQIAEQFTA 179
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWtpedGLGALIISPTRELAMQIFEVLRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 180 LGKPITLKCSVIVGGRSLIHQARELSERpHVVVATPGRLADLIESDPDTiakVFKKIQFFVLDEADRMLEGQYNDQLKPI 259
Cdd:cd17941   85 VGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGF---DTSNLQMLVLDEADRILDMGFKETLDAI 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 351065690 260 FESISEKRQTLLLSATITNNINMLHRVSTRKPYF 293
Cdd:cd17941  161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEY 194
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
82-457 3.88e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 183.63  E-value: 3.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  82 SEDNMTTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDP------ 155
Cdd:PRK04837   1 SKTHLTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapedrk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 156 -YGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiakVF- 233
Cdd:PRK04837  81 vNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN------HIn 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 234 -KKIQFFVLDEADRMLEGQYNDQLKPIFESISE--KRQTLLLSATITnninmlHRVstrKPYFFEDKgKDDESTVDRLEQ 310
Cdd:PRK04837 155 lGAIQVVVLDEADRMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLS------YRV---RELAFEHM-NNPEYVEVEPEQ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 311 KyvvCPVAVKDAyLVY-------------VVKNYSEKnpkssVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRL 377
Cdd:PRK04837 225 K---TGHRIKEE-LFYpsneekmrllqtlIEEEWPDR-----AIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 378 AALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQAVEQVIG 457
Cdd:PRK04837 296 RILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG 375
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
104-294 4.39e-52

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 177.00  E-value: 4.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILE-GSDILGCARTGTGKTLAFAIPILQKL-----SVDPYGIYALILTPTRELAFQIAEQF 177
Cdd:cd17964    9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQIAAEA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 178 TALGKPIT-LKCSVIVGGRSLIHQAREL-SERPHVVVATPGRLADLIEsDPdTIAKVFKKIQFFVLDEADRMLEGQYNDQ 255
Cdd:cd17964   89 KKLLQGLRkLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLE-NP-GVAKAFTDLDYLVLDEADRLLDMGFRPD 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 351065690 256 LKPIFESI----SEKRQTLLLSATITNNINMLHRVSTRKPYFF 294
Cdd:cd17964  167 LEQILRHLpeknADPRQTLLFSATVPDEVQQIARLTLKKDYKF 209
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
308-441 5.09e-51

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: 171.15  E-value: 5.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 308 LEQKYVVCPvavKDAYLVYVVKNYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKT 387
Cdd:cd18787    1 IKQLYVVVE---EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 351065690 388 LQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFV 441
Cdd:cd18787   78 VRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
91-283 3.79e-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: 172.29  E-value: 3.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIY----------A 160
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgrgrrkaypsA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 161 LILTPTRELAFQI---AEQFtALGKPItlKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESdpdtiAKV-FKKI 236
Cdd:cd17967   82 LILAPTRELAIQIyeeARKF-SYRSGV--RSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIER-----GRIsLSSI 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 351065690 237 QFFVLDEADRMLEGQYNDQLKPIFESIS----EKRQTLLLSATITNNINML 283
Cdd:cd17967  154 KFLVLDEADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRL 204
DEXDc smart00487
DEAD-like helicases superfamily;
104-311 4.79e-46

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.74  E-value: 4.79e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690   104 LQTMQIKTATPVQAACIPKILEG-SDILGCARTGTGKTLAFAIPILQKLSVDPyGIYALILTPTRELAFQIAEQFTALGK 182
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690   183 PITLKCSVIVGGRSLIHQAREL-SERPHVVVATPGRLADLIESDPdtiaKVFKKIQFFVLDEADRMLEGQYNDQLKPIFE 261
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDK----LSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 351065690   262 SISEKRQTLLLSATITNNINMLHRVSTRKPYFFedkgKDDESTVDRLEQK 311
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI----DVGFTPLEPIEQF 201
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
100-291 6.15e-46

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: 160.95  E-value: 6.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY--------GIYALILTPTRELAF 171
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldeetkddGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 172 QIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQ 251
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERR----LLVLNQCTYVVLDEADRMIDMG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 252 YNDQLKPIFESI--------------------SEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17945  157 FEPQVTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRP 216
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
74-291 9.86e-45

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: 157.54  E-value: 9.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  74 DTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPIL----- 148
Cdd:cd17953    6 DCPKPIQ---------KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikd 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 149 QKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDT 228
Cdd:cd17953   77 QRPVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGR 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351065690 229 IAKVfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17953  157 VTNL-RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
100-293 1.22e-44

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 156.27  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTA 179
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 180 LGKPIT-LKCSVIVGGRSLIHQARELSeRPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYNDQLKP 258
Cdd:cd17943   81 IGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELG----ALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 351065690 259 IFESISEKRQTLLLSATI-TNNINMLHRVsTRKPYF 293
Cdd:cd17943  156 IFSSLPKNKQVIAFSATYpKNLDNLLARY-MRKPVL 190
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
105-293 2.63e-44

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: 156.21  E-value: 2.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 105 QTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL-SVDPY-----GIYALILTPTRELAFQIAEQFT 178
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRvdrsdGTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 179 ALGKPIT-LKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESdpdTIAKVFKKIQFFVLDEADRMLEGQYNDQLK 257
Cdd:cd17949   87 KLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKN---TQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 351065690 258 PIFESISEK-------------RQTLLLSATITNNINMLHRVSTRKPYF 293
Cdd:cd17949  164 KILELLDDKrskaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVY 212
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
73-460 2.92e-44

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 164.58  E-value: 2.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  73 DDTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL- 151
Cdd:PLN00206 114 EAVPPPIL---------SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCc 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 152 ------SVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESD 225
Cdd:PLN00206 185 tirsghPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKH 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 226 PDTIAKVFkkiqFFVLDEADRMLEGQYNDQLKPIFESISEKrQTLLLSATITNNINMLHRvSTRKPYFFEDKGKDDESTv 305
Cdd:PLN00206 265 DIELDNVS----VLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFAS-SLAKDIILISIGNPNRPN- 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 306 DRLEQKYVVCPVAVKDAYLVYVVKNYSEKNPKSSVMIFAQTCRECQALAyMFEGLGFRVGSLHSQIPQKQRLAALSAFRS 385
Cdd:PLN00206 338 KAVKQLAIWVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANA-ITVVTGLKALSIHGEKSMKERREVMKSFLV 416
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 386 KTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYD-------VELLQAVEQVIGK 458
Cdd:PLN00206 417 GEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDrnlfpelVALLKSSGAAIPR 496

                 ..
gi 351065690 459 KL 460
Cdd:PLN00206 497 EL 498
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
100-283 1.46e-43

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: 153.89  E-value: 1.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL------SVDPYGIYALILTPTRELAFQI 173
Cdd:cd17961    5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 174 AEQFTALgkpiTLKCSV------IVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtIAKVFKKIQFFVLDEADRM 247
Cdd:cd17961   85 SKVLEQL----TAYCRKdvrvvnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESG---SLLLLSTLKYLVIDEADLV 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 351065690 248 LEGQYNDQLKPIFESISEKRQTLLLSATITNNINML 283
Cdd:cd17961  158 LSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEAL 193
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
104-291 5.39e-43

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: 152.34  E-value: 5.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL-----SVDPYGIYALILTPTRELAFQI---AE 175
Cdd:cd17960    5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIyevLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 176 QFTALGKPiTLKCSVIVGGRSLIHQARELSE-RPHVVVATPGRLADLIESDPDTIAkvFKKIQFFVLDEADRMLEGQYND 254
Cdd:cd17960   85 SFLEHHLP-KLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVK--VKSLEVLVLDEADRLLDLGFEA 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 351065690 255 QLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17960  162 DLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
102-294 4.98e-42

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: 150.86  E-value: 4.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 102 QQLQTMQIKTATPVQAACIPKILEGS---------DILGCARTGTGKTLAFAIPILQKLS--VDPYgIYALILTPTRELA 170
Cdd:cd17956    3 KNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSkrVVPR-LRALIVVPTKELV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSE--------RPHVVVATPGRLADLIESDPDTIakvFKKIQFFVLD 242
Cdd:cd17956   82 QQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylsRVDILVATPGRLVDHLNSTPGFT---LKHLRFLVID 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351065690 243 EADRMLEGQYNDQL----KPIFESISEKR----------------QTLLLSATITNNINMLHRVSTRKPYFF 294
Cdd:cd17956  159 EADRLLNQSFQDWLetvmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRPRLF 230
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
104-291 7.40e-42

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: 149.05  E-value: 7.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIP---ILQKLSVDPY-GIYALILTPTRELAFQIAEQFTA 179
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRnGTGVIIISPTRELALQIYGVAKE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 180 LGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIakvFKKIQFFVLDEADRMLEGQYNDQLKPI 259
Cdd:cd17942   85 LLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFL---YKNLQCLIIDEADRILEIGFEEEMRQI 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 351065690 260 FESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17942  162 IKLLPKRRQTMLFSATQTRKVEDLARISLKKK 193
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
71-294 9.87e-42

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: 150.89  E-value: 9.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  71 SSDDTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQK 150
Cdd:cd18052   34 TGRNPPPAIL---------TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 151 LSVDpyGI-----------YALILTPTRELAFQI---AEQFtALGKPItlKCSVIVGGRSLIHQARELSERPHVVVATPG 216
Cdd:cd18052  105 MMKE--GLtassfsevqepQALIVAPTRELANQIfleARKF-SYGTCI--RPVVVYGGVSVGHQIRQIEKGCHILVATPG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 217 RLADLIESdpdtiAKV-FKKIQFFVLDEADRMLEGQYNDQLKPIFESIS----EKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd18052  180 RLLDFIGR-----GKIsLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLKED 254

                 ...
gi 351065690 292 YFF 294
Cdd:cd18052  255 YLF 257
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
109-280 2.30e-41

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: 147.74  E-value: 2.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 109 IKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKL--SVDPYGIYALILTPTRELAFQIAEQFTALGKPITL 186
Cdd:cd17957   10 YREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYRELLKLSKGTGL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 187 KCSVIVGG-RSLIHQARELSERPHVVVATPGRLADLIESDPdtiaKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISE 265
Cdd:cd17957   90 RIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP----IDLSSVEYLVLDEADKLFEPGFREQTDEILAACTN 165
                        170
                 ....*....|....*.
gi 351065690 266 KR-QTLLLSATITNNI 280
Cdd:cd17957  166 PNlQRSLFSATIPSEV 181
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
113-292 6.16e-41

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: 146.67  E-value: 6.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 113 TPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIV 192
Cdd:cd17940   23 SPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 193 GGRSLIHQARELSERPHVVVATPGRLADLIESDpdtIAKVfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLL 272
Cdd:cd17940  103 GGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKG---VADL-SHCKTLVLDEADKLLSQDFQPIIEKILNFLPKERQILLF 178
                        170       180
                 ....*....|....*....|
gi 351065690 273 SATITNNINMLHRVSTRKPY 292
Cdd:cd17940  179 SATFPLTVKNFMDRHMHNPY 198
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
113-275 7.38e-41

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: 146.36  E-value: 7.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 113 TPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY-----GIYALILTPTRELAFQIAEQFTALGKPITLK 187
Cdd:cd17966   14 TAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPlergdGPIVLVLAPTRELAQQIQQEANKFGGSSRLR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 188 CSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIakvfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKR 267
Cdd:cd17966   94 NTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNL----RRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 169

                 ....*...
gi 351065690 268 QTLLLSAT 275
Cdd:cd17966  170 QTLMWSAT 177
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
91-290 2.19e-40

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: 145.54  E-value: 2.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  91 FSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSvdpygiyALILTPTRELA 170
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-------ALILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 FQIAEQFTALGKPI---TLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKVfkkiQFFVLDEADRM 247
Cdd:cd17938   74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSV----RFFVLDEADRL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 351065690 248 LEGQYNDQLKPIFESI-----SEKR-QTLLLSATitnninmLHRVSTRK 290
Cdd:cd17938  150 LSQGNLETINRIYNRIpkitsDGKRlQVIVCSAT-------LHSFEVKK 191
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
116-291 8.05e-40

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: 143.62  E-value: 8.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 116 QAACIPkILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGR 195
Cdd:cd17939   25 QRAIVP-IIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 196 SLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSAT 275
Cdd:cd17939  104 SVREDRRKLQYGPHIVVGTPGRVFDMLQRR----SLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVVLFSAT 179
                        170
                 ....*....|....*.
gi 351065690 276 ITNNINMLHRVSTRKP 291
Cdd:cd17939  180 MPHEVLEVTKKFMRDP 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
100-285 9.20e-40

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: 143.32  E-value: 9.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY-----GIYALILTPTRELAFQIA 174
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElekgeGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 175 EQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYND 254
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKK----ATNLQRVTYLVLDEADRMFDMGFEY 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 351065690 255 QLKPIFESISEKRQTLLLSATITNNINMLHR 285
Cdd:cd17952  157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLAR 187
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
74-285 2.08e-37

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: 138.63  E-value: 2.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  74 DTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPIL----- 148
Cdd:cd18051   15 NCPPHIE---------TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiye 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 149 ---QKLSVDPYGIY--------ALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGR 217
Cdd:cd18051   86 qgpGESLPSESGYYgrrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGR 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351065690 218 LADLIESdpdtiAKV-FKKIQFFVLDEADRMLEGQYNDQLKPIFESI----SEKRQTLLLSATITNNINMLHR 285
Cdd:cd18051  166 LVDMLER-----GKIgLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLAR 233
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
116-280 6.90e-37

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 135.65  E-value: 6.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 116 QAACIPkILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGR 195
Cdd:cd18046   27 QRAIMP-CIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 196 SLIHQARELSERPHVVVATPGRLADLIES---DPDtiakvfkKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLL 272
Cdd:cd18046  106 SVRDDAQKLQAGPHIVVGTPGRVFDMINRrylRTD-------YIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVLL 178

                 ....*...
gi 351065690 273 SATITNNI 280
Cdd:cd18046  179 SATMPNDV 186
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
100-291 1.12e-36

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: 135.16  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIP-ILQKLSVD---PY----GIYALILTPTRELA- 170
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEkklPFikgeGPYGLIVCPSRELAr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 171 --FQIAEQFTAL----GKPiTLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESdpdtiakvfKKI-----QFF 239
Cdd:cd17951   81 qtHEVIEYYCKAlqegGYP-QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNK---------KKInldicRYL 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 351065690 240 VLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINMLHRVSTRKP 291
Cdd:cd17951  151 CLDEADRMIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
115-280 2.96e-35

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 131.31  E-value: 2.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 115 VQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPI-TLKCSVIVG 193
Cdd:cd17950   28 VQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMpNVKTAVFFG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 194 GRSlIHQAREL--SERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEG-QYNDQLKPIFESISEKRQTL 270
Cdd:cd17950  108 GVP-IKKDIEVlkNKCPHIVVGTPGRILALVREK----KLKLSHVKHFVLDECDKMLEQlDMRRDVQEIFRATPHDKQVM 182
                        170
                 ....*....|
gi 351065690 271 LLSATITNNI 280
Cdd:cd17950  183 MFSATLSKEI 192
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
113-283 8.92e-34

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: 126.89  E-value: 8.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 113 TPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPI-TLKCSVI 191
Cdd:cd17962   14 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPMKTALL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 192 VGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKvfkkIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLL 271
Cdd:cd17962   94 VGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDN----IKIVVVDEADTMLKMGFQQQVLDILENISHDHQTIL 169
                        170
                 ....*....|..
gi 351065690 272 LSATITNNINML 283
Cdd:cd17962  170 VSATIPRGIEQL 181
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
76-283 1.22e-32

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: 126.28  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  76 PKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDP 155
Cdd:cd18050   58 PKPVF---------AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 156 Y-----GIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIa 230
Cdd:cd18050  129 YlergdGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL- 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 351065690 231 kvfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINML 283
Cdd:cd18050  208 ---RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQL 257
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
74-283 4.94e-32

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: 123.58  E-value: 4.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  74 DTPKPIQisednmttkKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSV 153
Cdd:cd18049   18 NCPKPVL---------NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 154 DPY-----GIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDT 228
Cdd:cd18049   89 QPFlergdGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTN 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 351065690 229 IakvfKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATITNNINML 283
Cdd:cd18049  169 L----RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQL 219
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
100-275 1.96e-30

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: 117.95  E-value: 1.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY------GIYALILTPTRELAFQI 173
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIpreqrnGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 174 AEQFTALgKPITLKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYN 253
Cdd:cd17958   81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNN----VINLKSITYLVLDEADRMLDMGFE 155
                        170       180
                 ....*....|....*....|..
gi 351065690 254 DQLKPIFESISEKRQTLLLSAT 275
Cdd:cd17958  156 PQIRKILLDIRPDRQTIMTSAT 177
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
327-432 1.69e-29

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: 111.92  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  327 VVKNYSEKNPKSSVMIFAQTCRECQAlAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHV 406
Cdd:pfam00271   5 ALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDV 83
                          90       100
                  ....*....|....*....|....*.
gi 351065690  407 DLVVNHNVPQCPKTYIHRVGRSARAG 432
Cdd:pfam00271  84 DLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
100-286 2.38e-28

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: 112.85  E-value: 2.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 100 ITQQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY-------GIYALILTPTRELAFQ 172
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLlaegpfnAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 173 IAEQFTALGKPITLKCSVIVGGRS-----LIHQarelsERPHVVVATPGRLADLIESDpdtIAKVfKKIQFFVLDEADRM 247
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTkrqirNPHF-----EEVDILVATPGALSKLLTSR---IYSL-EQLRHLVLDEADTL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 351065690 248 LEGQYNDQL-------------KPIFESISEKRQTLLLSATITNNIN-MLHRV 286
Cdd:cd17948  152 LDDSFNEKLshflrrfplasrrSENTDGLDPGTQLVLVSATMPSGVGeVLSKV 204
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
110-280 1.69e-27

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: 109.86  E-value: 1.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 110 KTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCS 189
Cdd:cd18045   20 EKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYMNVQCH 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 190 VIVGGRSLIHQARELSERPHVVVATPGRLADLIESDpdtiAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQT 269
Cdd:cd18045  100 ACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRR----SLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQV 175
                        170
                 ....*....|.
gi 351065690 270 LLLSATITNNI 280
Cdd:cd18045  176 VLVSATLPQDI 186
HELICc smart00490
helicase superfamily c-terminal domain;
351-432 3.23e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 99.21  E-value: 3.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690   351 QALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSAR 430
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 351065690   431 AG 432
Cdd:smart00490  81 AG 82
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
102-275 3.69e-25

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: 103.00  E-value: 3.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 102 QQLQTMQIKTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGI------YALILTPTRELAFQIAE 175
Cdd:cd17944    3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 176 QFTALGKPITLKCsvIVGGRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKVfkkiQFFVLDEADRMLEGQYNDQ 255
Cdd:cd17944   83 DFKDITRKLSVAC--FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKL----KHVVLDEVDQMLDMGFAEQ 156
                        170       180
                 ....*....|....*....|....*
gi 351065690 256 LKPI----FESISEKR-QTLLLSAT 275
Cdd:cd17944  157 VEEIlsvsYKKDSEDNpQTLLFSAT 181
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
104-275 9.01e-25

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: 101.88  E-value: 9.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 104 LQTMQIKTATPVQAACIPKILEG--SDILGCARTGTGKTLAFAIPILQKlsVDPYGIY--ALILTPTRELAFQIAEQFTA 179
Cdd:cd17963    9 LYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSR--VDPTLKSpqALCLAPTRELARQIGEVVEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 180 LGKPITLKCSVIVGGRSlIHQARELSErpHVVVATPGRLADLIES---DPdtiakvfKKIQFFVLDEADRMLEGQ-YNDQ 255
Cdd:cd17963   87 MGKFTGVKVALAVPGND-VPRGKKITA--QIVIGTPGTVLDWLKKrqlDL-------KKIKILVLDEADVMLDTQgHGDQ 156
                        170       180
                 ....*....|....*....|
gi 351065690 256 LKPIFESISEKRQTLLLSAT 275
Cdd:cd17963  157 SIRIKRMLPRNCQILLFSAT 176
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
135-560 2.11e-23

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 103.95  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 135 TGTGKTLAFAIPILQKLSVDPygiyALILTPTRELAFQIAEQFTALgkpitLKCSVIVGGRSlihqarelSERPHVVVAT 214
Cdd:COG1061  109 TGTGKTVLALALAAELLRGKR----VLVLVPRRELLEQWAEELRRF-----LGDPLAGGGKK--------DSDAPITVAT 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 215 PGRLA-----DLIESDPDTIakvfkkiqffVLDEADRMLEGQYNDqlkpIFESISEKRqTLLLSAT----------ITNN 279
Cdd:COG1061  172 YQSLArrahlDELGDRFGLV----------IIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfrsdgreilLFLF 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 280 INMLHRVSTR--------KPYFF-------EDKGKDDESTVDRLEQKYVVCPVAVKDaylvyVVKNYSEKNPKSS-VMIF 343
Cdd:COG1061  237 DGIVYEYSLKeaiedgylAPPEYygirvdlTDERAEYDALSERLREALAADAERKDK-----ILRELLREHPDDRkTLVF 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 344 AQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIH 423
Cdd:COG1061  312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 424 RVGR---SARAGRFGSALSFVTQyDVELLQAveqvIGKKLDELKVSPKHVTKYVTQVLVAKKEAELKLENQKFGEKKEIN 500
Cdd:COG1061  392 RLGRglrPAPGKEDALVYDFVGN-DVPVLEE----LAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELL 466
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 501 RRKELLmsgmDEDEADRHLEEMRTRRMTNSKRKLEKISGQLDKRDRFQKKLAAKKVKKEE 560
Cdd:COG1061  467 EELELL----EDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAK 522
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
105-276 2.97e-19

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: 87.43  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 105 QTMQIKtATPVQAACIPKILEGSDI----------------LGCARTGTGKTLAFAIPILQKLS---------------- 152
Cdd:cd17965   25 TDEEIK-PSPIQTLAIKKLLKTLMRkvtkqtsneepklevfLLAAETGSGKTLAYLAPLLDYLKrqeqepfeeaeeeyes 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 153 -VDPYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVIVGGRSLIHQAREL--SERPHVVVATPGRLADLIESDPdti 229
Cdd:cd17965  104 aKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPGKLASLAKSRP--- 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 351065690 230 aKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISEKRQTLLLSATI 276
Cdd:cd17965  181 -KILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
126-275 3.29e-17

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 78.60  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 126 GSDILGCARTGTGKTLAFAIPILQKLsvDPYGIYALILTPTRELAFQIAEQFTALGKPiTLKCSVIVGGRSLIHQARELS 205
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLL--LKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351065690 206 ERPHVVVATPGRLADLIESDpdtIAKVFKKIQFFVLDEADRMLegqYNDQLKPIFESISEKR-----QTLLLSAT 275
Cdd:cd00046   78 GDADIIIATPDMLLNLLLRE---DRLFLKDLKLIIVDEAHALL---IDSRGALILDLAVRKAglknaQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
89-280 6.58e-12

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: 65.13  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  89 KKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEG--SDILGCARTGTGKTLAFAIPILQKlsVDPYGIYA--LILT 164
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYPqcLCLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 165 PTRELAFQIAEQFTALGK--PITLKCSVIVGGRslihQARELSERPHVVVATPGRLAD----LIESDPdtiakvfKKIQF 238
Cdd:cd18047   79 PTYELALQTGKVIEQMGKfyPELKLAYAVRGNK----LERGQKISEQIVIGTPGTVLDwcskLKFIDP-------KKIKV 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 351065690 239 FVLDEADRMLEGQ-YNDQLKPIFESISEKRQTLLLSATITNNI 280
Cdd:cd18047  148 FVLDEADVMIATQgHQDQSIRIQRMLPRNCQMLLFSATFEDSV 190
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
320-432 9.04e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 67.83  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 320 KDAYLVYVVKNYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQ--------IPQKQRLAALSAFRSKTLQVI 391
Cdd:COG1111  336 KLSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVL 415
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 351065690 392 ICTDVASRGLDIPHVDLVVNH-NVPQcPKTYIHRVGRSARAG 432
Cdd:COG1111  416 VATSVAEEGLDIPEVDLVIFYePVPS-EIRSIQRKGRTGRKR 456
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
87-280 1.16e-11

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: 64.66  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  87 TTKKFSQLGVCSWITQQLQTMQIKTATPVQAACIPKILEG--SDILGCARTGTGKTLAFAIPILQKLSVDPYGIYALILT 164
Cdd:cd18048   16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 165 PTRELAFQIAEQFTALGKpitlkcsvIVGGRSLIHQARelSERP--------HVVVATPGRLAD------LIEsdpdtia 230
Cdd:cd18048   96 PTFELALQTGKVVEEMGK--------FCVGIQVIYAIR--GNRPgkgtdieaQIVIGTPGTVLDwcfklrLID------- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 351065690 231 kvFKKIQFFVLDEADRMLEGQ-YNDQLKPIFESISEKRQTLLLSATITNNI 280
Cdd:cd18048  159 --VTNISVFVLDEADVMINVQgHSDHSVRVKRSMPKECQMLLFSATFEDSV 207
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
113-278 2.06e-11

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 63.05  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 113 TPVQAACIPKI-LEGSDILGCARTGTGKTLAFAIPILQKLSVdpYGIYALILTPTRELAFQIAEQFTALGKPITLKCSVI 191
Cdd:cd17921    3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALAT--SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 192 VGGRSLihqARELSERPHVVVATPGRLADLIESDPDTIakvFKKIQFFVLDEADRMLEGQYNDQLKPIFESI---SEKRQ 268
Cdd:cd17921   81 TGDPSV---NKLLLAEADILVATPEKLDLLLRNGGERL---IQDVRLVVVDEAHLIGDGERGVVLELLLSRLlriNKNAR 154
                        170
                 ....*....|
gi 351065690 269 TLLLSATITN 278
Cdd:cd17921  155 FVGLSATLPN 164
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
116-433 5.15e-11

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 65.63  E-value: 5.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 116 QAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPyGIYALILTPTRELAF-QIAEqFTALGKPITLKCSV-IVG 193
Cdd:COG1205   61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALARdQLRR-LRELAEALGLGVRVaTYD 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 194 GRSLIHQARELSERPHVVVATPgrlaDLIES----DPDTIAKVFKKIQFFVLDEA---------------DRMLE--GQY 252
Cdd:COG1205  139 GDTPPEERRWIREHPDIVLTNP----DMLHYgllpHHTRWARFFRNLRYVVIDEAhtyrgvfgshvanvlRRLRRicRHY 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 253 NDqlKPIFesisekrqtLLLSATITNNINMLHRVStrkpyffedkGKD----DESTVDRLEQKYV------VCPVAVKDA 322
Cdd:COG1205  215 GS--DPQF---------ILASATIGNPAEHAERLT----------GRPvtvvDEDGSPRGERTFVlwnpplVDDGIRRSA 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 323 YL--VYVVKNYSEKNPKssVMIFAQT----------CREcqalAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQV 390
Cdd:COG1205  274 LAeaARLLADLVREGLR--TLVFTRSrrgaellaryARR----ALREPDLADRVAAYRAGYLPEERREIERGLRSGELLG 347
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 351065690 391 IICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGR 433
Cdd:COG1205  348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQ 390
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
116-278 3.34e-10

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 59.52  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 116 QAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPyGIYALILTPTRELAFQIAEQFTALGKPITLK--CSVIVG 193
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-GSRALYLYPTKALAQDQLRSLRELLEQLGLGirVATYDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 194 GRSLIHQARELSERPHVVVATPGRLADLIESDPDTIAKVFKKIQFFVLDEAdRMLEGQYNDQ-------LKPIFESISEK 266
Cdd:cd17923   84 DTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEA-HTYRGVFGSHvalllrrLRRLCRRYGAD 162
                        170
                 ....*....|..
gi 351065690 267 RQTLLLSATITN 278
Cdd:cd17923  163 PQFILTSATIGN 174
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
324-431 8.21e-10

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: 57.22  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 324 LVYVVKNYSEKNPKSSVMIFAQTCRECQALAYMFE---------------GLGFRVGSLHSQIPQKQRLAALSAFRSKTL 388
Cdd:cd18802   12 LIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKehpstlafircgfliGRGNSSQRKRSLMTQRKQKETLDKFRDGEL 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 351065690 389 QVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRsARA 431
Cdd:cd18802   92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
114-278 5.03e-09

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 55.80  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 114 PVQAACIPK-ILEGSDILGCARTGTGKTLAFAIPILQKLSVDPYGIYaliLTPTRELAFQIAEQFTALgKPITLKCSVIV 192
Cdd:cd18028    4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALY---LVPLRALASEKYEEFKKL-EEIGLKVGIST 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 193 GgrSLIHQARELSERpHVVVATPGRLADLIESDPDTIakvfKKIQFFVLDE---ADRMLEGqyndqlkPIFESISEK--- 266
Cdd:cd18028   80 G--DYDEDDEWLGDY-DIIVATYEKFDSLLRHSPSWL----RDVGVVVVDEihlISDEERG-------PTLESIVARlrr 145
                        170
                 ....*....|....*.
gi 351065690 267 ----RQTLLLSATITN 278
Cdd:cd18028  146 lnpnTQIIGLSATIGN 161
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
126-278 8.09e-09

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 54.90  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 126 GSDILGCARTGTGKTLAFAIPILQKLSVDPY-GIYALILTPTRELafqIAEQFTALGKPIT-LKCSVIVGGRsliH---- 199
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEkGVQVLYISPLKAL---INDQERRLEEPLDeIDLEIPVAVR---Hgdts 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 200 ---QARELSERPHVVVATPGRLADLIESDPdtIAKVFKKIQFFVLDEADRMLEGQYNDQLKPIFESISE----KRQTLLL 272
Cdd:cd17922   75 qseKAKQLKNPPGILITTPESLELLLVNKK--LRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKltgrPLRRIGL 152

                 ....*.
gi 351065690 273 SATITN 278
Cdd:cd17922  153 SATLGN 158
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
388-436 2.06e-07

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 48.47  E-value: 2.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 351065690 388 LQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGS 436
Cdd:cd18785   23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEG 71
PRK13767 PRK13767
ATP-dependent helicase; Provisional
110-428 3.79e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 52.97  E-value: 3.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 110 KTATPVQAACIPKILEGSDILGCARTGTGKTLAFAIPILQKLSVDPY------GIYALILTPTRELA-----------FQ 172
Cdd:PRK13767  31 GTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGRegeledKVYCLYVSPLRALNndihrnleeplTE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 173 IAEQFTALGKPIT-LKCSVIVGGRSLIHQARELSERPHVVVATPGRLADLIESdPDtiakvFKK----IQFFVLDEADRM 247
Cdd:PRK13767 111 IREIAKERGEELPeIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNS-PK-----FREklrtVKWVIVDEIHSL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 248 LEGQYNDQLkpifeSISEKRQTLL---------LSATitnnINMLHRVSTrkpyF---FEDKGKD-DESTVD-RLEQKY- 312
Cdd:PRK13767 185 AENKRGVHL-----SLSLERLEELaggefvrigLSAT----IEPLEEVAK----FlvgYEDDGEPrDCEIVDaRFVKPFd 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 313 --VVCPvaVKDayLVY------------VVKNYSEKNpkSSVMIFAQTCRECQALAY----MFEGLG--FRVGSLHSQIP 372
Cdd:PRK13767 252 ikVISP--VDD--LIHtpaeeisealyeTLHELIKEH--RTTLIFTNTRSGAERVLYnlrkRFPEEYdeDNIGAHHSSLS 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 351065690 373 QKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRS 428
Cdd:PRK13767 326 REVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRA 381
PRK13766 PRK13766
Hef nuclease; Provisional
324-433 1.03e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.80  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 324 LVYVVKNYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQ--------IPQKQRLAALSAFRSKTLQVIICTD 395
Cdd:PRK13766 352 LREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTS 431
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 351065690 396 VASRGLDIPHVDLVVNHN-VPQCPKTyIHRVGRSAR--AGR 433
Cdd:PRK13766 432 VAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGRqeEGR 471
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
373-430 1.56e-06

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: 47.74  E-value: 1.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 351065690 373 QKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSAR 430
Cdd:cd18801   76 QKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
135-275 1.64e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 47.69  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 135 TGTGKTLaFAIPILQKLSVDPygiyALILTPTRELAFQIAEQFTALGKPITLKcsvIVGGRSLIHQARELserphVVVAT 214
Cdd:cd17926   27 TGSGKTL-TALALIAYLKELR----TLIVVPTDALLDQWKERFEDFLGDSSIG---LIGGGKKKDFDDAN-----VVVAT 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351065690 215 PgrlaDLIESDPDTIAKVFKKIQFFVLDEADRmLEGqynDQLKPIFESISEKRQtLLLSAT 275
Cdd:cd17926   94 Y----QSLSNLAEEEKDLFDQFGLLIVDEAHH-LPA---KTFSEILKELNAKYR-LGLTAT 145
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
362-432 2.20e-06

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 47.65  E-value: 2.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351065690 362 FRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIH----RVGRSARAG 432
Cdd:cd18792   61 ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHqlrgRVGRGKHQS 135
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
315-450 2.80e-06

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 50.14  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 315 CPVAVKDAYLVYVVKnyseKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICT 394
Cdd:COG0514  212 KPPDDKLAQLLDFLK----EHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT 287
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 351065690 395 dVA-SRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSFVTQYDVELLQ 450
Cdd:COG0514  288 -IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
322-429 2.92e-06

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 47.34  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 322 AYLVYVVKNYSEK-NPKSSVmifaqtcRECQALAYMFEGlGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRG 400
Cdd:cd18811   29 AYVIYPLIEESEKlDLKAAV-------AMYEYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVG 100
                         90       100       110
                 ....*....|....*....|....*....|...
gi 351065690 401 LDIPHVDLVVNHNVPQCPKTYIH----RVGRSA 429
Cdd:cd18811  101 VDVPNATVMVIEDAERFGLSQLHqlrgRVGRGD 133
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
313-430 1.80e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 44.95  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 313 VVCPVAVKDAYLVYVVKNYSEKN------PKSSVMIFAQTCRECQALAYMF------EGLGFRVGSLHSQIPQKQRLAAL 380
Cdd:cd18796    8 VILPVAPEIFPWAGESGADAYAEviflleRHKSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVE 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 351065690 381 SAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSAR 430
Cdd:cd18796   88 AALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
339-410 2.12e-05

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 43.70  E-value: 2.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351065690 339 SVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRL---AALSAFRSKTLQVIICTDVASRGLDIPHVDLVV 410
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
329-435 4.70e-05

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: 43.35  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 329 KNYSEKNPKSSVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDL 408
Cdd:cd18794   22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101
                         90       100
                 ....*....|....*....|....*..
gi 351065690 409 VVNHNVPQCPKTYIHRVGrsaRAGRFG 435
Cdd:cd18794  102 VIHYSLPKSMESYYQESG---RAGRDG 125
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
111-277 7.13e-05

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: 43.56  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 111 TATPVQAACIPKIL------EGSDILGCARTGTGKTLAFAIPILQKLSVdpyGIYALILTPTRELAFQIAEQFTALGKPI 184
Cdd:cd17918   15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAALLAYKN---GKQVAILVPTEILAHQHYEEARKFLPFI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 185 tlKCSVIVGGRslihQARELSErPHVVVATPGrladLIESDpdtiaKVFKKIQFFVLDEADRMLEGQYndqlkpifESIS 264
Cdd:cd17918   92 --NVELVTGGT----KAQILSG-ISLLVGTHA----LLHLD-----VKFKNLDLVIVDEQHRFGVAQR--------EALY 147
                        170
                 ....*....|...
gi 351065690 265 EKRQTLLLSATIT 277
Cdd:cd17918  148 NLGATHFLEATAT 160
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
128-296 1.15e-04

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 43.57  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 128 DILGCARTGTGKTLAFAIPILQKLS--VDPYG---------IYaliLTPTRELAFQIAEQFTALGKPITLKCSVIVGGRS 196
Cdd:cd18020   19 NMLICAPTGAGKTNIAMLTILHEIRqhVNQGGvikkddfkiVY---IAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 197 LihQARELSErPHVVVATPGRLaDLIESDPDTIAKVFKKIQFFVLDEAdRMLegqyNDQLKPIFESI-------SEKRQT 269
Cdd:cd18020   96 L--TKKEIAE-TQIIVTTPEKW-DVVTRKSSGDVALSQLVRLLIIDEV-HLL----HDDRGPVIESLvartlrqVESTQS 166
                        170       180       190
                 ....*....|....*....|....*....|...
gi 351065690 270 LL----LSATITNNINMLH--RVSTRKPYFFED 296
Cdd:cd18020  167 MIrivgLSATLPNYLDVADflRVNPYKGLFFFD 199
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
127-244 2.41e-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: 42.64  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 127 SDILGCARTGTGKTLaFAIPILQKLSVDPYGIY-----ALILTPTRELAFQiaeQFTALGKPITLKCSVIVGGRSLIHQA 201
Cdd:cd18034   17 RNTIVVLPTGSGKTL-IAVMLIKEMGELNRKEKnpkkrAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKWT 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 351065690 202 R----ELSERPHVVVATPGRLADLIESdpdtiAKV-FKKIQFFVLDEA 244
Cdd:cd18034   93 KerwkEELEKYDVLVMTAQILLDALRH-----GFLsLSDINLLIFDEC 135
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
363-432 6.52e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.40  E-value: 6.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351065690 363 RVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIH----RVGRSARAG 432
Cdd:cd18810   53 RIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYqlrgRVGRSKERA 126
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
115-243 8.88e-04

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.80  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 115 VQAACIPKILEgSDI--LGCARTGTGKTLAFAIPILQKL----SVDPYGIYALILTPTRELAFQIAEQFTALGKPITLKC 188
Cdd:cd18023    5 IQSEVFPDLLY-SDKnfVVSAPTGSGKTVLFELAILRLLkernPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSC 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 351065690 189 SVIVGGRSlIHQARELSErPHVVVATPGRLaDLIESDPDTIAKVFKKIQFFVLDE 243
Cdd:cd18023   84 AELTGDTE-MDDTFEIQD-ADIILTTPEKW-DSMTRRWRDNGNLVQLVALVLIDE 135
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
351-464 8.98e-04

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


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 40.37  E-value: 8.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 351 QALAYMFEGLGFRVGSLHSQIPQKqrlaaLSAFRSKTLQVIIctDVAS------RGLDIPH-VDLVVNHNVPqcPKTYIH 423
Cdd:cd18798   41 EELKEFLERHGIKAELALSSTEKN-----LEKFEEGEIDVLI--GVASyygvlvRGIDLPErIKYAIFYGVP--VTTYIQ 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 351065690 424 RVGRSAR--AGRFGSALSFVTQYDVELLQAVEQVIGKKLDELK 464
Cdd:cd18798  112 ASGRTSRlyAGGLTKGLSVVLVDDPELFEALKKRLKLILDEFI 154
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
361-445 1.06e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 42.01  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 361 GFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVDLVVNHNVPQCPKTYIHRVGRSARAGRFGSALSF 440
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339

                 ....*
gi 351065690 441 vtqYD 445
Cdd:PRK11057 340 ---YD 341
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
340-411 2.19e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 40.98  E-value: 2.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351065690 340 VMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSK--TLQVIICTDVASRGLDIPHVDLVVN 411
Cdd:COG0553  552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIH 625
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
114-244 8.67e-03

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 37.90  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690 114 PVQAACIPKILEGSDILGCARTGTGKTLAFAIP--ILQKLsvdpygiyALILTPTRELAFQIAEQFTALGKPitlkcSVI 191
Cdd:cd17920   15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPLISLMQDQVDRLQQLGIR-----AAA 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351065690 192 VGGRSLIHQARELSER-----PHVVVATPGRLA-----DLIESDPdtiakVFKKIQFFVLDEA 244
Cdd:cd17920   82 LNSTLSPEEKREVLLRikngqYKLLYVTPERLLspdflELLQRLP-----ERKRLALIVVDEA 139
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
328-505 9.77e-03

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: 38.82  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  328 VKNYSEKNPKssVMIFAQTCRECQALAYMFEGLGFRVGSLHSQIPQKQRLAALSAFRSKTLQVIICTDVASRGLDIPHVD 407
Cdd:TIGR00631 435 IRQRVARNER--VLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065690  408 LV--VNHNVPQCPKTY---IHRVGRSARAGRfGSALSF---VTQYDVELLQAVEQVIGKKLD---ELKVSPKHVTKYVTQ 476
Cdd:TIGR00631 513 LVaiLDADKEGFLRSErslIQTIGRAARNVN-GKVIMYadkITDSMQKAIEETERRRKIQMAyneEHGITPQTIRKPIRD 591
                         170       180       190
                  ....*....|....*....|....*....|
gi 351065690  477 VLVAK-KEAELKLENQKFGEKKEINRRKEL 505
Cdd:TIGR00631 592 ILDIElKEKEDAAKKKKKGEDLSDLSKKEL 621
 
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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