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Conserved domains on  [gi|490869766|ref|WP_004731781|]
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MULTISPECIES: ATP-dependent RNA helicase DbpA [Vibrio]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 11485501)

ATP-dependent RNA helicase DbpA is a DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-459 0e+00

ATP-dependent RNA helicase DbpA; Provisional


:

Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 898.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   1 MSTSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  81 TRELADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 161 EMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHSSIQQHFYKVEGTEaRDDALELMLLH 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE-RLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 241 HQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFEL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 321 SRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLPAKPIA--KPYYSNMVTIQIDGGKKAKLR 398
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLsgVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 399 AGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARILK 459
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-459 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 898.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   1 MSTSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  81 TRELADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 161 EMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHSSIQQHFYKVEGTEaRDDALELMLLH 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE-RLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 241 HQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFEL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 321 SRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLPAKPIA--KPYYSNMVTIQIDGGKKAKLR 398
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLsgVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 399 AGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARILK 459
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
3-372 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 549.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   3 TSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKR-FRVQSLVLCPT 81
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  82 RELADQVAKEIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLE 161
Cdd:COG0513   81 RELALQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 162 MGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTH-DHSSIQQHFYKVEGTEaRDDALELMLLH 240
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENaTAETIEQRYYLVDKRD-KLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 241 HQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFEL 320
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490869766 321 SRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLP 372
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 3.31e-97

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: 290.11  E-value: 3.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL----RVKRFRVQSLVLCPTRELADQVAK 90
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpepKKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  91 EIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDA 170
Cdd:cd00268   81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490869766 171 VIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-195 5.89e-60

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: 193.61  E-value: 5.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   28 TPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQVAKEIRTLARGIhNIKVLTL 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  108 CGGMPMGPQIGSLeHGAHILVGTPGRILDHLeRERIDLSELNTLVLDEADRMLEMGFQDALDAVIEAAPKDRQTLLFSAT 187
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 490869766  188 FPKQIKSV 195
Cdd:pfam00270 158 LPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
19-211 8.01e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 171.14  E-value: 8.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766    19 LDSLGYTEMTPIQALSLPTILDG-KDVIGQGKTGSGKTAAFGLGVLQNLRvKRFRVQSLVLCPTRELADQVAKEIRTLAr 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766    98 GIHNIKVLTLCGGMPMGPQIGSLEHG-AHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVIEAAP 176
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 490869766   177 KDRQTLLFSATFPKQIKSVADRIMNNPEMVKVEST 211
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
151-389 3.80e-05

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 45.52  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  151 LVLDEADRMLE---MGFQDALDAvieAAPKDRQTLLFSATFPKQIKSVADRImnnpEMVKVESTHDHSSIQQHF-YKVEG 226
Cdd:TIGR01587 128 LIFDEVHFYDEytlALILAVLEV---LKDNDVPILLMSATLPKFLKEYAEKI----GYVEFNEPLDLKEERRFEnHRFIL 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  227 TEARDDALELML-----LHHQPESAVVFCNTKKEVQNVNDELSHRG--FSVIELHGDMEQRERDQALVQ-----FSNKTI 294
Cdd:TIGR01587 201 IESDKVGEISSLerlleFIKKGGSIAIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAKKEAEllremKKSNEK 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  295 SILVATDVAARGLDVDnldavFNF---ELSrDPEVHVHRIGRTGRAGSKgvaisffsekemhrvaqIDEYMDMPIEPSQL 371
Cdd:TIGR01587 281 FVIVATQVIEASLDIS-----ADVmitELA-PIDSLIQRLGRLHRYGRK-----------------IGENFEVYIITIAP 337
                         250
                  ....*....|....*...
gi 490869766  372 PAKPIAKPYYSNMVTIQI 389
Cdd:TIGR01587 338 EGKLFPYPYELVERTIQK 355
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-459 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 898.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   1 MSTSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCP 80
Cdd:PRK11776   1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  81 TRELADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRML 160
Cdd:PRK11776  81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 161 EMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHSSIQQHFYKVEGTEaRDDALELMLLH 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE-RLPALQRLLLH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 241 HQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFEL 320
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 321 SRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLPAKPIA--KPYYSNMVTIQIDGGKKAKLR 398
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLsgVPLLPEMVTLCIDGGKKDKLR 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 399 AGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARILK 459
Cdd:PRK11776 400 PGDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
3-372 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 549.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   3 TSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKR-FRVQSLVLCPT 81
Cdd:COG0513    1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  82 RELADQVAKEIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLE 161
Cdd:COG0513   81 RELALQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 162 MGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTH-DHSSIQQHFYKVEGTEaRDDALELMLLH 240
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENaTAETIEQRYYLVDKRD-KLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 241 HQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFEL 320
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490869766 321 SRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLP 372
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELP 370
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
6-368 3.89e-103

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 314.19  E-value: 3.89e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL----RVKRFRVQSLVLCPT 81
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGPPRILILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  82 RELADQVAKEIRTLARGIHnIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLE 161
Cdd:PRK11192  83 RELAMQVADQARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 162 MGF-QDALDAVIEAAPKdRQTLLFSATFP-KQIKSVADRIMNNPEMVKVE-STHDHSSIQQHFYKVEGTEARDDALELML 238
Cdd:PRK11192 162 MGFaQDIETIAAETRWR-KQTLLFSATLEgDAVQDFAERLLNDPVEVEAEpSRRERKKIHQWYYRADDLEHKTALLCHLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 239 LHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNF 318
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 490869766 319 ELSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEP 368
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
6-372 1.48e-99

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 311.01  E-value: 1.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQ 165
Cdd:PRK11634  88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 166 DALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVEST-HDHSSIQQHFYKVEGTEaRDDALELMLLHHQPE 244
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvTTRPDISQSYWTVWGMR-KNEALVRFLEAEDFD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 245 SAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDP 324
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 490869766 325 EVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLP 372
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELP 374
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
15-207 3.31e-97

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: 290.11  E-value: 3.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL----RVKRFRVQSLVLCPTRELADQVAK 90
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpepKKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  91 EIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDA 170
Cdd:cd00268   81 VARKLGKG-TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490869766 171 VIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
3-373 5.74e-91

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 284.11  E-value: 5.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   3 TSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFR--VQS 75
Cdd:PRK01297  86 KTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMgePRA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  76 LVLCPTRELADQVAKEIRTLARgIHNIKVLTLCGGMPMGPQIGSLE-HGAHILVGTPGRILDHLERERIDLSELNTLVLD 154
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 155 EADRMLEMGFQDALDAVIEAAPK--DRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHS-SIQQHFYKVEGTeard 231
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASdTVEQHVYAVAGS---- 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 232 DALELM--LLHHQP-ESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLD 308
Cdd:PRK01297 321 DKYKLLynLVTQNPwERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490869766 309 VDNLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQLPA 373
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPA 465
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
1-370 1.02e-86

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 271.46  E-value: 1.02e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   1 MSTSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVK-----RFRVQ- 74
Cdd:PRK04837   5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHpapedRKVNQp 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  75 -SLVLCPTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVL 153
Cdd:PRK04837  85 rALIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 154 DEADRMLEMGFQDALDAVIE--AAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHSS-IQQH-FYKvegteA 229
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRrmPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHrIKEElFYP-----S 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 230 RDD--ALELMLLHHQ-PESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARG 306
Cdd:PRK04837 239 NEEkmRLLQTLIEEEwPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490869766 307 LDVDNLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIEPSQ 370
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSK 382
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
6-376 5.88e-84

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 265.52  E-value: 5.88e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVK------RFRVQSLVLC 79
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  80 PTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDhLERER-IDLSELNTLVLDEADR 158
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNaVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 159 MLEMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDHSS-IQQHFYKVEGTEARdDALELM 237
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEqVTQHVHFVDKKRKR-ELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 238 LLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFN 317
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490869766 318 FELSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPI--------EP-SQLPAKPI 376
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIpriaipgyEPdPSIKAEPI 387
PTZ00110 PTZ00110
helicase; Provisional
5-348 1.18e-81

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 262.02  E-value: 1.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   5 KFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVK-RFRVQS----LVLC 79
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQpLLRYGDgpivLVLA 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  80 PTRELADQVAKEIRTLARgIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRM 159
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 160 LEMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVA-DRIMNNPEMVKVES---THDHSsIQQHFYKVEGTEARDDALE 235
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLArDLCKEEPVHVNVGSldlTACHN-IKQEVFVVEEHEKRGKLKM 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 236 LM-LLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDA 314
Cdd:PTZ00110 369 LLqRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
                        330       340       350
                 ....*....|....*....|....*....|....
gi 490869766 315 VFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFS 348
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLT 482
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
6-368 1.17e-75

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 247.17  E-value: 1.17e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRV-------QSLVL 78
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrkpedpRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  79 CPTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERI-DLSELNTLVLDEAD 157
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 158 RMLEMGFQDALDAVIEAAPK--DRQTLLFSATFPKQIKSVADRIMNNPEMVKVES-THDHSSIQQHFYkvegTEARDDAL 234
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETeTITAARVRQRIY----FPADEEKQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 235 ELML-LHHQPESA--VVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDN 311
Cdd:PRK04537 246 TLLLgLLSRSEGArtMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490869766 312 LDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMD--MPIEP 368
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEqkIPVEP 384
PTZ00424 PTZ00424
helicase 45; Provisional
6-367 3.91e-75

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 240.88  E-value: 3.91e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQ 165
Cdd:PTZ00424 110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 166 DALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTH-DHSSIQQHFYKVEGTEARDDALELMLLHHQPE 244
Cdd:PTZ00424 189 GQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDElTLEGIRQFYVAVEKEEWKFDTLCDLYETLTIT 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 245 SAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDP 324
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 490869766 325 EVHVHRIGRTGRAGSKGVAISFFSEKEMHRVAQIDEYMDMPIE 367
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIE 391
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
11-201 2.80e-65

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: 208.98  E-value: 2.80e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  11 LKPELLNTLDSLGYTEMTPIQALSLPTIL-DGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFRVQSLVLCPTREL 84
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  85 ADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEH-GAHILVGTPGRILDHLERER--IDLSELNTLVLDEADRMLE 161
Cdd:cd17964   81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGvaKAFTDLDYLVLDEADRLLD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490869766 162 MGFQDALDAVIEAAPK----DRQTLLFSATFPKQIKSVADRIMN 201
Cdd:cd17964  161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
6-203 3.56e-63

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: 203.22  E-value: 3.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLE---RERIDLSELNTLVLDEADRMLEM 162
Cdd:cd17955   81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490869766 163 GFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
6-209 1.14e-62

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: 201.78  E-value: 1.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERER-IDLSELNTLVLDEADRMLEMGF 164
Cdd:cd17954   82 QQISEQFEALGSSI-GLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDF 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490869766 165 QDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPemVKVE 209
Cdd:cd17954  161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP--VKIE 203
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
6-207 2.13e-60

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: 195.99  E-value: 2.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL--RVKRFRVQSLVLCPTRE 83
Cdd:cd17959    3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkaHSPTVGARALILSPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  84 LADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMG 163
Cdd:cd17959   83 LALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 490869766 164 FQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd17959  162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
6-202 3.35e-60

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: 196.17  E-value: 3.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL------RVKRFRV----QS 75
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppSVGRGRRkaypSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  76 LVLCPTRELADQVAKEIRTLARGIHnIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDE 155
Cdd:cd17967   82 LILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490869766 156 ADRMLEMGFQDALDAVIEAA---PKD-RQTLLFSATFPKQIKSVADRIMNN 202
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHPdmpPKGeRQTLMFSATFPREIQRLAADFLKN 211
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
28-195 5.89e-60

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: 193.61  E-value: 5.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   28 TPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQVAKEIRTLARGIhNIKVLTL 107
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  108 CGGMPMGPQIGSLeHGAHILVGTPGRILDHLeRERIDLSELNTLVLDEADRMLEMGFQDALDAVIEAAPKDRQTLLFSAT 187
Cdd:pfam00270  80 LGGDSRKEQLEKL-KGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*...
gi 490869766  188 FPKQIKSV 195
Cdd:pfam00270 158 LPRNLEDL 165
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
6-206 2.97e-59

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: 192.90  E-value: 2.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQ 165
Cdd:cd17940   81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490869766 166 DALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMV 206
Cdd:cd17940  160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
15-203 6.06e-59

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


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 192.08  E-value: 6.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFRVqsLVLCPTRELADQVA 89
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrpkKKAATRV--LVLVPTRELAMQCF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  90 KEIRTLARgIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERER-IDLSELNTLVLDEADRMLEMGFQDAL 168
Cdd:cd17947   79 SVLQQLAQ-FTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490869766 169 DAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17947  158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
6-201 4.25e-57

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: 189.41  E-value: 4.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFR---------VQSL 76
Cdd:cd18052   45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTassfsevqePQAL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  77 VLCPTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEA 156
Cdd:cd18052  125 IVAPTRELANQIFLEARKFSYGT-CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490869766 157 DRMLEMGFQDALDAVIEAA---PK-DRQTLLFSATFPKQIKSVADRIMN 201
Cdd:cd18052  204 DRMLDMGFGPEIRKLVSEPgmpSKeDRQTLMFSATFPEEIQRLAAEFLK 252
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
217-347 1.74e-56

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: 183.09  E-value: 1.74e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 217 IQQHFYKVEGTEARDDALELMLLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISI 296
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490869766 297 LVATDVAARGLDVDNLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFF 347
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
6-349 3.24e-55

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 191.92  E-value: 3.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQnlRVKRFRVQ---------SL 76
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIS--RCCTIRSGhpseqrnplAM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  77 VLCPTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEA 156
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGL-PFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 157 DRMLEMGFQDALDAVIEAAPKDrQTLLFSATFPKQIKSVADRIMNNPEMVKV-ESTHDHSSIQQHFYKVEGTEARDDALE 235
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQLAIWVETKQKKQKLFD 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 236 LML--LHHQPeSAVVFCNTKKEVQNVNDELS-HRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNL 312
Cdd:PLN00206 359 ILKskQHFKP-PAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 490869766 313 DAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFSE 349
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
15-206 1.01e-52

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: 176.74  E-value: 1.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFRVQ---SLVLCPTRELAD 86
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppLDEETKDDgpyALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  87 QVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQD 166
Cdd:cd17945   81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 167 ALDAVIEAAPKD--------------------RQTLLFSATFPKQIKSVADRIMNNPEMV 206
Cdd:cd17945  160 QVTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
15-203 2.62e-52

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: 174.86  E-value: 2.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQS-----LVLCPTRELADQVA 89
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgpivLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  90 KEIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALD 169
Cdd:cd17966   81 QEANKFGGS-SRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 490869766 170 AVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
5-203 2.78e-52

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: 175.64  E-value: 2.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   5 KFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQS-----LVLC 79
Cdd:cd17953   13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGegpigLIMA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  80 PTRELADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHL---ERERIDLSELNTLVLDEA 156
Cdd:cd17953   93 PTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEA 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490869766 157 DRMLEMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17953  172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
19-209 1.39e-51

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: 172.86  E-value: 1.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  19 LDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFR----VQSLVLCPTRELADQVAKEIRT 94
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTpedgLGALIISPTRELAMQIFEVLRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  95 LARGiHNIKVLTLCGGMPMGPQIGSLeHGAHILVGTPGRILDHL-ERERIDLSELNTLVLDEADRMLEMGFQDALDAVIE 173
Cdd:cd17941   85 VGKY-HSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490869766 174 AAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVE 209
Cdd:cd17941  163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
15-208 2.00e-51

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: 172.39  E-value: 2.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL--RVKRFRVQSLVLCPTRELADQVAKEI 92
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  93 RTLARGIhNIKVLTLCGGM----PMGPQIGSlehGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDAL 168
Cdd:cd17957   81 LKLSKGT-GLRIVLLSKSLeakaKDGPKSIT---KYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490869766 169 DAVIEAAP-KDRQTLLFSATFPKQIKSVADRIMNNPEMVKV 208
Cdd:cd17957  157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
15-208 4.27e-51

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: 171.60  E-value: 4.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFRVQSLVLCPTRELADQVA 89
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  90 KEIRTLARGIHN-IKVLTLCGGMPMGPQIGSL-EHGAHILVGTPGRILDHLER--ERIDLSELNTLVLDEADRMLEMGFQ 165
Cdd:cd17960   81 EVLQSFLEHHLPkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490869766 166 DALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPemVKV 208
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP--VRV 201
DEXDc smart00487
DEAD-like helicases superfamily;
19-211 8.01e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 171.14  E-value: 8.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766    19 LDSLGYTEMTPIQALSLPTILDG-KDVIGQGKTGSGKTAAFGLGVLQNLRvKRFRVQSLVLCPTRELADQVAKEIRTLAr 97
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLG- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766    98 GIHNIKVLTLCGGMPMGPQIGSLEHG-AHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVIEAAP 176
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 490869766   177 KDRQTLLFSATFPKQIKSVADRIMNNPEMVKVEST 211
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
4-208 1.22e-50

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: 170.60  E-value: 1.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   4 SKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRE 83
Cdd:cd17950    2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  84 LADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLEHGA-HILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEm 162
Cdd:cd17950   82 LAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLE- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490869766 163 gfqdALD------AVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKV 208
Cdd:cd17950  161 ----QLDmrrdvqEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
4-202 9.08e-50

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: 169.84  E-value: 9.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   4 SKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL----------------- 66
Cdd:cd18051   21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesgyyg 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  67 RVKRFRVqSLVLCPTRELADQVAKEIRTLARGIHnIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLS 146
Cdd:cd18051  101 RRKQYPL-ALVLAPTRELASQIYDEARKFAYRSR-VRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 147 ELNTLVLDEADRMLEMGFQDALDAVIE--AAPK--DRQTLLFSATFPKQIKSVADRIMNN 202
Cdd:cd18051  179 YCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
11-203 1.34e-49

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: 167.89  E-value: 1.34e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  11 LKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQVAK 90
Cdd:cd17939    4 LSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  91 EIRTLarGIH-NIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALD 169
Cdd:cd17939   84 VVKAL--GDYmGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 490869766 170 AVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17939  162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
6-206 2.12e-49

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: 167.50  E-value: 2.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQnlrvkrfRVQSLVLCPTRELA 85
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIRTLARGIHN--IKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMG 163
Cdd:cd17938   74 EQTYNCIENFKKYLDNpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490869766 164 FQDALDAVIEAAPK-----DR-QTLLFSATFPK-QIKSVADRIMNNPEMV 206
Cdd:cd17938  154 NLETINRIYNRIPKitsdgKRlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
15-203 2.30e-49

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: 166.96  E-value: 2.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQVAKEIRT 94
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  95 LARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVIEA 174
Cdd:cd17962   81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
                        170       180
                 ....*....|....*....|....*....
gi 490869766 175 APKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17962  161 ISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
11-208 1.81e-48

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: 165.06  E-value: 1.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  11 LKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL------RVKRFRVQSLVLCPTREL 84
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  85 ADQVAKEIRTLARGIHN-IKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERI-DLSELNTLVLDEADRMLEM 162
Cdd:cd17961   81 AQQVSKVLEQLTAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490869766 163 GFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKV 208
Cdd:cd17961  161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
15-203 2.65e-48

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: 164.13  E-value: 2.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQ-----SLVLCPTRELADQVA 89
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKgegpiAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  90 KEIRTLARgIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALD 169
Cdd:cd17952   81 LEAKKFGK-AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 490869766 170 AVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
11-203 5.31e-48

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: 163.52  E-value: 5.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  11 LKPELLNTLDSLGYTEMTPIQALSLPTILDG--KDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQV 88
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  89 AKEIRTLARgIHNIKV-LTLCGG-MPMGPQIGslehgAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEM-GFQ 165
Cdd:cd17963   81 GEVVEKMGK-FTGVKVaLAVPGNdVPRGKKIT-----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHG 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490869766 166 DALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd17963  155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
22-207 1.83e-47

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: 162.76  E-value: 1.83e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  22 LGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQ------SLVLCPTRELADQVAKEIRTL 95
Cdd:cd17949    9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  96 ARGIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLER-ERIDLSELNTLVLDEADRMLEMGFQDALDAVIEA 174
Cdd:cd17949   89 LKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 490869766 175 -------------APKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd17949  169 lddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
15-188 6.62e-47

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: 162.02  E-value: 6.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLP-TILDGKDVIGQGKTGSGKTAAFGLGVLQNL-----RVKRFRVQ----SLVLCPTREL 84
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKQkplrALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  85 ADQVAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILD-------HLEReridLSELNTLVLDEAD 157
Cdd:cd17946   81 AVQVKDHLKAIAKYT-NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWEliqegneHLAN----LKSLRFLVLDEAD 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490869766 158 RMLEMG-FQ------DALDAVIEAAPKDRQTLLFSATF 188
Cdd:cd17946  156 RMLEKGhFAelekilELLNKDRAGKKRKRQTFVFSATL 193
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
19-200 6.78e-46

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: 158.09  E-value: 6.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  19 LDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLR-----VKRFRV-QSLVLCPTRELADQVAKEI 92
Cdd:cd17944    5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqqpRKRGRApKVLVLAPTRELANQVTKDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  93 RTLARgihNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVI 172
Cdd:cd17944   85 KDITR---KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490869766 173 EAAPK-----DRQTLLFSATFPKQIKSVADRIM 200
Cdd:cd17944  162 SVSYKkdsedNPQTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
15-207 2.04e-45

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: 156.66  E-value: 2.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELADQVAKEIRT 94
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  95 LARGIHNIKVLTLCGGMPMGPQIGSLEhGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVIEA 174
Cdd:cd17943   81 IGKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490869766 175 APKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd17943  160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
6-203 4.15e-44

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: 153.37  E-value: 4.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIrtLARGIH-NIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGF 164
Cdd:cd18046   81 QQIQKVV--MALGDYmGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490869766 165 QDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd18046  159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
5-202 7.78e-44

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: 153.63  E-value: 7.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   5 KFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQS-----LVLC 79
Cdd:cd18049   25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  80 PTRELADQVAKEIRTLARGIHnIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRM 159
Cdd:cd18049  105 PTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490869766 160 LEMGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNN 202
Cdd:cd18049  184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
16-204 1.13e-43

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: 152.13  E-value: 1.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  16 LNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQS----LVLCPTRELADQ---V 88
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNgtgvIIISPTRELALQiygV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  89 AKEIRTLargiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSE-LNTLVLDEADRMLEMGFQDA 167
Cdd:cd17942   82 AKELLKY----HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEE 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490869766 168 LDAVIEAAPKDRQTLLFSATFPKQIKSVAdRIMNNPE 204
Cdd:cd17942  158 MRQIIKLLPKRRQTMLFSATQTRKVEDLA-RISLKKK 193
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
6-203 1.93e-43

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: 151.47  E-value: 1.93e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRELA 85
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  86 DQVAKEIrtLARGIH-NIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGF 164
Cdd:cd18045   81 VQIQKVL--LALGDYmNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 490869766 165 QDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNP 203
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
15-196 1.17e-42

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: 149.80  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVL-----QNLRVKRFRVQ---SLVLCPTRELAD 86
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  87 QVAKEIRTLARGIH-----NIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLE 161
Cdd:cd17951   81 QTHEVIEYYCKALQeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490869766 162 MGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVA 196
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFA 195
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
15-202 3.34e-41

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: 147.85  E-value: 3.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQS-----LVLCPTRELADQVA 89
Cdd:cd18050   73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  90 KEIRTLARGiHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDALD 169
Cdd:cd18050  153 QVADDYGKS-SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 231
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490869766 170 AVIEAAPKDRQTLLFSATFPKQIKSVADRIMNN 202
Cdd:cd18050  232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
15-206 2.76e-37

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: 135.28  E-value: 2.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNL------RVKRFRVQSLVLCPTRELADQV 88
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdlqpipREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  89 AKEIRTLArgIHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDAL 168
Cdd:cd17958   81 EAECSKYS--YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490869766 169 DAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMV 206
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
15-187 8.01e-35

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: 129.67  E-value: 8.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDG---------KDVIGQGKTGSGKTAAFGLGVLQNL--RVKRfRVQSLVLCPTRE 83
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALskRVVP-RLRALIVVPTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  84 LADQVAKEIRTLARGIHnIKVLTLCGGMPMGPQIGSLEHGAH--------ILVGTPGRILDHLER-ERIDLSELNTLVLD 154
Cdd:cd17956   80 LVQQVYKVFESLCKGTG-LKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNStPGFTLKHLRFLVID 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490869766 155 EADRMLEMGFQDALDAVIEA--------------------APKDRQTLLFSAT 187
Cdd:cd17956  159 EADRLLNQSFQDWLETVMKAlgrptapdlgsfgdanllerSVRPLQKLLFSAT 211
RRM_EcDbpA_like cd12501
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ...
386-458 8.75e-34

RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.


Pssm-ID: 409924 [Multi-domain]  Cd Length: 73  Bit Score: 121.58  E-value: 8.75e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490869766 386 TIQIDGGKKAKLRAGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARIL 458
Cdd:cd12501    1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRLL 73
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
2-209 1.18e-33

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: 126.29  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   2 STSKFSSIALKPELLNTLDSLGYTEMTPIQALSLPTILDG--KDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLC 79
Cdd:cd18048   16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  80 PTRELADQVAKEIRTLARGIHNIKVLTLCGG--MPMGPQIgslehGAHILVGTPGRILDHLERER-IDLSELNTLVLDEA 156
Cdd:cd18048   96 PTFELALQTGKVVEEMGKFCVGIQVIYAIRGnrPGKGTDI-----EAQIVIGTPGTVLDWCFKLRlIDVTNISVFVLDEA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490869766 157 DRMLEM-GFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVKVE 209
Cdd:cd18048  171 DVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLK 224
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
229-338 8.08e-30

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: 8.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  229 ARDDALELMLLHHQPESAVVFCNTKKEVQNvnDELSHR-GFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGL 307
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 490869766  308 DVDNLDAVFNFELSRDPEVHVHRIGRTGRAG 338
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
15-223 1.61e-27

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: 109.76  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  15 LLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQ-------SLVLCPTRELADQ 87
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  88 VAKEIRTLARGIhNIKVLTLCGGMPMGPQIGSLEHGAHILVGTPGRILDHLERERIDLSELNTLVLDEADRMLEMGFQDA 167
Cdd:cd17948   81 IGSVAQSLTEGL-GLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490869766 168 L--------------DAVIEAAPKdRQTLLFSATFPKQIKSVADRIMNNPEMVKVESTHDH---SSIQQHFYK 223
Cdd:cd17948  160 LshflrrfplasrrsENTDGLDPG-TQLVLVSATMPSGVGEVLSKVIDVDSIETVTSDKLHrlmPHVKQKFLR 231
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
6-207 5.06e-25

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: 102.11  E-value: 5.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   6 FSSIALKPELLNTLDSLGYTEMTPIQALSLPTIL--DGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVQSLVLCPTRE 83
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  84 LADQVAKEIRTLARGIHNIKVLTLCGG--MPMGPQIGSlehgaHILVGTPGRILDH-LERERIDLSELNTLVLDEADRML 160
Cdd:cd18047   83 LALQTGKVIEQMGKFYPELKLAYAVRGnkLERGQKISE-----QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMI 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490869766 161 E-MGFQDALDAVIEAAPKDRQTLLFSATFPKQIKSVADRIMNNPEMVK 207
Cdd:cd18047  158 AtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
HELICc smart00490
helicase superfamily c-terminal domain;
257-338 3.21e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.74  E-value: 3.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   257 QNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDPEVHVHRIGRTGR 336
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 490869766   337 AG 338
Cdd:smart00490  81 AG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
41-187 5.40e-24

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: 97.47  E-value: 5.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  41 GKDVIGQGKTGSGKTAAFGLGVLQNLRVKRFRVqsLVLCPTRELADQVAKEIRTLARgiHNIKVLTLCGGMPMGPQIGSL 120
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 121 EHGAHILVGTPGRILDHLERE-RIDLSELNTLVLDEADRMLEMGFQDALD--AVIEAAPKDRQTLLFSAT 187
Cdd:cd00046   77 LGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
386-457 1.47e-21

DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].


Pssm-ID: 461082 [Multi-domain]  Cd Length: 72  Bit Score: 87.82  E-value: 1.47e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490869766  386 TIQIDGGKKAKLRAGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARI 457
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
50-333 6.14e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 92.40  E-value: 6.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  50 TGSGKTAaFGLGVLQNLRVKRfRVqsLVLCPTRELADQVAKEIRTLARGIHNIKvltlcggmpmgpqiGSLEHGAHILVG 129
Cdd:COG1061  109 TGTGKTV-LALALAAELLRGK-RV--LVLVPRRELLEQWAEELRRFLGDPLAGG--------------GKKDSDAPITVA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 130 TPGRILDHLERERIDlSELNTLVLDEADRMLEMGFQDALDAVieaapKDRQTLLFSAT-------------FPKQIKSV- 195
Cdd:COG1061  171 TYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAF-----PAAYRLGLTATpfrsdgreillflFDGIVYEYs 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 196 -----ADRIMNNPEMVKVES-----THDHSSIQQHFYK--VEGTEARDDAL-ELMLLHHQPESAVVFCNTKKEVQNVNDE 262
Cdd:COG1061  245 lkeaiEDGYLAPPEYYGIRVdltdeRAEYDALSERLREalAADAERKDKILrELLREHPDDRKTLVFCSSVDHAEALAEL 324
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 263 LSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDPEVHVHRIGR 333
Cdd:COG1061  325 LNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
221-347 3.86e-15

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: 71.86  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 221 FYKV---EGTEARDDALELMLLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISIL 297
Cdd:cd18794    5 FYSVrpkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490869766 298 VATdvAARGLDVDNLD--AVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFF 347
Cdd:cd18794   85 VAT--VAFGMGIDKPDvrFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
7-214 1.88e-13

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: 70.10  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   7 SSIALKPELLNTldslGYTEMTPIQALSLPTIL---------DGKDVIGQGK-------TGSGKTAAFGLGVL------- 63
Cdd:cd17965   15 IKEILKGSNKTD----EEIKPSPIQTLAIKKLLktlmrkvtkQTSNEEPKLEvfllaaeTGSGKTLAYLAPLLdylkrqe 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  64 ----------QNLRVKRFRVQSLVLCPTRELADQVAKEIRTLARGIH-NIKVLTLCGGMPMGPQIGSLEHGAHILVGTPG 132
Cdd:cd17965   91 qepfeeaeeeYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 133 RILDHLERERIDLSELNTLVLDEADRMLEMGFQDALDAVIEAAPKDRQTLLFSATFPKQIksvaDRIMNN--PEMVKVES 210
Cdd:cd17965  171 KLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEF----DKTLRKlfPDVVRIAT 246

                 ....
gi 490869766 211 THDH 214
Cdd:cd17965  247 PRLH 250
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
221-350 8.35e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 64.01  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 221 FYKVE--GTEARDDALELMLLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILV 298
Cdd:COG0514  206 RLEVVpkPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIV 285
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490869766 299 ATdvAARGLDVD--NLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFFSEK 350
Cdd:COG0514  286 AT--IAFGMGIDkpDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
8-344 5.16e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 61.45  E-value: 5.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   8 SIALKPELLNTLDSLGYTEMTPIQALSLP-TILDGKDVIGQGKTGSGKTAAFGLGVLQNLRvKRFRVqsLVLCPTRELAD 86
Cdd:COG1204    4 AELPLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALL-NGGKA--LYIVPLRALAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  87 QVAKEIRTLARGIhNIKVLTLCGGMPMGPQ-IGSlehgAHILVGTPGRiLDHLERERID-LSELNTLVLDEA------DR 158
Cdd:COG1204   81 EKYREFKRDFEEL-GIKVGVSTGDYDSDDEwLGR----YDILVATPEK-LDSLLRNGPSwLRDVDLVVVDEAhliddeSR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 159 --MLEMgfqdALDAVIEAAPkDRQTLLFSATfpkqIKSVAD--RIMNNPEmvkVEST----------HDHSSIQqhfYKV 224
Cdd:COG1204  155 gpTLEV----LLARLRRLNP-EAQIVALSAT----IGNAEEiaEWLDAEL---VKSDwrpvplnegvLYDGVLR---FDD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 225 EGTEARDDALELMlLHH--QPESAVVFCNTKKEVQNV-----------------------------NDELSHRGFSVIEL 273
Cdd:COG1204  220 GSRRSKDPTLALA-LDLleEGGQVLVFVSSRRDAESLakkladelkrrltpeereeleelaeelleVSEETHTNEKLADC 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 274 --------HGDMEQRERDqaLVQ--FSNKTISILVATDVAARGLdvdNLDA--VFNFELSRDPEVH-----VHR-IGRTG 335
Cdd:COG1204  299 lekgvafhHAGLPSELRR--LVEdaFREGLIKVLVATPTLAAGV---NLPArrVIIRDTKRGGMVPipvleFKQmAGRAG 373
                        410
                 ....*....|.
gi 490869766 336 RAG--SKGVAI 344
Cdd:COG1204  374 RPGydPYGEAI 384
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
386-452 5.38e-10

RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.


Pssm-ID: 409698 [Multi-domain]  Cd Length: 71  Bit Score: 55.25  E-value: 5.38e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490869766 386 TIQIDGGKKAKLRAGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQ 452
Cdd:cd12252    1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKK 67
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
234-344 7.83e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 61.28  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 234 LELMLLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGD--------MEQRERDQALVQFSNKTISILVATDVAAR 305
Cdd:COG1111  344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEE 423
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490869766 306 GLDVDNLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAI 344
Cdd:COG1111  424 GLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGRVVV 462
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
50-156 4.41e-09

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: 56.12  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  50 TGSGKT--AAFGLGVL--QNLRVKRFRVQSLVLCPTRELADQVAKEIRTLArgihNIKVLTLCGGMpmGPQIGSLEH--- 122
Cdd:cd18034   25 TGSGKTliAVMLIKEMgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHT----DLKVGEYSGEM--GVDKWTKERwke 98
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490869766 123 ---GAHILVGTPGRILDHLERERIDLSELNTLVLDEA 156
Cdd:cd18034   99 eleKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
245-352 6.91e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 58.19  E-value: 6.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 245 SAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDP 324
Cdd:PRK11057 238 SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
                         90       100
                 ....*....|....*....|....*...
gi 490869766 325 EVHVHRIGRTGRAGSKGVAISFFSEKEM 352
Cdd:PRK11057 318 ESYYQETGRAGRDGLPAEAMLFYDPADM 345
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
31-156 8.48e-09

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: 54.90  E-value: 8.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  31 QALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLrVKRFRVQSLVLCPTRELA-DQVaKEIRTLARGIH-NIKVLTLC 108
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAqDQL-RSLRELLEQLGlGIRVATYD 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490869766 109 GGMPMGPQIGSLEHGAHILVGTPGR----ILDHLERERIDLSELNTLVLDEA 156
Cdd:cd17923   83 GDTPREERRAIIRNPPRILLTNPDMlhyaLLPHHDRWARFLRNLRYVVLDEA 134
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
236-332 1.35e-08

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 53.25  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 236 LMLLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSN--KTISILVATDVAARGLdvdNL- 312
Cdd:cd18793   20 LEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGL---NLt 96
                         90       100
                 ....*....|....*....|....*...
gi 490869766 313 --DAVFNFELSRDPEVH------VHRIG 332
Cdd:cd18793   97 aaNRVILYDPWWNPAVEeqaidrAHRIG 124
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
294-347 1.79e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 51.17  E-value: 1.79e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490869766 294 ISILVATDVAARGLDVDNLDAVFNFELSRDPEVHVHRIGRTGRAGSKGVAISFF 347
Cdd:cd18785   23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
10-156 3.67e-08

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: 56.00  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  10 ALKPELLNTLDSLGYTEMTPIQALSLPTILDGKDVIGQGKTGSGKTAAFGLGVLQNLRVKRfRVQSLVLCPTRELA-DQV 88
Cdd:COG1205   40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALArDQL 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490869766  89 AKeIRTLARGIH-NIKVLTLCGGMPMG--PQIgsLEHgAHILVGTP-----GrILDHLERERIDLSELNTLVLDEA 156
Cdd:COG1205  119 RR-LRELAEALGlGVRVATYDGDTPPEerRWI--REH-PDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEA 189
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
26-189 1.63e-07

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: 51.11  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  26 EMTPIQALSLPTILDGKD--VIGQGkTGSGKTAAFGLGVLQNLRVKRFRVqsLVLCPTRELADQVAKEIRTLARgIHNIK 103
Cdd:cd17921    1 LLNPIQREALRALYLSGDsvLVSAP-TSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFG-PLGKN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 104 VLTLCGGMPMGPQigsLEHGAHILVGTPgRILDHLER--ERIDLSELNTLVLDEAdRMLEMG-----FQDALDAVIEAAP 176
Cdd:cd17921   77 VGLLTGDPSVNKL---LLAEADILVATP-EKLDLLLRngGERLIQDVRLVVVDEA-HLIGDGergvvLELLLSRLLRINK 151
                        170
                 ....*....|...
gi 490869766 177 KdRQTLLFSATFP 189
Cdd:cd17921  152 N-ARFVGLSATLP 163
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
43-340 7.81e-07

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 50.89  E-value: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  43 DVIGQGKTGSGKTAAfGLGVLQNLRVKRFRVQSLVLCPTRELADQVAKEIRTLARGIHNIKVLTLCGGMPMGPQIGSLE- 121
Cdd:cd09639    1 LLVIEAPTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMGDSEEFEh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 122 ------HGAHILVGTPGRI--LDHL---------ERERIDLSELNT-LVLDEADRMLE---MGFQDALDAvieAAPKDRQ 180
Cdd:cd09639   80 lfplyiHSNDTLFLDPITVctIDQVlksvfgefgHYEFTLASIANSlLIFDEVHFYDEytlALILAVLEV---LKDNDVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 181 TLLFSATFPKQIKSVADRImnnpEMVKVESTHDHSSIQQHFYKVEgtEARDDA----LELML-LHHQPESAVVFCNTKKE 255
Cdd:cd09639  157 ILLMSATLPKFLKEYAEKI----GYVEENEPLDLKPNERAPFIKI--ESDKVGeissLERLLeFIKKGGSVAIIVNTVDR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 256 VQNVNDELSHRG--FSVIELHGDMEQRER----DQALVQFSNKTISILVATDVAARGLDVDnldavFNF---ELSrDPEV 326
Cdd:cd09639  231 AQEFYQQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDIS-----VDVmitELA-PIDS 304
                        330
                 ....*....|....
gi 490869766 327 HVHRIGRTGRAGSK 340
Cdd:cd09639  305 LIQRLGRLHRYGEK 318
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
277-336 1.01e-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: 48.12  E-value: 1.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 277 MEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFELSRDPEVHVHRIGRTGR 336
Cdd:cd18801   74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
50-188 3.57e-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: 46.53  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  50 TGSGKTAaFGLGVLQNLRVKRFrvqsLVLCPTRELADQVAKEIRTLaRGIHNIKVLTlcggmpmgpqIGSLEH--GAHIL 127
Cdd:cd17926   27 TGSGKTL-TALALIAYLKELRT----LIVVPTDALLDQWKERFEDF-LGDSSIGLIG----------GGKKKDfdDANVV 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490869766 128 VGTPgRILDHLERERIDLSELNTLVL-DEADRMLEMGFQDALDaviEAAPKDRqtLLFSATF 188
Cdd:cd17926   91 VATY-QSLSNLAEEEKDLFDQFGLLIvDEAHHLPAKTFSEILK---ELNAKYR--LGLTATP 146
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
387-457 1.17e-05

RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409923 [Multi-domain]  Cd Length: 73  Bit Score: 43.22  E-value: 1.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 387 IQIDGGKKAKLRAGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARI 457
Cdd:cd12500    2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVKVNK 72
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
233-340 2.20e-05

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: 44.12  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 233 ALELMLLHHQPESAVVFCNTkkevqnvndeLSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNL 312
Cdd:cd18802   40 VLSRLLKEHPSTLAFIRCGF----------LIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPAC 109
                         90       100
                 ....*....|....*....|....*...
gi 490869766 313 DAVFNFELSRDPEVHVHRIGRTGRAGSK 340
Cdd:cd18802  110 NLVIRFDLPKTLRSYIQSRGRARAPNSK 137
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
244-334 2.47e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 46.76  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 244 ESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTIS--ILVATDVAARGLdvdNL---DAVFNF 318
Cdd:COG0553  550 EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGL---NLtaaDHVIHY 626
                         90       100
                 ....*....|....*....|..
gi 490869766 319 ELSRDPEVH------VHRIGRT 334
Cdd:COG0553  627 DLWWNPAVEeqaidrAHRIGQT 648
PRK13766 PRK13766
Hef nuclease; Provisional
238-339 3.42e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 46.41  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 238 LLHHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGD--------MEQRERDQALVQFSNKTISILVATDVAARGLDV 309
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
                         90       100       110
                 ....*....|....*....|....*....|....
gi 490869766 310 DNLDAVFNFElsrdP---EVH-VHRIGRTGRAGS 339
Cdd:PRK13766 440 PSVDLVIFYE----PvpsEIRsIQRKGRTGRQEE 469
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
151-389 3.80e-05

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 45.52  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  151 LVLDEADRMLE---MGFQDALDAvieAAPKDRQTLLFSATFPKQIKSVADRImnnpEMVKVESTHDHSSIQQHF-YKVEG 226
Cdd:TIGR01587 128 LIFDEVHFYDEytlALILAVLEV---LKDNDVPILLMSATLPKFLKEYAEKI----GYVEFNEPLDLKEERRFEnHRFIL 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  227 TEARDDALELML-----LHHQPESAVVFCNTKKEVQNVNDELSHRG--FSVIELHGDMEQRERDQALVQ-----FSNKTI 294
Cdd:TIGR01587 201 IESDKVGEISSLerlleFIKKGGSIAIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAKKEAEllremKKSNEK 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  295 SILVATDVAARGLDVDnldavFNF---ELSrDPEVHVHRIGRTGRAGSKgvaisffsekemhrvaqIDEYMDMPIEPSQL 371
Cdd:TIGR01587 281 FVIVATQVIEASLDIS-----ADVmitELA-PIDSLIQRLGRLHRYGRK-----------------IGENFEVYIITIAP 337
                         250
                  ....*....|....*...
gi 490869766  372 PAKPIAKPYYSNMVTIQI 389
Cdd:TIGR01587 338 EGKLFPYPYELVERTIQK 355
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
47-159 4.03e-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: 44.33  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  47 QGKTGSGKTAAFGLGVLQNLRVKRfrvQSLVLCPTRELADQVAKEIRTLargIHNIKVLTLCGGMPmgPQIGSlehGAHI 126
Cdd:cd17918   42 SGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKF---LPFINVELVTGGTK--AQILS---GISL 110
                         90       100       110
                 ....*....|....*....|....*....|...
gi 490869766 127 LVGTPGRILDHLERERIDLselntLVLDEADRM 159
Cdd:cd17918  111 LVGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
386-458 4.28e-05

RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409922 [Multi-domain]  Cd Length: 73  Bit Score: 41.40  E-value: 4.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490869766 386 TIQIDGGKKAKLRAGDILGALTGQGGIDGKSVGKINLFAMRAYVAVERSMAKKALGKIESGKMKGRQFRARIL 458
Cdd:cd12499    1 RYRIEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
30-155 5.78e-05

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: 43.88  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  30 IQALSLPTILDG-KDVIGQGKTGSGKTAAFGLGVLQNLR----VKRFRVQSLVLCPTRELADQVAKEIRtlAR-GIHNIK 103
Cdd:cd18023    5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKernpLPWGNRKVVYIAPIKALCSEKYDDWK--EKfGPLGLS 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490869766 104 VLTLCGGMPMGPqIGSLEHgAHILVGTPGRiLDHLERERIDLSELNTLV----LDE 155
Cdd:cd18023   83 CAELTGDTEMDD-TFEIQD-ADIILTTPEK-WDSMTRRWRDNGNLVQLValvlIDE 135
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
254-311 1.12e-04

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 42.33  E-value: 1.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490869766 254 KEVQNVNDELSHR---GFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDN 311
Cdd:cd18811   45 KAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPN 105
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
223-344 7.68e-04

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 39.84  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 223 KVEGTEARDDALELMLLHHQPE-SAVVFCNTKKEVQNVNDELShrGFSVIelHGDMEQRERDqaLVQ--FSNKTISILVA 299
Cdd:cd18795   22 DVMNKFDSDIIVLLKIETVSEGkPVLVFCSSRKECEKTAKDLA--GIAFH--HAGLTREDRE--LVEelFREGLIKVLVA 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490869766 300 TDVAARGLdvdNLDA---------VFNFELSRD-PEVHVHR-IGRTGRAG--SKGVAI 344
Cdd:cd18795   96 TSTLAAGV---NLPArtviikgtqRYDGKGYRElSPLEYLQmIGRAGRPGfdTRGEAI 150
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
50-160 7.77e-04

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


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 40.39  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  50 TGSGKTAaFGLGVLQNLRVKRFRVqsLVLCPTRELADQVAKEIRTLARGIH-NIKVLTLCGGMPMGPQIGSLEH----GA 124
Cdd:cd17924   41 TGVGKTT-FGLATSLYLASKGKRS--YLIFPTKSLVKQAYERLSKYAEKAGvEVKILVYHSRLKKKEKEELLEKiekgDF 117
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490869766 125 HILVGTPGRILDHleRERIDLSELNTLVLDEADRML 160
Cdd:cd17924  118 DILVTTNQFLSKN--FDLLSNKKFDFVFVDDVDAVL 151
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
50-158 1.00e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 40.19  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  50 TGSGKTAAFGLGVLQNLRVKRFRVqsLVLCPTRELADQVAKEIRTLARGIHNIKVLTlcgGMPMGPQIGSLEHGAHILVG 129
Cdd:cd18035   25 TGLGKTIIAILVAADRLTKKGGKV--LILAPSRPLVEQHAENLKRVLNIPDKITSLT---GEVKPEERAERWDASKIIVA 99
                         90       100
                 ....*....|....*....|....*....
gi 490869766 130 TPGRILDHLERERIDLSELNTLVLDEADR 158
Cdd:cd18035  100 TPQVIENDLLAGRITLDDVSLLIFDEAHH 128
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
240-355 1.10e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.81  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  240 HHQPESAVVFCNTKKEVQNVNDELSHRGFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDAVFNFE 319
Cdd:PLN03137  677 NHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHS 756
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 490869766  320 LSRDPEVHVHRIGRTGRAGSKGVAISFFSEKEMHRV 355
Cdd:PLN03137  757 LPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRV 792
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
244-315 1.25e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 38.69  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490869766 244 ESAVVFCNTKKEVQNVNDELSHRGFSVIELHGD--MEQRERDQALVQFSNKT-ISILVATDVAARGLDVDNLDAV 315
Cdd:cd18799    7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFGELkPPILVTVDLLTTGVDIPEVDNV 81
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
254-344 1.36e-03

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: 39.17  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766 254 KEVQNVNDELSHR--GFSVIELHGDMEQRERDQALVQFSNKTISILVATDVAARGLDVDNLDA--VFN---FELSrdpEV 326
Cdd:cd18792   45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTmiIEDadrFGLS---QL 121
                         90
                 ....*....|....*...
gi 490869766 327 HVHRiGRTGRAGSKGVAI 344
Cdd:cd18792  122 HQLR-GRVGRGKHQSYCY 138
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
41-155 1.96e-03

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: 39.10  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  41 GKDVIGQGKTGSGKTAAFGLGVLQNL-RVKRFRVQSLVLCPTRELADQVAKEIRTLARGIH-NIKVLTLCGGMPMGPQIG 118
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDlEIPVAVRHGDTSQSEKAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490869766 119 SLEHGAHILVGTPGRILDHLERERID--LSELNTLVLDE 155
Cdd:cd17922   81 QLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
PRK13767 PRK13767
ATP-dependent helicase; Provisional
24-131 4.15e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 39.87  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766  24 YTEMTPIQALSLPTILDGKDVIGQGKTGSGKT-AAFgLGVLQNLrVKRFRVQSL---VLC----PTRELA-------DQV 88
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDEL-FRLGREGELedkVYClyvsPLRALNndihrnlEEP 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490869766  89 AKEIRTLARG----IHNIKVLTLCGGMPMGPQIGSLEHGAHILVGTP 131
Cdd:PRK13767 108 LTEIREIAKErgeeLPEIRVAIRTGDTSSYEKQKMLKKPPHILITTP 154
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
24-66 5.85e-03

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 39.32  E-value: 5.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490869766  24 YTEMTPIQALSLPTILDGKDVIGQGKTGSGKT-AAFgLGVLQNL 66
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDEL 64
ResIII pfam04851
Type III restriction enzyme, res subunit;
50-189 6.88e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.27  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490869766   50 TGSGKT---AAFGLGVLQNLRVKRFrvqsLVLCPTRELADQVAKEIRTLARGIHNIKVLTlcggmpMGPQIGSLEHGAHI 126
Cdd:pfam04851  32 TGSGKTltaAKLIARLFKKGPIKKV----LFLVPRKDLLEQALEEFKKFLPNYVEIGEII------SGDKKDESVDDNKI 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490869766  127 LVGTPGRILDHLERERIDLSELNTLVL--DEADRMLEMGFQDALDAVIEAapkdrqTLL-FSATFP 189
Cdd:pfam04851 102 VVTTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASSYRNILEYFKPA------FLLgLTATPE 161
 
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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