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Conserved domains on  [gi|444285213|gb|ELU90294|]
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putative DEAD-box ATP-dependent RNA helicase CshB [Streptococcus pneumoniae PNI0360]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-392 8.56e-162

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 462.69  E-value: 8.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD-EASDSVQAVITAPSR 79
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDpSRPRAPQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSDVevRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTL 159
Cdd:COG0513   82 ELALQVAEELRKLAKYLGL--RVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 160 DMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQIYQLTQS 239
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 240 MQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAI 319
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285213 320 PQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEKL-GIKFSPKMVKDGEFQDTYDRDRRANREKKQDK 392
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLK 392
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-392 8.56e-162

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 462.69  E-value: 8.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD-EASDSVQAVITAPSR 79
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDpSRPRAPQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSDVevRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTL 159
Cdd:COG0513   82 ELALQVAEELRKLAKYLGL--RVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 160 DMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQIYQLTQS 239
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 240 MQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAI 319
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285213 320 PQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEKL-GIKFSPKMVKDGEFQDTYDRDRRANREKKQDK 392
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLK 392
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
12-203 9.46e-84

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: 255.44  E-value: 9.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDE----ASDSVQAVITAPSRELATQIYQ 87
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  88 VARQISAHSDVevRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETV 167
Cdd:cd00268   81 VARKLGKGTGL--KVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 444285213 168 DKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd00268  158 EKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPV 193
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
16-366 4.15e-80

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 255.11  E-value: 4.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  16 LKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQiyqVARQIS-- 93
Cdd:PRK11776  19 LNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQ---VAKEIRrl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 AHSDVEVRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADS 173
Cdd:PRK11776  96 ARFIPNIKVLTLCGGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 174 LPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTkTVISDTIDNWLISTKGHDKNAQIYQLTQSMQPYLAMIFVNTKT 253
Cdd:PRK11776 175 APARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 254 RADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRT 333
Cdd:PRK11776 254 ECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRT 333
                        330       340       350
                 ....*....|....*....|....*....|....
gi 444285213 334 GRNGLPGTAITLYQPSDDSDIRELEK-LGIKFSP 366
Cdd:PRK11776 334 GRAGSKGLALSLVAPEEMQRANAIEDyLGRKLNW 367
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
25-192 4.67e-50

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 167.42  E-value: 4.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   25 TEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEVRVVn 104
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  105 yVGGTDKARQIEKLESnqPHIVIGTPGRIYDLVKSGDLaIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQFMVFS 184
Cdd:pfam00270  80 -LGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLS 155

                  ....*...
gi 444285213  185 ATIPQKLQ 192
Cdd:pfam00270 156 ATLPRNLE 163
DEXDc smart00487
DEAD-like helicases superfamily;
16-212 5.34e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 163.43  E-value: 5.34e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213    16 LKELKFTTPTEVQDKLIPIVLAG-RDLVGESKTGSGKTHTFLLPIFQQLDEaSDSVQAVITAPSRELATQIYQVARQISA 94
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213    95 HSDVevRVVNYVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSL 174
Cdd:smart00487  80 SLGL--KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 444285213   175 PKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTV 212
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-392 8.56e-162

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 462.69  E-value: 8.56e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD-EASDSVQAVITAPSR 79
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDpSRPRAPQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSDVevRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTL 159
Cdd:COG0513   82 ELALQVAEELRKLAKYLGL--RVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 160 DMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQIYQLTQS 239
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 240 MQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAI 319
Cdd:COG0513  239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285213 320 PQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEKL-GIKFSPKMVKDGEFQDTYDRDRRANREKKQDK 392
Cdd:COG0513  319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEKLK 392
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
12-203 9.46e-84

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: 255.44  E-value: 9.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDE----ASDSVQAVITAPSRELATQIYQ 87
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  88 VARQISAHSDVevRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETV 167
Cdd:cd00268   81 VARKLGKGTGL--KVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 444285213 168 DKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd00268  158 EKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPV 193
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
16-366 4.15e-80

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 255.11  E-value: 4.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  16 LKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQiyqVARQIS-- 93
Cdd:PRK11776  19 LNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQ---VAKEIRrl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 AHSDVEVRVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADS 173
Cdd:PRK11776  96 ARFIPNIKVLTLCGGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 174 LPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTkTVISDTIDNWLISTKGHDKNAQIYQLTQSMQPYLAMIFVNTKT 253
Cdd:PRK11776 175 APARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 254 RADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRT 333
Cdd:PRK11776 254 ECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRT 333
                        330       340       350
                 ....*....|....*....|....*....|....
gi 444285213 334 GRNGLPGTAITLYQPSDDSDIRELEK-LGIKFSP 366
Cdd:PRK11776 334 GRAGSKGLALSLVAPEEMQRANAIEDyLGRKLNW 367
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
3-371 7.66e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 229.03  E-value: 7.66e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   3 FTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQ-------AVIT 75
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgeprALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  76 APSRELATQIYQVARQISAHSDVEVrvVNYVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEA 155
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNV--MTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 156 DMTLDMGFLETVDKIADSLPK--DLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQI 233
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLL 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 234 YQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSH 313
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 444285213 314 VINDAIPQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEK-LGIKFSPKMVKD 371
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEElLGRKISCEMPPA 465
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
1-359 9.41e-64

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 216.64  E-value: 9.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRE 80
Cdd:PRK11634   6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  81 LATQIYQVARQISAHSDvEVRVVNYVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLD 160
Cdd:PRK11634  86 LAVQVAEAMTDFSKHMR-GVNVVALYGGQRYDVQLRALRQG-PQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 161 MGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQIYQLTQSM 240
Cdd:PRK11634 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 241 QPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIP 320
Cdd:PRK11634 244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 444285213 321 QDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEK 359
Cdd:PRK11634 324 MDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
1-345 1.29e-63

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 211.34  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDE--ASDSVQA--VITA 76
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDfpRRKSGPPriLILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  77 PSRELATQIYQVARQISAHSDVEVRVVNyvGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEAD 156
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATIT--GGVAYMNHAEVFSENQ-DIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 157 MTLDMGFLETVDKIADSLPKDLQFMVFSATIPQK-LQPFLKKYLSNPVM--------EKIKtktvisdtIDNW--LISTK 225
Cdd:PRK11192 158 RMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEveaepsrrERKK--------IHQWyyRADDL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 226 GHdKNAQIYQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARG 305
Cdd:PRK11192 230 EH-KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 444285213 306 IDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITL 345
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
PTZ00424 PTZ00424
helicase 45; Provisional
21-359 1.59e-63

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 210.45  E-value: 1.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  21 FTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEV 100
Cdd:PTZ00424  48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 101 RVVnyVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQF 180
Cdd:PTZ00424 128 HAC--VGGTVVRDDINKLKAGV-HMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 181 MVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHD-KNAQIYQLTQSMQPYLAMIFVNTKTRADELH 259
Cdd:PTZ00424 205 ALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLT 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 260 SYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLP 339
Cdd:PTZ00424 285 KKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRK 364
                        330       340
                 ....*....|....*....|
gi 444285213 340 GTAITLYQPSDDSDIRELEK 359
Cdd:PTZ00424 365 GVAINFVTPDDIEQLKEIER 384
PTZ00110 PTZ00110
helicase; Provisional
2-360 1.24e-62

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 211.94  E-value: 1.24e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIF-----QQLDEASDSVQAVITA 76
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaQPLLRYGDGPIVLVLA 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  77 PSRELATQIYQVARQISAHSDVEVRVVnyVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEAD 156
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVA--YGGVPKRGQIYALR-RGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 157 MTLDMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSN-PVMEKIKTKTV-ISDTIDNWLISTKGHDKNAQIY 234
Cdd:PTZ00110 288 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLtACHNIKQEVFVVEEHEKRGKLK 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 235 QLTQSM--QPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVS 312
Cdd:PTZ00110 368 MLLQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 444285213 313 HVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEKL 360
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKV 495
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
3-345 1.04e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 200.97  E-value: 1.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   3 FTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL--DEASDSVQ-----AVIT 75
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKvnqprALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  76 APSRELATQIYQVARQISAHSDVEVRVVnYvGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEA 155
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLA-Y-GGDGYDKQLKVLE-SGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 156 DMTLDMGFLetvdkiadslpKDLQF-------------MVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLI 222
Cdd:PRK04837 167 DRMFDLGFI-----------KDIRWlfrrmppanqrlnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 223 STKGHDKNAQIYQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLA 302
Cdd:PRK04837 236 YPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 444285213 303 ARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITL 345
Cdd:PRK04837 316 ARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
1-372 3.38e-58

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 197.72  E-value: 3.38e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD------EASDSVQAVI 74
Cdd:PRK10590   1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItrqphaKGRRPVRALI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  75 TAPSRELATQIYQVARQISAHSDVEVRVVnyVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDE 154
Cdd:PRK10590  81 LTPTRELAAQIGENVRDYSKYLNIRSLVV--FGGVSINPQMMKLRGGV-DVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 155 ADMTLDMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQIY 234
Cdd:PRK10590 158 ADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 235 QLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHV 314
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 444285213 315 INDAIPQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDSDIRELEKLGIKFSPKMVKDG 372
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPG 375
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
3-204 6.84e-56

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: 184.04  E-value: 6.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   3 FTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELA 82
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  83 TQIYQVARQISAHSDVEVRVVnyVGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMG 162
Cdd:cd17940   81 LQTSQVCKELGKHMGVKVMVT--TGGTSLRDDIMRL-YQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 444285213 163 FLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17940  158 FQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYE 199
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-345 1.32e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 193.63  E-value: 1.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL-------DEASDSVQAV 73
Cdd:PRK04537   9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRAL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  74 ITAPSRELATQIYQVARQISAhsDVEVRVVNYVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDL-AIHKAKTFVV 152
Cdd:PRK04537  89 ILAPTRELAIQIHKDAVKFGA--DLGLRFALVYGGVDYDKQRELLQQGV-DVIIATPGRLIDYVKQHKVvSLHACEICVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 153 DEADMTLDMGFLETVDKIADSLPK--DLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKN 230
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 231 AQIYQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEG 310
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 444285213 311 VSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITL 345
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
12-203 6.65e-52

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: 173.53  E-value: 6.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDS-----VQAVITAPSRELATQIY 86
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgqVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  87 QVARQISAHSDVEVRVVNYVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIhKAKTF---VVDEADMTLDMGF 163
Cdd:cd17960   81 EVLQSFLEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKV-KVKSLevlVLDEADRLLDLGF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 444285213 164 LETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17960  160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPV 199
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
14-203 8.51e-52

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: 172.83  E-value: 8.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  14 EALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQIs 93
Cdd:cd17943    3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKI- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 AHSDVEVRVVNYVGGTDKARQIEKLesNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADS 173
Cdd:cd17943   82 GKKLEGLKCEVFIGGTPVKEDKKKL--KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 444285213 174 LPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17943  160 LPKNKQVIAFSATYPKNLDNLLARYMRKPV 189
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
12-199 5.29e-51

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 171.61  E-value: 5.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLA-GRDLVGESKTGSGKTHTFLLPIFQQL-----DEASDSVQAVITAPSRELATQI 85
Cdd:cd17964    5 LLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  86 YQVARQ-ISAHSDVEVRVVnyVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIH--KAKTFVVDEADMTLDMG 162
Cdd:cd17964   85 AAEAKKlLQGLRKLRVQSA--VGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKAftDLDYLVLDEADRLLDMG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 444285213 163 FLETVDKIADSLPK----DLQFMVFSATIPQKLQPFLKKYL 199
Cdd:cd17964  163 FRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
2-204 2.01e-50

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: 169.79  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSV--QAVITAPSR 79
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSDVevRVVNYVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTL 159
Cdd:cd17959   82 ELALQTLKVTKELGKFTDL--RTALLVGGDSLEEQFEALASN-PDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 444285213 160 DMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17959  159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVL 203
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
25-192 4.67e-50

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 167.42  E-value: 4.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   25 TEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEVRVVn 104
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  105 yVGGTDKARQIEKLESnqPHIVIGTPGRIYDLVKSGDLaIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQFMVFS 184
Cdd:pfam00270  80 -LGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLS 155

                  ....*...
gi 444285213  185 ATIPQKLQ 192
Cdd:pfam00270 156 ATLPRNLE 163
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
14-208 2.49e-49

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: 166.72  E-value: 2.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  14 EALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELAtqiYQVARQIS 93
Cdd:cd17954   13 EACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA---QQISEQFE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 A-HSDVEVRVVNYVGGTDKARQIEKLeSNQPHIVIGTPGRIYD-LVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIA 171
Cdd:cd17954   90 AlGSSIGLKSAVLVGGMDMMAQAIAL-AKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDFEPEIDKIL 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 444285213 172 DSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVmeKIK 208
Cdd:cd17954  169 KVIPRERTTYLFSATMTTKVAKLQRASLKNPV--KIE 203
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
1-343 3.07e-49

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 175.36  E-value: 3.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQ-----QLDEASDSVQ--AV 73
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctiRSGHPSEQRNplAM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  74 ITAPSRELATQIYQVARQISAHSDVEVRVVnyVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVD 153
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALV--VGGDAMPQQLYRIQ-QGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 154 EADMTLDMGFLETVDKIADSLPKDlQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTVISDTIDNWLISTKGHDKNAQI 233
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKL 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 234 YQLTQSMQPYL--AMIFVNTKTRADELHSYLT-AQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEG 310
Cdd:PLN00206 357 FDILKSKQHFKppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                        330       340       350
                 ....*....|....*....|....*....|...
gi 444285213 311 VSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAI 343
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAI 469
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
14-203 1.24e-48

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: 165.09  E-value: 1.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  14 EALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELAtqiYQVARQIS 93
Cdd:cd17955   12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA---YQIAEQFR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 AH-SDVEVRVVNYVGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAI---HKAKTFVVDEADMTLDMGFLETVDK 169
Cdd:cd17955   89 ALgAPLGLRCCVIVGGMDMVKQALEL-SKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGSFEDDLAT 167
                        170       180       190
                 ....*....|....*....|....*....|....
gi 444285213 170 IADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17955  168 ILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
15-207 1.70e-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: 164.68  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  15 ALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDS------VQAVITAPSRELATQIYQV 88
Cdd:cd17961    8 AIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqgTRALILVPTRELAQQVSKV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  89 ARQISAHSDVEVRVVNYVGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAI-HKAKTFVVDEADMTLDMGFLETV 167
Cdd:cd17961   88 LEQLTAYCRKDVRVVNLSASSSDSVQRALL-AEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEEDL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 444285213 168 DKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKI 207
Cdd:cd17961  167 KSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEXDc smart00487
DEAD-like helicases superfamily;
16-212 5.34e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 163.43  E-value: 5.34e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213    16 LKELKFTTPTEVQDKLIPIVLAG-RDLVGESKTGSGKTHTFLLPIFQQLDEaSDSVQAVITAPSRELATQIYQVARQISA 94
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213    95 HSDVevRVVNYVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSL 174
Cdd:smart00487  80 SLGL--KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 444285213   175 PKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKTKTV 212
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
2-199 5.40e-48

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: 163.81  E-value: 5.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL----DEASDSV------Q 71
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgPPSVGRGrrkaypS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  72 AVITAPSRELATQIYQVARQISAHSDVEVRVVnYvGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFV 151
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVV-Y-GGADVVHQQLQLL-RGCDILVATPGRLVDFIERGRISLSSIKFLV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 444285213 152 VDEADMTLDMGFLETVDKIA---DSLPKDL-QFMVFSATIP---QKL-QPFLKKYL 199
Cdd:cd17967  158 LDEADRMLDMGFEPQIRKIVehpDMPPKGErQTLMFSATFPreiQRLaADFLKNYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
15-203 9.09e-47

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: 159.73  E-value: 9.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  15 ALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL---DEASDSVQAVITAPSRELATQIYQVARQ 91
Cdd:cd17947    4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  92 ISAHSDVEVRVVnyVGGTDKARQIEKLESnQPHIVIGTPGRIYDLVK-SGDLAIHKAKTFVVDEADMTLDMGFLETVDKI 170
Cdd:cd17947   84 LAQFTDITFALA--VGGLSLKAQEAALRA-RPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 444285213 171 ADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17947  161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPV 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
15-203 1.04e-45

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: 157.07  E-value: 1.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  15 ALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD----EASDSVQAVITAPSRELATQIYQVAR 90
Cdd:cd17941    4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEVLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  91 QISAHSDVEVRVVnyVGGTDKarQIEKLESNQPHIVIGTPGRIYD-LVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDK 169
Cdd:cd17941   84 KVGKYHSFSAGLI--IGGKDV--KEEKERINRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 444285213 170 IADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPE 193
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
2-204 1.61e-44

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: 154.43  E-value: 1.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSREL 81
Cdd:cd17950    3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  82 ATQIYQVARQISAH-SDVEVRVVnyVGGTDKARQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADM--- 157
Cdd:cd17950   83 AFQISNEYERFSKYmPNVKTAVF--FGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKmle 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 444285213 158 TLDMgfLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17950  161 QLDM--RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLE 205
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
12-203 2.60e-44

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: 154.46  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD-----EASDSVQAVITAPSRELATQIY 86
Cdd:cd17953   23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdqrpvKPGEGPIGLIMAPTRELALQIY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  87 QVARQISahSDVEVRVVNYVGGTDKARQIEKLESNQpHIVIGTPGRIYDLV--KSGDLAIHKAKTFVV-DEADMTLDMGF 163
Cdd:cd17953  103 VECKKFS--KALGLRVVCVYGGSGISEQIAELKRGA-EIVVCTPGRMIDILtaNNGRVTNLRRVTYVVlDEADRMFDMGF 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 444285213 164 LETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17953  180 EPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
1-199 2.62e-44

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 155.51  E-value: 2.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL----DEASD-----SVQ 71
Cdd:cd18052   43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegLTASSfsevqEPQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  72 AVITAPSRELATQIYQVARQISAHSDVEVrVVNYvGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFV 151
Cdd:cd18052  123 ALIVAPTRELANQIFLEARKFSYGTCIRP-VVVY-GGVSVGHQIRQIEKG-CHILVATPGRLLDFIGRGKISLSKLKYLI 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 444285213 152 VDEADMTLDMGFLETVDKIADSL---PK-DLQFMVFSATIPQKLQ----PFLKK-YL 199
Cdd:cd18052  200 LDEADRMLDMGFGPEIRKLVSEPgmpSKeDRQTLMFSATFPEEIQrlaaEFLKEdYL 256
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
12-203 3.63e-44

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: 153.29  E-value: 3.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIF-----QQLDEASDSVQAVITAPSRELATQIY 86
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  87 QVARQISAHSDVEVRVVnyVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLET 166
Cdd:cd17966   81 QEANKFGGSSRLRNTCV--YGGAPKGPQIRDLRRG-VEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 444285213 167 VDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17966  158 IRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYI 194
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
12-204 3.91e-43

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: 151.32  E-value: 3.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEA--------SDSVQAVITAPSRELAT 83
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLppldeetkDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  84 QIYQVARQISAHSDveVRVVNYVGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGF 163
Cdd:cd17945   81 QIEEETQKFAKPLG--IRVVSIVGGHSIEEQAFSL-RNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285213 164 LETVDKIADSLPKDL--------------------QFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17945  158 EPQVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVV 218
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
21-203 4.06e-43

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: 150.55  E-value: 4.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  21 FTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEV 100
Cdd:cd17939   17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 101 RVvnYVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQF 180
Cdd:cd17939   97 HA--CIGGTSVREDRRKLQYG-PHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQV 173
                        170       180
                 ....*....|....*....|...
gi 444285213 181 MVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17939  174 VLFSATMPHEVLEVTKKFMRDPV 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
217-346 6.88e-43

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: 147.27  E-value: 6.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 217 IDNWLISTKGHDKNAQIY-QLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEY 295
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 444285213 296 IVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLY 346
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
16-204 1.36e-42

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: 148.89  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  16 LKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDE--ASDSVQAVITAPSRELATQIYQVARQIS 93
Cdd:cd17957    5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYRELLKLS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  94 AHSDVEVRVVNYvGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADS 173
Cdd:cd17957   85 KGTGLRIVLLSK-SLEAKAKDGPKS-ITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAA 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 444285213 174 LP-KDLQFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17957  163 CTnPNLQRSLFSATIPSEVEELARSVMKDPIR 194
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
2-201 1.78e-42

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: 150.19  E-value: 1.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDE-------ASDSVQ--- 71
Cdd:cd18051   22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslPSESGYygr 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  72 ------AVITAPSRELATQIYQVARQISAHSDVEVRVVnYvGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIH 145
Cdd:cd18051  102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVV-Y-GGADIGQQMRDLERG-CHLLVATPGRLVDMLERGKIGLD 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 146 KAKTFVVDEADMTLDMGFLETVDKIA--DSLPK--DLQFMVFSATIPQKLQPFLKKYLSN 201
Cdd:cd18051  179 YCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
12-205 8.42e-42

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: 147.08  E-value: 8.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQqldeasdSVQAVITAPSRELATQIYQVARQ 91
Cdd:cd17938   10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELAEQTYNCIEN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  92 ISAH-SDVEVRVVNYVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKI 170
Cdd:cd17938   83 FKKYlDNPKLRVALLIGGVKAREQLKRLESGV-DIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRI 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 444285213 171 ADSLPK------DLQFMVFSATipqkLQPFLKKYLSNPVME 205
Cdd:cd17938  162 YNRIPKitsdgkRLQVIVCSAT----LHSFEVKKLADKIMH 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
21-203 9.70e-41

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: 144.13  E-value: 9.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  21 FTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEV 100
Cdd:cd18046   19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALGDYMGIKC 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 101 RVVnyVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQF 180
Cdd:cd18046   99 HAC--IGGTSVRDDAQKLQAG-PHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQV 175
                        170       180
                 ....*....|....*....|...
gi 444285213 181 MVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd18046  176 VLLSATMPNDVLEVTTKFMRDPI 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
15-192 1.46e-40

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 143.65  E-value: 1.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  15 ALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEAS----DSVQAVITAPSRELATQIYQVAR 90
Cdd:cd17942    4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkprNGTGVIIISPTRELALQIYGVAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  91 QISAHSDVEVRVVnyVGGTDKARQIEKLESNQPhIVIGTPGRIYD-LVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDK 169
Cdd:cd17942   84 ELLKYHSQTFGIV--IGGANRKAEAEKLGKGVN-ILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180
                 ....*....|....*....|...
gi 444285213 170 IADSLPKDLQFMVFSATIPQKLQ 192
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVE 183
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
12-203 9.34e-40

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: 141.71  E-value: 9.34e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLP-IFQQLDE-------ASDSVQAVITAPSRELAT 83
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQekklpfiKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  84 QIYQVARQISAHSDV----EVRVVNYVGGTDKARQIEKLeSNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTL 159
Cdd:cd17951   81 QTHEVIEYYCKALQEggypQLRCLLCIGGMSVKEQLEVI-RKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 444285213 160 DMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17951  160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPV 203
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
12-203 5.52e-39

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: 139.47  E-value: 5.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIF-----QQLDEASDSVQAVITAPSRELATQIY 86
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  87 QVARQISAHSDVEVRVVnyVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLET 166
Cdd:cd17952   81 LEAKKFGKAYNLRVVAV--YGGGSKWEQAKALQEG-AEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQ 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 444285213 167 VDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17952  158 VRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPI 194
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
16-203 1.18e-38

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: 138.45  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  16 LKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAh 95
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMK- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  96 SDVEVRVVNYVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLP 175
Cdd:cd17962   84 GLPPMKTALLVGGLPLPPQLYRLQQGV-KVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
                        170       180
                 ....*....|....*....|....*...
gi 444285213 176 KDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17962  163 HDHQTILVSATIPRGIEQLAGQLLQNPV 190
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
15-203 3.42e-38

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: 137.32  E-value: 3.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  15 ALKELKFTTPTEVQDKLIPIVLAG--RDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQI 92
Cdd:cd17963    8 GLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEVVEKM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  93 SAHSDVEVRVVnyVGGTDKARQiEKLESnqpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDM-GFLETVDKIA 171
Cdd:cd17963   88 GKFTGVKVALA--VPGNDVPRG-KKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRIK 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 444285213 172 DSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd17963  162 RMLPRNCQILLFSATFPDSVRKFAEKIAPNAN 193
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
21-203 2.83e-37

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: 134.90  E-value: 2.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  21 FTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEV 100
Cdd:cd18045   19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYMNVQC 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 101 RVVnyVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQF 180
Cdd:cd18045   99 HAC--IGGTSVGDDIRKLDYGQ-HIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQV 175
                        170       180
                 ....*....|....*....|...
gi 444285213 181 MVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd18045  176 VLVSATLPQDILEMTNKFMTDPI 198
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
1-199 5.94e-37

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: 135.14  E-value: 5.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   1 MSFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIF-----QQLDEASDSVQAVIT 75
Cdd:cd18049   24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPICLVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  76 APSRELATQIYQVARQISAHSdvEVRVVNYVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEA 155
Cdd:cd18049  104 APTRELAQQVQQVAAEYGRAC--RLKSTCIYGGAPKGPQIRDLERGV-EICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 444285213 156 DMTLDMGFLETVDKIADSLPKDLQFMVFSATIPQKL----QPFLKKYL 199
Cdd:cd18049  181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVrqlaEDFLKDYI 228
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
2-203 5.00e-36

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: 133.98  E-value: 5.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD-----EASDSVQAVITA 76
Cdd:cd18050   63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqpylERGDGPICLVLA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  77 PSRELATQIYQVARQISAHSDVEVRVVnyVGGTDKARQIEKLESNQpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEAD 156
Cdd:cd18050  143 PTRELAQQVQQVADDYGKSSRLKSTCI--YGGAPKGPQIRDLERGV-EICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 444285213 157 MTLDMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPV 203
Cdd:cd18050  220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYV 266
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
12-218 7.68e-36

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: 132.36  E-value: 7.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIP-IVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDS---------VQAVITAPSREL 81
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqkpLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  82 ATQIYQVARQISAHSDVevRVVNYVGGTDKARQiEKLESNQPHIVIGTPGRIYDLVKSGD--LA-IHKAKTFVVDEADMT 158
Cdd:cd17946   81 AVQVKDHLKAIAKYTNI--KIASIVGGLAVQKQ-ERLLKKRPEIVVATPGRLWELIQEGNehLAnLKSLRFLVLDEADRM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285213 159 LDMGFLETVDKIADSLPKD-------LQFMVFSATIPQKLQPFLKKyLSNPVMEKIKTKTVISDTID 218
Cdd:cd17946  158 LEKGHFAELEKILELLNKDragkkrkRQTFVFSATLTLDHQLPLKL-NSKKKKKKKEKKQKLELLIE 223
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
12-204 3.15e-34

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: 126.81  E-value: 3.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLD------EASDSVQAVITAPSRELATQI 85
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqpiprEQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  86 YQvarQISAHSDVEVRVVNYVGGTDKARQIEKLESNqPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLE 165
Cdd:cd17958   81 EA---ECSKYSYKGLKSVCVYGGGNRNEQIEDLSKG-VDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEP 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 444285213 166 TVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVM 204
Cdd:cd17958  157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMI 195
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
14-209 3.05e-33

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: 125.17  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  14 EALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL--DEASDSVQ-----AVITAPSRELATQIY 86
Cdd:cd17948    3 EILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaprGLVITPSRELAEQIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  87 QVARQISAHSDVEVRVVnyVGGTDKaRQIEKLESNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLET 166
Cdd:cd17948   83 SVAQSLTEGLGLKVKVI--TGGRTK-RQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 444285213 167 VDKI-------------ADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIKT 209
Cdd:cd17948  160 LSHFlrrfplasrrsenTDGLDPGTQLVLVSATMPSGVGEVLSKVIDVDSIETVTS 215
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
19-206 2.45e-32

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: 121.92  E-value: 2.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  19 LKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQ------AVITAPSRELATQIYQVARQI 92
Cdd:cd17949    9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  93 sahsdveVR-----VVNYV-GGT----DKARqIEKLESnqphIVIGTPGRIYDLVKSGD-LAIHKAKTFVVDEADMTLDM 161
Cdd:cd17949   89 -------LKpfhwiVPGYLiGGEkrksEKAR-LRKGVN----ILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDM 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 444285213 162 GFLETVDKI-------------ADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEK 206
Cdd:cd17949  157 GFEKDITKIlellddkrskaggEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
27-199 1.07e-27

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: 109.17  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  27 VQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASD------SVQAVITAPSRELATQIYQVARQISAhsdvEV 100
Cdd:cd17944   16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITR----KL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 101 RVVNYVGGTDKARQIEKLEsNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKI-ADSLPKDL- 178
Cdd:cd17944   92 SVACFYGGTPYQQQIFAIR-NGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlSVSYKKDSe 170
                        170       180
                 ....*....|....*....|....
gi 444285213 179 ---QFMVFSATIPQKLQPFLKKYL 199
Cdd:cd17944  171 dnpQTLLFSATCPDWVYNVAKKYM 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
228-337 1.06e-25

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: 100.75  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  228 DKNAQIYQLTQSMQPYLAMIFVNTKTRADElHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGID 307
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 444285213  308 IEGVSHVINDAIPQDLSFFVHRVGRTGRNG 337
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
2-208 3.05e-25

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: 103.18  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAG--RDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSR 79
Cdd:cd18048   19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSdVEVRVVNYVGGT--DKARQIEKlesnqpHIVIGTPGRIYD-LVKSGDLAIHKAKTFVVDEAD 156
Cdd:cd18048   99 ELALQTGKVVEEMGKFC-VGIQVIYAIRGNrpGKGTDIEA------QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEAD 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 444285213 157 MTLDM-GFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNPVMEKIK 208
Cdd:cd18048  172 VMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLK 224
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
12-202 2.60e-24

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: 100.40  E-value: 2.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAG---------RDLVGESKTGSGKTHTFLLPIFQQLDEASD-SVQAVITAPSREL 81
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVpRLRALIVVPTKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  82 ATQIYQVARQISAHSDveVRVVNYVGGTD---KARQIEKLESNQ----PHIVIGTPGRIYDLVKSGD-LAIHKAKTFVVD 153
Cdd:cd17956   81 VQQVYKVFESLCKGTG--LKVVSLSGQKSfkkEQKLLLVDTSGRylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLVID 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285213 154 EADMTLDMGF---LETVDK-----------------IADSLPKDLQFMVFSATI---PQKLQpFLKkyLSNP 202
Cdd:cd17956  159 EADRLLNQSFqdwLETVMKalgrptapdlgsfgdanLLERSVRPLQKLLFSATLtrdPEKLS-SLK--LHRP 227
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
2-202 8.70e-22

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: 92.86  E-value: 8.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEVQDKLIPIVLAG--RDLVGESKTGSGKTHTFLLPIFQQLDEASDSVQAVITAPSR 79
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  80 ELATQIYQVARQISAHSDvEVRVVNYVGGtdkaRQIEKLESNQPHIVIGTPGRIYD-LVKSGDLAIHKAKTFVVDEAD-M 157
Cdd:cd18047   82 ELALQTGKVIEQMGKFYP-ELKLAYAVRG----NKLERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADvM 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 444285213 158 TLDMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKKYLSNP 202
Cdd:cd18047  157 IATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
HELICc smart00490
helicase superfamily c-terminal domain;
256-337 1.31e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.42  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   256 DELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGR 335
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 444285213   336 NG 337
Cdd:smart00490  81 AG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
12-197 7.09e-17

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: 80.11  E-value: 7.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKE------LKFTT---PTEVQDKLIPIVL---AGRDLVGESK-------------TGSGKTHTFLLPIFQQL--D 64
Cdd:cd17965   10 VREAIIKeilkgsNKTDEeikPSPIQTLAIKKLLktlMRKVTKQTSNeepklevfllaaeTGSGKTLAYLAPLLDYLkrQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  65 EASDS---------------VQAVITAPSRELATQIYQVARQISAHSDVEVRVVNYVGGTDKaRQIEKLESNQPHIVIGT 129
Cdd:cd17965   90 EQEPFeeaeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSY-QRLQLAFKGRIDILVTT 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285213 130 PGRIYDLVKSGDLAIHKAKTFVVDEADMTLDMGFLETVDKIADSLPKDLQFMVFSATIPQKLQPFLKK 197
Cdd:cd17965  169 PGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRK 236
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
44-186 4.05e-16

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: 75.13  E-value: 4.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  44 ESKTGSGKTHTFLLPIFQQLDEASDsvQAVITAPSRELATQIYQVARQISAHSdveVRVVNYVGGTDKARQiEKLESNQP 123
Cdd:cd00046    7 TAPTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRELFGPG---IRVAVLVGGSSAEER-EKNKLGDA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285213 124 HIVIGTPGRIYDLVKSGDLA-IHKAKTFVVDEADMTLDMGFLETVDKIAD--SLPKDLQFMVFSAT 186
Cdd:cd00046   81 DIIIATPDMLLNLLLREDRLfLKDLKLIIVDEAHALLIDSRGALILDLAVrkAGLKNAQVILLSAT 146
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
247-346 2.16e-11

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: 61.07  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 247 IFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFF 326
Cdd:cd18794   35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESY 114
                         90       100
                 ....*....|....*....|
gi 444285213 327 VHRVGRTGRNGLPGTAITLY 346
Cdd:cd18794  115 YQESGRAGRDGLPSECILFY 134
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-444 2.28e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 65.82  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213   2 SFTKFQFKNYIREALKELKFTTPTEvQDKLIpIVLAgrdlvgeskTGSGKTHTFLLPIfqqlDEASDSVQAVITAPSREL 81
Cdd:COG1061   75 SGTSFELRPYQQEALEALLAALERG-GGRGL-VVAP---------TGTGKTVLALALA----AELLRGKRVLVLVPRREL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  82 ATQIYQVARqisahsdvevRVVNYVGGTDKARQIEKlesnqpHIVIGTpgriYDLVKSGDL--AIHKAKTFVV-DEADMT 158
Cdd:COG1061  140 LEQWAEELR----------RFLGDPLAGGGKKDSDA------PITVAT----YQSLARRAHldELGDRFGLVIiDEAHHA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 159 LDMGFLETVDKI--------------ADSLPKDLQF---MVFSATIPQKL-QPFLKKY----LSNPVMEKIKTKTVISDT 216
Cdd:COG1061  200 GAPSYRRILEAFpaayrlgltatpfrSDGREILLFLfdgIVYEYSLKEAIeDGYLAPPeyygIRVDLTDERAEYDALSER 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 217 IDNWLIStkGHDKNAQIYQ--LTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFE 294
Cdd:COG1061  280 LREALAA--DAERKDKILRelLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 295 YIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLYqpsD--DSDIRELEKLGIKFSPKMVKDG 372
Cdd:COG1061  358 ILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVY---DfvGNDVPVLEELAKDLRDLAGYRV 434
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285213 373 EFQDTYDRDRRANREKKQDKLDIEMIGLVKKKKKKVKPGYKKKIQWAVDEKRRKTKRAENRARGRAERKAKR 444
Cdd:COG1061  435 EFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAE 506
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
227-401 2.31e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 65.55  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 227 HDKNAQIYQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATdlAA--R 304
Cdd:COG0514  215 DDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAfgM 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 305 GIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLYQPSDDsDIREleklgikfspKMVKDGEFqdtyDRDRRA 384
Cdd:COG0514  293 GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV-AIQR----------FFIEQSPP----DEERKR 357
                        170
                 ....*....|....*..
gi 444285213 385 NREKKQDkldiEMIGLV 401
Cdd:COG0514  358 VERAKLD----AMLAYA 370
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
232-350 1.20e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 63.58  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 232 QIYQLTQSMQPYLAMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGV 311
Cdd:PRK11057 226 QLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNV 305
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 444285213 312 SHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLYQPSD 350
Cdd:PRK11057 306 RFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD 344
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
12-351 7.13e-10

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 61.00  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASDSvQAVITAPSRELATQIYQVARQ 91
Cdd:COG1205   45 LRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-TALYLYPTKALARDQLRRLRE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  92 ISAHSDVEVRVVNYVGGTDKA--RQIEKlesnQPHIVIGTPgriyDLVKSGDLAIHKA--------KTFVVDEA------ 155
Cdd:COG1205  124 LAEALGLGVRVATYDGDTPPEerRWIRE----HPDIVLTNP----DMLHYGLLPHHTRwarffrnlRYVVIDEAhtyrgv 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 156 ---DMTLdmgFLETVDKIADSLPKDLQFMVFSATI--PQKL------QPFL----------KKY--LSNP-VMEKIKTKT 211
Cdd:COG1205  196 fgsHVAN---VLRRLRRICRHYGSDPQFILASATIgnPAEHaerltgRPVTvvdedgsprgERTfvLWNPpLVDDGIRRS 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 212 VISDTIDnwLISTkghdknaqiyqLTQSMQPYLAmiFVNTKTRADELHSYLTAQ------GLKVAKIHGDIAPRERKRIM 285
Cdd:COG1205  273 ALAEAAR--LLAD-----------LVREGLRTLV--FTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIE 337
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285213 286 NQVQN--LDFeyIVAT---DLaarGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGTAITLyqPSDD 351
Cdd:COG1205  338 RGLRSgeLLG--VVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV--AGDD 401
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
38-154 1.81e-09

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 56.44  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  38 GRDLVGESKTGSGKTHTFLLPIFQQL-DEASDSVQAVITAPSRELATQIYQVARQISAHSDVEVRVVNYVGGT---DKAR 113
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTsqsEKAK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 444285213 114 QIEKLesnqPHIVIGTPGRIYDLV--KSGDLAIHKAKTFVVDE 154
Cdd:cd17922   81 QLKNP----PGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
40-337 1.26e-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: 53.20  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  40 DLVGESKTGSGKTHTFLLPIFQQLDEA-SDSVqaVITAPSRELATQIYQVARQI-----SAHSDVEVRVVNYVGGTDKAR 113
Cdd:cd09639    1 LLVIEAPTGYGKTEAALLWALHSLKSQkADRV--IIALPTRATINAMYRRAKEAfgetgLYHSSILSSRIKEMGDSEEFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 114 QIEKLESNQPHIVIGTPGRIYD---LVKSGDLAIHKAKT---------FVVDEADMTLD--MGFLETV-DKIADslpKDL 178
Cdd:cd09639   79 HLFPLYIHSNDTLFLDPITVCTidqVLKSVFGEFGHYEFtlasianslLIFDEVHFYDEytLALILAVlEVLKD---NDV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 179 QFMVFSATIPQKLQPFLKKYLsnPVMEKiktKTVISDTIDNWLISTKGHDKNAQIYQLTQSMQPYLA----MIFVNTKTR 254
Cdd:cd09639  156 PILLMSATLPKFLKEYAEKIG--YVEEN---EPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKggsvAIIVNTVDR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 255 ADELHSYLTAQGLKVAK--IHGDIAP--RERK--RIMNQVQNLDFEYIVATDLAARGIDIEgVSHVINDAIPQDLsfFVH 328
Cdd:cd09639  231 AQEFYQQLKEKGPEEEImlIHSRFTEkdRAKKeaELLLEFKKSEKFVIVATQVIEASLDIS-VDVMITELAPIDS--LIQ 307

                 ....*....
gi 444285213 329 RVGRTGRNG 337
Cdd:cd09639  308 RLGRLHRYG 316
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
35-187 1.44e-07

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


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 51.43  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  35 VLAGRDLVGESKTGSGKTHTFLLPIFQQLDEASdSVQAVITAPSRELATQIYQVARQISAHSDVEVRVVNYVGGTDKARQ 114
Cdd:cd17923   12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVATYDGDTPREER 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 115 iEKLESNQPHIVIGTPGRI-YDLVKSGDLAIH---KAKTFVVDEA---------DMTLdmgFLETVDKIADSLPKDLQFM 181
Cdd:cd17923   91 -RAIIRNPPRILLTNPDMLhYALLPHHDRWARflrNLRYVVLDEAhtyrgvfgsHVAL---LLRRLRRLCRRYGADPQFI 166

                 ....*.
gi 444285213 182 VFSATI 187
Cdd:cd17923  167 LTSATI 172
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
47-189 7.65e-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: 49.18  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  47 TGSGKTHTFLLPIFQQLdEASDSVqAVITAPSRELATQIYQVARQISAHSdvEVRVVNYVGGTdkarQIEKLESNQPHIV 126
Cdd:cd17921   26 TSSGKTLIAELAILRAL-ATSGGK-AVYIAPTRALVNQKEADLRERFGPL--GKNVGLLTGDP----SVNKLLLAEADIL 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285213 127 IGTPgRIYDLV--KSGDLAIHKAKTFVVDEADM--------TLDmgflETVDKIADSLPKdLQFMVFSATIPQ 189
Cdd:cd17921   98 VATP-EKLDLLlrNGGERLIQDVRLVVVDEAHLigdgergvVLE----LLLSRLLRINKN-ARFVGLSATLPN 164
PRK13767 PRK13767
ATP-dependent helicase; Provisional
11-130 1.07e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 51.04  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  11 YIREALKElKFTTPTEVQDKLIPIVLAGRDLVGESKTGSGKTHTFLLPIFQQL------DEASDSVQAVITAPSRELA-- 82
Cdd:PRK13767  21 YVREWFKE-KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrlgreGELEDKVYCLYVSPLRALNnd 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  83 ---------TQIYQVARQISAHSDvEVRVVNYVGGT---DKARQIEKlesnQPHIVIGTP 130
Cdd:PRK13767 100 ihrnleeplTEIREIAKERGEELP-EIRVAIRTGDTssyEKQKMLKK----PPHILITTP 154
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
251-336 2.84e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 47.24  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 251 TKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHV-INDA----IPQDLSF 325
Cdd:cd18790   36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDAdkegFLRSETS 115
                         90
                 ....*....|.
gi 444285213 326 FVHRVGRTGRN 336
Cdd:cd18790  116 LIQTIGRAARN 126
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
279-346 1.78e-05

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: 42.69  E-value: 1.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285213 279 RERKRIMNQvqnldFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNG-LPGTAITLY 346
Cdd:cd18785   14 EHAEEIASS-----LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
12-154 3.39e-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: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  12 IREALKELKFTtPTEVQDKLIPIVLAG------RDLVGESKTGSGKTHTFLLPIFqqlDEASDSVQAVITAPSRELATQI 85
Cdd:cd17918    5 IQELCKSLPFS-LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAAL---LAYKNGKQVAILVPTEILAHQH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285213  86 YQVARQISAhsdvEVRVVNYVGGTDkarqiEKLESnQPHIVIGTPGRIYDLVKSGDLAIhkaktFVVDE 154
Cdd:cd17918   81 YEEARKFLP----FINVELVTGGTK-----AQILS-GISLLVGTHALLHLDVKFKNLDL-----VIVDE 134
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
11-130 3.43e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 46.25  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  11 YIREALKElKFTTPTEVQDKLIPIVLAGRD-LVgESKTGSGKTHTFLLPIFQQL------DEASDSVQAV-IT------- 75
Cdd:COG1201   13 AVRAWFAA-RFGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELarrprpGELPDGLRVLyISplkalan 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285213  76 -------APSRELATQIYQVARQISahsdVEVRvvnyVGGT---DKARQIEKLesnqPHIVIGTP 130
Cdd:COG1201   91 diernlrAPLEEIGEAAGLPLPEIR----VGVR----TGDTpasERQRQRRRP----PHILITTP 143
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
247-335 4.70e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.41  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 247 IFVNTKTRADELHSYL------TAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVAT---DLaarGIDIEGVSHVIND 317
Cdd:cd18796   43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATsslEL---GIDIGDVDLVIQI 119
                         90
                 ....*....|....*...
gi 444285213 318 AIPQDLSFFVHRVGRTGR 335
Cdd:cd18796  120 GSPKSVARLLQRLGRSGH 137
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
35-188 6.24e-05

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 43.48  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  35 VLAGRDLVGESKTGSGKThtfLLPIFQQLDEASDSVQAVITAPSRELATQIYqvaRQISAHSDVEVRVVNYVGgtDKARQ 114
Cdd:cd18028   14 LLKGENLLISIPTASGKT---LIAEMAMVNTLLEGGKALYLVPLRALASEKY---EEFKKLEEIGLKVGISTG--DYDED 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285213 115 IEKLESNqpHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEADMTLDM---GFLETVDKIADSLPKDLQFMVFSATIP 188
Cdd:cd18028   86 DEWLGDY--DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEergPTLESIVARLRRLNPNTQIIGLSATIG 160
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
47-155 1.20e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.02  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  47 TGSGKTHTFLLPI----FQQLDEASDSVQAVITAPSRELATQIYQVARQisaHSDVEVRVvnYVGGTDK---ARQIEKLE 119
Cdd:cd18034   25 TGSGKTLIAVMLIkemgELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRS---HTDLKVGE--YSGEMGVdkwTKERWKEE 99
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 444285213 120 SNQPHIVIGTPGRIYDLVKSGDLAIHKAKTFVVDEA 155
Cdd:cd18034  100 LEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
247-316 2.36e-04

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: 40.92  E-value: 2.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285213 247 IFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRERKRIMNQVQNLD--FEYIVATDLAARGIDIEGVSHVIN 316
Cdd:cd18793   32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVIL 103
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
245-308 3.23e-04

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: 40.24  E-value: 3.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285213 245 AMIFVNTKTRADELHSYLTAQGLKVAKIHGDIAPRER---KRIMNQVQNLDFEYIVATDLAARGIDI 308
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDI 75
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
267-349 3.60e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.79  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 267 LKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSH-VINDAIPQDLSFFVHRVGRTGRNGLPGTAITL 345
Cdd:cd18810   52 ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTiIIERADKFGLAQLYQLRGRVGRSKERAYAYFL 131

                 ....
gi 444285213 346 YQPS 349
Cdd:cd18810  132 YPDQ 135
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
48-154 4.81e-04

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


Pssm-ID: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 41.36  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  48 GSGKThtfLLPIFQQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEVRVV-NYVGGTDKARQIEKLESNQPHIV 126
Cdd:cd17992   76 GSGKT---VVAALAMLAAVENGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLtGSTKAKEKREILEKIASGEIDIV 152
                         90       100
                 ....*....|....*....|....*...
gi 444285213 127 IGTPGRIYDLVKSGDLAIhkaktFVVDE 154
Cdd:cd17992  153 IGTHALIQEDVEFHNLGL-----VIIDE 175
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
248-343 6.84e-04

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 39.93  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 248 FVNTKTRADELHSYLTAQGLKVAKIHGDIA-------PRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIP 320
Cdd:cd18797   41 FCRSRKLAELLLRYLKARLVEEGPLASKVAsyragylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYP 120
                         90       100
                 ....*....|....*....|...
gi 444285213 321 QDLSFFVHRVGRTGRNGLPGTAI 343
Cdd:cd18797  121 GSLASLWQQAGRAGRRGKDSLVI 143
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
245-337 8.62e-04

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 41.64  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 245 AMIFVNTKTRADELHSYLTAQGLKVAKIHGDiAPRERKRIMNQVQNL---------DFEYIVATDLAARGIDIEGVSHVI 315
Cdd:COG1111  356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQ-ASKEGDKGLTQKEQIeilerfragEFNVLVATSVAEEGLDIPEVDLVI 434
                         90       100
                 ....*....|....*....|...
gi 444285213 316 N-DAIPQDLSfFVHRVGRTGRNG 337
Cdd:COG1111  435 FyEPVPSEIR-SIQRKGRTGRKR 456
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
262-350 3.38e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 39.88  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  262 LTAQGLKVAKIHGDIAPRERKRIMNQVQNLDFEYIVATDLAARGIDIEGVSHVINDAIPQDLSFFVHRVGRTGRNGLPGT 341
Cdd:PLN03137  700 LQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSS 779

                  ....*....
gi 444285213  342 AITLYQPSD 350
Cdd:PLN03137  780 CVLYYSYSD 788
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
37-187 4.58e-03

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


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 38.08  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  37 AGRDLVGES-----KTGSGKThTFLLPIfqQLDEASDSVQAVITAPSRELATQIYQVARQISAHSDVEVRVVNYVGGTDK 111
Cdd:cd17924   26 AKRLLRGKSfaiiaPTGVGKT-TFGLAT--SLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSRLKK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 112 ARQ---IEKLESNQPHIVIGTPGRIYDLVKSgdLAIHKAKTFVVDEADMTLDMGfletvdKIADSLPKDLQF---MVFSA 185
Cdd:cd17924  103 KEKeelLEKIEKGDFDILVTTNQFLSKNFDL--LSNKKFDFVFVDDVDAVLKSS------KNIDRLLKLLGFgqlVVSSA 174

                 ..
gi 444285213 186 TI 187
Cdd:cd17924  175 TG 176
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
48-154 5.18e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 39.36  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213  48 GSGKTHTFLLPIFQqldeASDS-VQAVITAPSRELATQIYQVARQISAHSDVEVRVVnyVGGT---DKARQIEKLESNQP 123
Cdd:PRK10917 292 GSGKTVVAALAALA----AIEAgYQAALMAPTEILAEQHYENLKKLLEPLGIRVALL--TGSLkgkERREILEAIASGEA 365
                         90       100       110
                 ....*....|....*....|....*....|.
gi 444285213 124 HIVIGTPGRIYDLVKSGDLAIhkaktFVVDE 154
Cdd:PRK10917 366 DIVIGTHALIQDDVEFHNLGL-----VIIDE 391
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
227-335 9.93e-03

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: 36.56  E-value: 9.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285213 227 HDKNAQIYQLTQsmqpylAMIFVNTKTRADELHSYLTAQGLKV-AKIHGDIAPRERKRIMNQVQNLD---------FEYI 296
Cdd:cd18801   21 HFKKKQEGSDTR------VIIFSEFRDSAEEIVNFLSKIRPGIrATRFIGQASGKSSKGMSQKEQKEvieqfrkggYNVL 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 444285213 297 VATDLAARGIDIEGVSHVI-NDAIPQDLSfFVHRVGRTGR 335
Cdd:cd18801   95 VATSIGEEGLDIGEVDLIIcYDASPSPIR-MIQRMGRTGR 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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