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Conserved domains on  [gi|4689114|gb|AAD27766|]
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putative ATP-dependent RNA helicase ROK1 [Homo sapiens]

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];
162-532 2.81e-108

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 331.73  E-value: 2.81e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIIS 241
Cdd:COG0513   3 SFADL----GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  242 PTRELASQIHRELIKISEGTGFRIHMIH-----KAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLV 316
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYggvsiGRQIRALKRGV------DIVVATPGRLLDLIERG--ALDLSGVETLV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  317 VDESDKLLKM-----------------QTGsetswlpfswpahptrseepMFSATFAYDVEQWCNSTwtMSSvcP----L 375
Cdd:COG0513 151 LDEADRMLDMgfiedierilkllpkerQTL--------------------LFSATMPPEIRKLAKRY--LKN--PvrieV 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  376 EARNSAVETVEQELLFVGSETgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVH 455
Cdd:COG0513 207 APENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALD 285
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114  456 SFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 532
Cdd:COG0513 286 AFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ 362
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
162-532 2.81e-108

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 331.73  E-value: 2.81e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIIS 241
Cdd:COG0513   3 SFADL----GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  242 PTRELASQIHRELIKISEGTGFRIHMIH-----KAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLV 316
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYggvsiGRQIRALKRGV------DIVVATPGRLLDLIERG--ALDLSGVETLV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  317 VDESDKLLKM-----------------QTGsetswlpfswpahptrseepMFSATFAYDVEQWCNSTwtMSSvcP----L 375
Cdd:COG0513 151 LDEADRMLDMgfiedierilkllpkerQTL--------------------LFSATMPPEIRKLAKRY--LKN--PvrieV 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  376 EARNSAVETVEQELLFVGSETgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVH 455
Cdd:COG0513 207 APENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALD 285
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114  456 SFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 532
Cdd:COG0513 286 AFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ 362
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
176-365 7.40e-90

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: 276.01  E-value: 7.40e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-ANKGFRALIISPTRELASQIHREL 254
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPrKKKGLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  255 IKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKM----QTGS 330
Cdd:cd17957  81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP--IDLSSVEYLVLDEADKLFEPgfreQTDE 158
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4689114  331 etswlpfSWPA--HP--TRSeepMFSATFAYDVEQWCNS 365
Cdd:cd17957 159 -------ILAActNPnlQRS---LFSATIPSEVEELARS 187
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
129-538 5.61e-67

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 226.98  E-value: 5.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   129 SGKLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLAS 208
Cdd:PLN00206  89 PGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSC----GLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   209 APTGSGKTLAFSIPILMQLKQ------PANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFgPKS 282
Cdd:PLN00206 165 ADTGSGKTASFLVPIISRCCTirsghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL-YRI 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   283 SKKFDILVTTPNRLIYLL-KQDppgIDLASVEWLVVDESDKLLkmQTGSETSWLPFSWP-AHPtrsEEPMFSATFAYDVE 360
Cdd:PLN00206 244 QQGVELIVGTPGRLIDLLsKHD---IELDNVSVLVLDEVDCML--ERGFRDQVMQIFQAlSQP---QVLLFSATVSPEVE 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   361 QWCNSTWTMSSVCPLEARNSAVETVEQELLFVGSETGKLLAVRELVKKG-FNPPVLVFVQSIERAkELFHELI--YEGIN 437
Cdd:PLN00206 316 KFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhFKPPAVVFVSSRLGA-DLLANAItvVTGLK 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   438 VDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTE 517
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
                        410       420
                 ....*....|....*....|.
gi 4689114   518 DDKPLLRSVANVIQQAGCPVP 538
Cdd:PLN00206 475 EDRNLFPELVALLKSSGAAIP 495
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
189-361 5.48e-37

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 135.06  E-value: 5.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    189 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPaNKGFRALIISPTRELASQIHRELIKISEGTGFRIHMI 268
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL-DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    269 HKAAVAAKKFgpKSSKKFDILVTTPNRLIYLLKQDPpgiDLASVEWLVVDESDKLLKMQTGSETSWLPFSWPAHPTRSee 348
Cdd:pfam00270  80 LGGDSRKEQL--EKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL-- 152
                         170
                  ....*....|...
gi 4689114    349 pMFSATFAYDVEQ 361
Cdd:pfam00270 153 -LLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
180-388 8.43e-37

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 136.08  E-value: 8.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114     180 ILDAGFQMPTPIQMQAIPVMLHG-RELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELASQIHRELIKIS 258
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR--GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114     259 EGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQTGSETSWLPFS 338
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 4689114     339 WPAHPTRSeepMFSATFAYDVEQwcNSTWTMSSVCPLEARNSAVETVEQE 388
Cdd:smart00487 157 LPKNVQLL---LLSATPPEEIEN--LLELFLNDPVFIDVGFTPLEPIEQF 201
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
188-512 1.01e-15

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 80.67  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHRELIKISEGTG-- 262
Cdd:TIGR04121  14 PRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLagpEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlp 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    263 FRIHM------IHKAAvAAKKFGPksskkfDILVTTPNRLIYLLKQ-DPPGI--DLASVewlVVDESDKLLKMQTGSET- 332
Cdd:TIGR04121  94 IRVETrtgdtsSSERA-RQRKKPP------DILLTTPESLALLLSYpDAARLfkDLRCV---VVDEWHELAGSKRGDQLe 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    333 ---SWLpfswpahptRSEEPMF-----SATFAyDVEQWCN-----STWTMSSVCPLEARNSAVETV--EQELLFVGSETG 397
Cdd:TIGR04121 164 lalARL---------RRLAPGLrrwglSATIG-NLEEARRvllgvGGAPAVLVRGKLPKAIEVISLlpESEERFPWAGHL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    398 KLLAVRELVKK-GFNPPVLVFVQSIERAKELFHELIYegINVD---VI---HAERTQQQRDNTVHSFRAGKIWVLICTAL 470
Cdd:TIGR04121 234 GLRALPEVYAEiDQARTTLVFTNTRSQAELWFQALWE--ANPEfalPIalhHGSLDREQRRWVEAAMAAGRLRAVVCTSS 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 4689114    471 LARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG-RAGNKGKAI 512
Cdd:TIGR04121 312 LDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL 354
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
162-532 2.81e-108

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 331.73  E-value: 2.81e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIIS 241
Cdd:COG0513   3 SFADL----GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  242 PTRELASQIHRELIKISEGTGFRIHMIH-----KAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLV 316
Cdd:COG0513  79 PTRELALQVAEELRKLAKYLGLRVATVYggvsiGRQIRALKRGV------DIVVATPGRLLDLIERG--ALDLSGVETLV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  317 VDESDKLLKM-----------------QTGsetswlpfswpahptrseepMFSATFAYDVEQWCNSTwtMSSvcP----L 375
Cdd:COG0513 151 LDEADRMLDMgfiedierilkllpkerQTL--------------------LFSATMPPEIRKLAKRY--LKN--PvrieV 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  376 EARNSAVETVEQELLFVGSETgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVH 455
Cdd:COG0513 207 APENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALD 285
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114  456 SFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 532
Cdd:COG0513 286 AFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ 362
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
176-365 7.40e-90

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: 276.01  E-value: 7.40e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-ANKGFRALIISPTRELASQIHREL 254
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPrKKKGLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  255 IKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKM----QTGS 330
Cdd:cd17957  81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP--IDLSSVEYLVLDEADKLFEPgfreQTDE 158
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4689114  331 etswlpfSWPA--HP--TRSeepMFSATFAYDVEQWCNS 365
Cdd:cd17957 159 -------ILAActNPnlQRS---LFSATIPSEVEELARS 187
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
129-538 5.61e-67

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 226.98  E-value: 5.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   129 SGKLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLAS 208
Cdd:PLN00206  89 PGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSC----GLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVS 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   209 APTGSGKTLAFSIPILMQLKQ------PANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFgPKS 282
Cdd:PLN00206 165 ADTGSGKTASFLVPIISRCCTirsghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL-YRI 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   283 SKKFDILVTTPNRLIYLL-KQDppgIDLASVEWLVVDESDKLLkmQTGSETSWLPFSWP-AHPtrsEEPMFSATFAYDVE 360
Cdd:PLN00206 244 QQGVELIVGTPGRLIDLLsKHD---IELDNVSVLVLDEVDCML--ERGFRDQVMQIFQAlSQP---QVLLFSATVSPEVE 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   361 QWCNSTWTMSSVCPLEARNSAVETVEQELLFVGSETGKLLAVRELVKKG-FNPPVLVFVQSIERAkELFHELI--YEGIN 437
Cdd:PLN00206 316 KFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhFKPPAVVFVSSRLGA-DLLANAItvVTGLK 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   438 VDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTE 517
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
                        410       420
                 ....*....|....*....|.
gi 4689114   518 DDKPLLRSVANVIQQAGCPVP 538
Cdd:PLN00206 475 EDRNLFPELVALLKSSGAAIP 495
PTZ00110 PTZ00110
helicase; Provisional
134-538 7.79e-66

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 224.65  E-value: 7.79e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   134 NLRKEKINFLRNKHKIH-VQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTG 212
Cdd:PTZ00110 102 ALSSKEVDEIRKEKEITiIAGENVPKPVVSFE----YTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETG 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   213 SGKTLAFSIPILMQLK-QPANK---GFRALIISPTRELASQIHRELIKIseGTGFRIHmiHKAAvaakkFG--PKSSKKF 286
Cdd:PTZ00110 178 SGKTLAFLLPAIVHINaQPLLRygdGPIVLVLAPTRELAEQIREQCNKF--GASSKIR--NTVA-----YGgvPKRGQIY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   287 ------DILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMqtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVE 360
Cdd:PTZ00110 249 alrrgvEILIACPGRLIDFLESNV--TNLRRVTYLVLDEADRMLDM--GFEPQIRKIVSQIRPDR-QTLMWSATWPKEVQ 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   361 QW----CNSTWTMSSVCPLEARnsAVETVEQELlFVGSETGKLLAVRELVKKGF--NPPVLVFVQSIERAKELFHELIYE 434
Cdd:PTZ00110 324 SLardlCKEEPVHVNVGSLDLT--ACHNIKQEV-FVVEEHEKRGKLKMLLQRIMrdGDKILIFVETKKGADFLTKELRLD 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   435 GINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITF 514
Cdd:PTZ00110 401 GWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTF 480
                        410       420
                 ....*....|....*....|....
gi 4689114   515 FTEDDKPLLRSVANVIQQAGCPVP 538
Cdd:PTZ00110 481 LTPDKYRLARDLVKVLREAKQPVP 504
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
162-598 3.01e-63

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 214.42  E-value: 3.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPankGF- 235
Cdd:PRK11192   2 TFSELE----LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprRKS---GPp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   236 RALIISPTRELASQIHRELIKISEGTGFRIHMIhKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWL 315
Cdd:PRK11192  75 RILILTPTRELAMQVADQARELAKHTHLDIATI-TGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE--NFDCRAVETL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   316 VVDESDKLLKMQTGS-------ETSWlpfswpahptRSEEPMFSATfaydveqwcnstwtmssvcpLEArnSAVETVEQE 388
Cdd:PRK11192 152 ILDEADRMLDMGFAQdietiaaETRW----------RKQTLLFSAT--------------------LEG--DAVQDFAER 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   389 LL----FVGSETG---------------------KLLA---VRELVKKGFnppvlVFVQSIERAKELFHELIYEGINVDV 440
Cdd:PRK11192 200 LLndpvEVEAEPSrrerkkihqwyyraddlehktALLChllKQPEVTRSI-----VFVRTRERVHELAGWLRKAGINCCY 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   441 IHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDK 520
Cdd:PRK11192 275 LEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDH 354
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4689114   521 PLLRSVANVIQQagcPV-PEYIKGFQKLLSKQKKKMIKKPlereSISTTPKCFLEKAKDKQKKvtgqnsKKKVALEDKS 598
Cdd:PRK11192 355 LLLGKIERYIEE---PLkARVIDELRPKTKAPSEKKTGKP----SKKVLAKRAEKKEKEKEKP------KVKKRHRDTK 420
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
172-532 1.67e-61

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 210.43  E-value: 1.67e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPANKG---FRALIISPTREL 246
Cdd:PRK10590   8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGrrpVRALILTPTREL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   247 ASQIHRELIKISEGTGFRiHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKM 326
Cdd:PRK10590  88 AAQIGENVRDYSKYLNIR-SLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN--AVKLDQVEILVLDEADRMLDM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   327 QTGSETSWLPFSWPAhptRSEEPMFSATFAYDVEQWCNSTWTMSSVCPLEARNSAVETVEQELLFVGSE-TGKLLAvrEL 405
Cdd:PRK10590 165 GFIHDIRRVLAKLPA---KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKrKRELLS--QM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   406 VKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVIN 485
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 4689114   486 YDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 532
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
168-538 2.81e-61

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 210.54  E-value: 2.81e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ--PANKGF----RALIIS 241
Cdd:PRK01297  90 HDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpPPKERYmgepRALIIA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   242 PTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDLasVEWLVVDESD 321
Cdd:PRK01297 170 PTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDM--VEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   322 KLLKMQTGSETSWLPFSWPaHPTRSEEPMFSATFAYDV----EQWCnstwTMSSVCPLEARNSAVETVEQELLFV-GSET 396
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTP-RKEERQTLLFSATFTDDVmnlaKQWT----TDPAIVEIEPENVASDTVEQHVYAVaGSDK 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   397 GKLLavRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGID 476
Cdd:PRK01297 323 YKLL--YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4689114   477 FKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVI-QQAGCPVP 538
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgRKISCEMP 463
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
385-515 9.05e-57

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: 187.33  E-value: 9.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  385 VEQELLFVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWV 464
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4689114  465 LICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFF 515
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
176-365 1.03e-53

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: 181.49  E-value: 1.03e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHR 252
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  253 ELIKISEGTGFRIHMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQTGSET 332
Cdd:cd00268  81 VARKLGKGTGLKVAAIY-GGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK--LDLSNVKYLVLDEADRMLDMGFEEDV 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4689114  333 SWLpfswpAHPTRSEEP--MFSATFAYDVEQWCNS 365
Cdd:cd00268 158 EKI-----LSALPKDRQtlLFSATLPEEVKELAKK 187
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
176-519 3.54e-50

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 180.00  E-value: 3.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQIHREL- 254
Cdd:PRK11776  15 LLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRFRVQALVLCPTRELADQVAKEIr 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   255 --------IKI---SEGTGFRI------HMIHkaavaakkfgpksskkfdILVTTPNRLIYLLKQDppGIDLASVEWLVV 317
Cdd:PRK11776  94 rlarfipnIKVltlCGGVPMGPqidsleHGAH------------------IIVGTPGRILDHLRKG--TLDLDALNTLVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   318 DESDKLLKM-----------QTgsetswlpfswpahPTRSEEPMFSATFAYDVEQWcnSTWTMSSvcPLEARNSAVE--- 383
Cdd:PRK11776 154 DEADRMLDMgfqdaidaiirQA--------------PARRQTLLFSATYPEGIAAI--SQRFQRD--PVEVKVESTHdlp 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   384 TVEQELLFVgSETGKLLAVRELVKKgFNP-PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKI 462
Cdd:PRK11776 216 AIEQRFYEV-SPDERLPALQRLLLH-HQPeSCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSC 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114   463 WVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDD 519
Cdd:PRK11776 294 SVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE 350
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
154-517 9.26e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 175.91  E-value: 9.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   154 TDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL------ 227
Cdd:PRK04537   2 SDKPLTDLTFSSFD----LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpal 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   228 --KQPANKgfRALIISPTRELASQIHRELIKISEGTGFRIHMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPP 305
Cdd:PRK04537  78 adRKPEDP--RALILAPTRELAIQIHKDAVKFGADLGLRFALVY-GGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   306 gIDLASVEWLVVDESDKLLKMQTGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQWCNSTWTMSSVCPLEARNSAVETV 385
Cdd:PRK04537 155 -VSLHACEICVLDEADRMFDLGFIKDIRFLLRRMPERGTR-QTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   386 EQELLFVGSETgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVL 465
Cdd:PRK04537 233 RQRIYFPADEE-KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEIL 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4689114   466 ICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTE 517
Cdd:PRK04537 312 VATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE 363
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
172-526 6.24e-46

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 171.57  E-value: 6.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELASQIH 251
Cdd:PRK11634  13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-PELKAPQILVLAPTRELAVQVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   252 RELikisegTGFRIHMIHKAAVA------------AKKFGPKsskkfdILVTTPNRLIYLLKQDPpgIDLASVEWLVVDE 319
Cdd:PRK11634  92 EAM------TDFSKHMRGVNVVAlyggqrydvqlrALRQGPQ------IVVGTPGRLLDHLKRGT--LDLSKLSGLVLDE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   320 SDKLLKMQTGSETSWLPFSWPA-HPTrseePMFSATFAYDVEQWCNStwTMSSvcPLEAR-NSAVET---VEQELLFVGS 394
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEgHQT----ALFSATMPEAIRRITRR--FMKE--PQEVRiQSSVTTrpdISQSYWTVWG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   395 ETGKLLAVRELVKKGFNPPVlVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARG 474
Cdd:PRK11634 230 MRKNEALVRFLEAEDFDAAI-IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARG 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4689114   475 IDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSV 526
Cdd:PRK11634 309 LDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNI 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
172-518 1.72e-42

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 158.21  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAF-----------SIPILMQLKQPankgfRALII 240
Cdd:PRK04837  15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFltatfhyllshPAPEDRKVNQP-----RALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   241 SPTRELASQIHRELIKISEGTGFrihmihKAAVAakkFGPKSSKK--------FDILVTTPNRLIYLLKQDPpgIDLASV 312
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGL------KLGLA---YGGDGYDKqlkvlesgVDILIGTTGRLIDYAKQNH--INLGAI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   313 EWLVVDESDKLLKMQTGSETSWLPFSWPAhPTRSEEPMFSATFAYDV-----EQWCNSTWTmsSVCPLEARNSAVetveQ 387
Cdd:PRK04837 159 QVVVLDEADRMFDLGFIKDIRWLFRRMPP-ANQRLNMLFSATLSYRVrelafEHMNNPEYV--EVEPEQKTGHRI----K 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   388 ELLFVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 467
Cdd:PRK04837 232 EELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVA 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4689114   468 TALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTED 518
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
PTZ00424 PTZ00424
helicase 45; Provisional
171-528 7.55e-42

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 155.75  E-value: 7.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   171 KINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPANKGFRALIISPTRELASQI 250
Cdd:PTZ00424  34 KLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQALILAPTRELAQQI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   251 HRELIKISEGTGFRIHMIHKAAVAAKKFGpKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLL----KM 326
Cdd:PTZ00424 113 QKVVLALGDYLKVRCHACVGGTVVRDDIN-KLKAGVHMVVGTPGRVYDMIDKRHLRVD--DLKLFILDEADEMLsrgfKG 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   327 QTGSETSWLPfswpahpTRSEEPMFSATFAYDVEQWcnSTWTMSSVCPLEARNS--AVETVEQELLFVGSETGKLLAVRE 404
Cdd:PTZ00424 190 QIYDVFKKLP-------PDVQVALFSATMPNEILEL--TTKFMRDPKRILVKKDelTLEGIRQFYVAVEKEEWKFDTLCD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   405 LVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVI 484
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 4689114   485 NYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVAN 528
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
162-354 7.34e-40

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: 144.37  E-value: 7.34e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLDQEYKinsrLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-ANKGFRALII 240
Cdd:cd17959   2 GFQSMGLSPP----LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHsPTVGARALIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  241 SPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPKSSKKfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDES 320
Cdd:cd17959  78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNP-DIIIATPGRLLHLLVEM--NLKLSSVEYVVFDEA 154
                       170       180       190
                ....*....|....*....|....*....|....
gi 4689114  321 DKLLKMQTGSETSWLPFSWPahPTRsEEPMFSAT 354
Cdd:cd17959 155 DRLFEMGFAEQLHEILSRLP--ENR-QTLLFSAT 185
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
162-361 3.21e-39

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: 143.40  E-value: 3.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFR-- 236
Cdd:cd17967   1 SFEEAG----LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVGRGRrk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  237 ----ALIISPTRELASQIHRELIKISEGTGFRI-------HMIHKAAvaakkfgpKSSKKFDILVTTPNRLIYLLKQDPp 305
Cdd:cd17967  77 aypsALILAPTRELAIQIYEEARKFSYRSGVRSvvvyggaDVVHQQL--------QLLRGCDILVATPGRLVDFIERGR- 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  306 gIDLASVEWLVVDESDKLLKMqtGSEtswlpfswP------AHPTRseeP--------MFSATFAYDVEQ 361
Cdd:cd17967 148 -ISLSSIKFLVLDEADRMLDM--GFE--------PqirkivEHPDM---PpkgerqtlMFSATFPREIQR 203
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
140-361 9.65e-38

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: 140.49  E-value: 9.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  140 INFLRNKH-KIHVQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLA 218
Cdd:cd18052  21 INFDKYDEiPVEVTGRNPPPAILTFE----EANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAA 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  219 FSIPILMQLKQ-----PANKGFR---ALIISPTRELASQIHRELIKISEGTGFRihmihkaAVAAkkFGPKSS------- 283
Cdd:cd18052  97 FLLPVLTGMMKegltaSSFSEVQepqALIVAPTRELANQIFLEARKFSYGTCIR-------PVVV--YGGVSVghqirqi 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  284 -KKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQTGSETSWL--PFSWPAHPTRsEEPMFSATFAYDVE 360
Cdd:cd18052 168 eKGCHILVATPGRLLDFIGRGK--ISLSKLKYLILDEADRMLDMGFGPEIRKLvsEPGMPSKEDR-QTLMFSATFPEEIQ 244

                .
gi 4689114  361 Q 361
Cdd:cd18052 245 R 245
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
189-361 5.48e-37

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 135.06  E-value: 5.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    189 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPaNKGFRALIISPTRELASQIHRELIKISEGTGFRIHMI 268
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL-DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    269 HKAAVAAKKFgpKSSKKFDILVTTPNRLIYLLKQDPpgiDLASVEWLVVDESDKLLKMQTGSETSWLPFSWPAHPTRSee 348
Cdd:pfam00270  80 LGGDSRKEQL--EKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL-- 152
                         170
                  ....*....|...
gi 4689114    349 pMFSATFAYDVEQ 361
Cdd:pfam00270 153 -LLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
180-388 8.43e-37

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 136.08  E-value: 8.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114     180 ILDAGFQMPTPIQMQAIPVMLHG-RELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELASQIHRELIKIS 258
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR--GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114     259 EGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQTGSETSWLPFS 338
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 4689114     339 WPAHPTRSeepMFSATFAYDVEQwcNSTWTMSSVCPLEARNSAVETVEQE 388
Cdd:smart00487 157 LPKNVQLL---LLSATPPEEIEN--LLELFLNDPVFIDVGFTPLEPIEQF 201
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
151-361 2.04e-36

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: 135.58  E-value: 2.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  151 VQGTDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-Q 229
Cdd:cd17953   2 VRGKDCPKPIQKWSQCG----LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  230 PANK---GFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGpKSSKKFDILVTTPNRLIYLLKQDPPG 306
Cdd:cd17953  78 RPVKpgeGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIA-ELKRGAEIVVCTPGRMIDILTANNGR 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4689114  307 I-DLASVEWLVVDESDKLLKMqtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQ 361
Cdd:cd17953 157 VtNLRRVTYVVLDEADRMFDM--GFEPQIMKIVNNIRPDR-QTVLFSATFPRKVEA 209
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
176-360 2.43e-36

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: 135.45  E-value: 2.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVML---------HGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIISPTREL 246
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLpsskstppyRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  247 ASQIHRELIKISEGTGFRIHMIHKAAVAAKK-------FGPKSSKKFDILVTTPNRLIYLLKQdPPGIDLASVEWLVVDE 319
Cdd:cd17956  81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEqklllvdTSGRYLSRVDILVATPGRLVDHLNS-TPGFTLKHLRFLVIDE 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  320 SDKLLK-------------MQTGSETSWLPFSWPAHPTRSEEPM----FSATFAYDVE 360
Cdd:cd17956 160 ADRLLNqsfqdwletvmkaLGRPTAPDLGSFGDANLLERSVRPLqkllFSATLTRDPE 217
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
176-361 4.04e-36

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: 133.92  E-value: 4.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPANKGFRALIISPTRELASQIHRE 253
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyRPKKKAATRVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  254 LIKISEGTGFRIHMI-----HKAAVAAKKFGPksskkfDILVTTPNRLIYLLKqDPPGIDLASVEWLVVDESDKLLKMQT 328
Cdd:cd17947  81 LQQLAQFTDITFALAvgglsLKAQEAALRARP------DIVIATPGRLIDHLR-NSPSFDLDSIEILVLDEADRMLEEGF 153
                       170       180       190
                ....*....|....*....|....*....|....
gi 4689114  329 GSETSWLPFSWPahptRSEEPM-FSATFAYDVEQ 361
Cdd:cd17947 154 ADELKEILRLCP----RTRQTMlFSATMTDEVKD 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
397-506 3.39e-35

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: 128.10  E-value: 3.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    397 GKLLAVRELVKKGFNPPVLVFVQSIERAK-ELFHELiyEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 475
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEaELLLEK--EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 4689114    476 DFKGVNLVINYDFPTSSVEYIHRIGRTGRAG 506
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
176-326 8.32e-33

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: 125.51  E-value: 8.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPA------NKGFRALIISPTRELAS 248
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsRLPPldeetkDDGPYALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  249 QIHRELIKISEGTGFRIHMIhkaaVAAKKF---GPKSSKKFDILVTTPNRLIYLLkqDPPGIDLASVEWLVVDESDKLLK 325
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSI----VGGHSIeeqAFSLRNGCEILIATPGRLLDCL--ERRLLVLNQCTYVVLDEADRMID 154

                .
gi 4689114  326 M 326
Cdd:cd17945 155 M 155
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
176-358 1.06e-32

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: 125.43  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPIL---MQLKQ-----PANKGFRALIISPTREL 246
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILerlLSQKSsngvgGKQKPLRALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  247 ASQIHRELIKISEGTGFRIhMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGID-LASVEWLVVDESDKLLk 325
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKI-ASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnLKSLRFLVLDEADRML- 158
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4689114  326 mQTGS--ETSWLPFSWPAHPTRSEEPM----FSATFAYD 358
Cdd:cd17946 159 -EKGHfaELEKILELLNKDRAGKKRKRqtfvFSATLTLD 196
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
162-331 1.59e-32

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: 123.97  E-value: 1.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpANKGFRALIIS 241
Cdd:cd17954   1 TFKELG----VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE-NPQRFFALVLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  242 PTRELASQIHRELIKISEGTGFR-------IHMIHKAAVAAKKfgPKsskkfdILVTTPNRLIYLLkQDPPGIDLASVEW 314
Cdd:cd17954  76 PTRELAQQISEQFEALGSSIGLKsavlvggMDMMAQAIALAKK--PH------VIVATPGRLVDHL-ENTKGFSLKSLKF 146
                       170
                ....*....|....*..
gi 4689114  315 LVVDESDKLLKMQTGSE 331
Cdd:cd17954 147 LVMDEADRLLNMDFEPE 163
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
172-324 3.04e-32

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: 123.46  E-value: 3.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPIL---MQLKQPANK--GFRALIISPTREL 246
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIqkiLKAKAESGEeqGTRALILVPTREL 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4689114  247 ASQIHRELIKISEGTGFRIHMIHKAA-VAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPgIDLASVEWLVVDESDKLL 324
Cdd:cd17961  81 AQQVSKVLEQLTAYCRKDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSL-LLLSTLKYLVIDEADLVL 158
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
176-327 9.82e-32

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: 121.91  E-value: 9.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPANKGFRALIISPTRELASQIH 251
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkANLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  252 RELIKISEGTGFRIHMI-----HKAAVAAKKFgpkSSKKFDILVTTPNRLIYLLKQDPPGIDLASVEWLVVDESDKLLKM 326
Cdd:cd17960  81 EVLQSFLEHHLPKLKCQlliggTNVEEDVKKF---KRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDEADRLLDL 157

                .
gi 4689114  327 Q 327
Cdd:cd17960 158 G 158
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
168-359 1.24e-30

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: 118.55  E-value: 1.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELA 247
Cdd:cd17940   2 EDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  248 SQIHRELIKISEGTGFRIhMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQ 327
Cdd:cd17940  81 LQTSQVCKELGKHMGVKV-MVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGV--ADLSHCKTLVLDEADKLLSQD 157
                       170       180       190
                ....*....|....*....|....*....|...
gi 4689114  328 -TGSETSWLPFSwpahPTRSEEPMFSATFAYDV 359
Cdd:cd17940 158 fQPIIEKILNFL----PKERQILLFSATFPLTV 186
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
182-326 1.28e-30

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: 118.55  E-value: 1.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  182 DAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHRELIKIS 258
Cdd:cd17941   7 EAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyreRWTPEDGLGALIISPTRELAMQIFEVLRKVG 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  259 EGTGFRIHMIhkaaVAAKKFGPKSSK--KFDILVTTPNRLIYLLKQDpPGIDLASVEWLVVDESDKLLKM 326
Cdd:cd17941  87 KYHSFSAGLI----IGGKDVKEEKERinRMNILVCTPGRLLQHMDET-PGFDTSNLQMLVLDEADRILDM 151
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
176-363 2.61e-30

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: 117.52  E-value: 2.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPA---NKGFRALIISPTRELASQIH 251
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRElekGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  252 RELIKISEGTGFRIHMIHKAA-----VAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKM 326
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGskweqAKALQEGA------EIVVATPGRLIDMVKKK--ATNLQRVTYLVLDEADRMFDM 152
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4689114  327 qtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQWC 363
Cdd:cd17952 153 --GFEYQVRSIVGHVRPDR-QTLLFSATFKKKIEQLA 186
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
172-366 5.79e-30

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: 117.30  E-value: 5.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  172 INSRLLQNILDAGFQMPTPIQMQAIPVML-HGRELLASAPTGSGKTLAFSIP----ILMQLKQPANKGFRALIISPTREL 246
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPaiqsLLNTKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  247 ASQIHRELIKISEG-TGFRIHM------IHKAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDPPGIDLASVEWLVVDE 319
Cdd:cd17964  81 ALQIAAEAKKLLQGlRKLRVQSavggtsRRAELNRLRRGRP------DILVATPGRLIDHLENPGVAKAFTDLDYLVLDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4689114  320 SDKLLKMqtGSETSwLPFSWPAHPTRSEEP----MFSATFAYDVEQWCNST 366
Cdd:cd17964 155 ADRLLDM--GFRPD-LEQILRHLPEKNADPrqtlLFSATVPDEVQQIARLT 202
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
176-365 9.73e-30

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: 116.11  E-value: 9.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPAnkgfrALIISPTRELASQIH 251
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCltehRNPS-----ALILTPTRELAVQIE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  252 RELIKISEGTgfrIHMIHKAAVAAKKFGP---KSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKMqt 328
Cdd:cd17962  76 DQAKELMKGL---PPMKTALLVGGLPLPPqlyRLQQGVKVIIATPGRLLDILKQS--SVELDNIKIVVVDEADTMLKM-- 148
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4689114  329 GSETSWLPFsWPAHPTRSEEPMFSATFAYDVEQWCNS 365
Cdd:cd17962 149 GFQQQVLDI-LENISHDHQTILVSATIPRGIEQLAGQ 184
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
153-355 6.76e-29

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: 115.14  E-value: 6.76e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  153 GTDLPDPIATFQQLDQEYKINSrllqNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----- 227
Cdd:cd18051  13 GENCPPHIETFSDLDLGEIIRN----NIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgp 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  228 -----KQPANKGFR-----ALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFgpkssKKFD----ILVTTP 293
Cdd:cd18051  89 geslpSESGYYGRRkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQM-----RDLErgchLLVATP 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4689114  294 NRLIYLLKQDPPGIDlaSVEWLVVDESDKLLKMqtGSETSW--------LPfswpahPTRSEEP-MFSATF 355
Cdd:cd18051 164 GRLVDMLERGKIGLD--YCKYLVLDEADRMLDM--GFEPQIrriveqdtMP------PTGERQTlMFSATF 224
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
176-326 9.19e-29

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 113.33  E-value: 9.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPANKGFR----ALIISPTRELASQI 250
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdLQPIPREQRngpgVLVLTPTRELALQI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4689114  251 HRELIKISEgTGFRIHMIHKAAVAAKKFgPKSSKKFDILVTTPNRLIYLlkQDPPGIDLASVEWLVVDESDKLLKM 326
Cdd:cd17958  81 EAECSKYSY-KGLKSVCVYGGGNRNEQI-EDLSKGVDIIIATPGRLNDL--QMNNVINLKSITYLVLDEADRMLDM 152
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
168-354 2.54e-28

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: 112.32  E-value: 2.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ-PAnkGFRALIISPTREL 246
Cdd:cd17955   2 EDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEdPY--GIFALVLTPTREL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  247 ASQIHRELIKISEGTGFR-------IHMIHKAAVAAKKfgPKsskkfdILVTTPNRLIYLLKQDPPGI-DLASVEWLVVD 318
Cdd:cd17955  80 AYQIAEQFRALGAPLGLRccvivggMDMVKQALELSKR--PH------IVVATPGRLADHLRSSDDTTkVLSRVKFLVLD 151
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4689114  319 ESDKLLkmqTGSETSWLPFSWPAHPTRSEEPMFSAT 354
Cdd:cd17955 152 EADRLL---TGSFEDDLATILSALPPKRQTLLFSAT 184
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
176-361 7.02e-28

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: 110.92  E-value: 7.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-QP---ANKGFRALIISPTRELASQIH 251
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaQPpleRGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  252 RELIKISEGTGFRIHMIHKAAvaakkfgPKSSKKFD------ILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLK 325
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGA-------PKGPQIRDlrrgveICIATPGRLIDFLDQGK--TNLRRVTYLVLDEADRMLD 151
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4689114  326 MqtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQ 361
Cdd:cd17966 152 M--GFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRR 184
HELICc smart00490
helicase superfamily c-terminal domain;
425-506 8.09e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 106.53  E-value: 8.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114     425 KELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGR 504
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 4689114     505 AG 506
Cdd:smart00490  81 AG 82
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
176-367 6.02e-26

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: 105.48  E-value: 6.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLkqpankgFRALIISPTRELASQIHRELI 255
Cdd:cd17938  10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QI-------VVALILEPSRELAEQTYNCIE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  256 KIS-EGTGFRI-HMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMQTGSETS 333
Cdd:cd17938  82 NFKkYLDNPKLrVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK--LDLSSVRFFVLDEADRLLSQGNLETIN 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4689114  334 WLPFSWPAHPT---RSEEPMFSATF-AYDVEQWC-----NSTW 367
Cdd:cd17938 160 RIYNRIPKITSdgkRLQVIVCSATLhSFEVKKLAdkimhFPTW 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
184-326 1.89e-25

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: 104.59  E-value: 1.89e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  184 GFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPA------NKGFRALIISPTRELASQIHRELIKI 257
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL-LSLeprvdrSDGTLALVLVPTRELALQIYEVLEKL 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4689114  258 segtGFRIHMIHKAAVAA--KKFGPKSS--KKFDILVTTPNRLIYLLkQDPPGIDLASVEWLVVDESDKLLKM 326
Cdd:cd17949  89 ----LKPFHWIVPGYLIGgeKRKSEKARlrKGVNILIATPGRLLDHL-KNTQSFDVSNLRWLVLDEADRLLDM 156
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
177-361 4.10e-25

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: 102.82  E-value: 4.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  177 LQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIP---ILMQLK-QPANkGFRALIISPTRELASQIH- 251
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKfKPRN-GTGVIIISPTRELALQIYg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  252 --RELIKISEGT-GFRIHMIHKAAVAAkkfgpKSSKKFDILVTTPNRLIYLLkQDPPGIDLASVEWLVVDESDKLLKMQT 328
Cdd:cd17942  81 vaKELLKYHSQTfGIVIGGANRKAEAE-----KLGKGVNILVATPGRLLDHL-QNTKGFLYKNLQCLIIDEADRILEIGF 154
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4689114  329 GSE----TSWLpfswpahPTRSEEPMFSATFAYDVEQ 361
Cdd:cd17942 155 EEEmrqiIKLL-------PKRRQTMLFSATQTRKVED 184
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
176-355 9.56e-25

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: 101.57  E-value: 9.56e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-LERRHPQVLILAPTREIAVQIHDVFK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  256 KISE-GTGFRIH-MIHKAAVAAKKfgpKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKMQTGSETS 333
Cdd:cd17943  80 KIGKkLEGLKCEvFIGGTPVKEDK---KKLKGCHIAVGTPGRIKQLIELG--ALNVSHVRLFVLDEADKLMEGSFQKDVN 154
                       170       180
                ....*....|....*....|..
gi 4689114  334 WLpFSwpAHPTRSEEPMFSATF 355
Cdd:cd17943 155 WI-FS--SLPKNKQVIAFSATY 173
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
131-361 1.46e-23

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: 100.47  E-value: 1.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  131 KLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAP 210
Cdd:cd18050  32 EVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQAN----FPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  211 TGSGKTLAFSIPILMQLK-QP---ANKGFRALIISPTRELASQIHRelIKISEGTGFRIHMIHKAAVAAKkfGPKS---S 283
Cdd:cd18050 108 TGSGKTLAYLLPAIVHINhQPyleRGDGPICLVLAPTRELAQQVQQ--VADDYGKSSRLKSTCIYGGAPK--GPQIrdlE 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  284 KKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMqtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQ 361
Cdd:cd18050 184 RGVEICIATPGRLIDFLEAGK--TNLRRCTYLVLDEADRMLDM--GFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRQ 256
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
176-324 2.46e-23

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: 98.98  E-value: 2.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQ-LKQPANKGF-----RALIISPTRELASQ 249
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGpfnapRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  250 IHRELIKISEGTGFRIHMIH----KAAVAAKKFGpksskKFDILVTTPNRLIYLLKQdppGI-DLASVEWLVVDESDKLL 324
Cdd:cd17948  81 IGSVAQSLTEGLGLKVKVITggrtKRQIRNPHFE-----EVDILVATPGALSKLLTS---RIySLEQLRHLVLDEADTLL 152
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
176-326 3.21e-23

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: 97.79  E-value: 3.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILM-----QLKQP--ANKGFRALIISPTRELAS 248
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMfaleqEKKLPfiKGEGPYGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  249 QIHrELI-----KISEGTGFRIH---------MIHKAAVAakkfgpksSKKFDILVTTPNRLIYLLKQDPpgIDLASVEW 314
Cdd:cd17951  81 QTH-EVIeyyckALQEGGYPQLRcllciggmsVKEQLEVI--------RKGVHIVVATPGRLMDMLNKKK--INLDICRY 149
                       170
                ....*....|..
gi 4689114  315 LVVDESDKLLKM 326
Cdd:cd17951 150 LCLDEADRMIDM 161
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
201-528 4.04e-23

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 103.57  E-value: 4.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  201 HGRELLASAPTGSGKTLAFSIpILMQLKQPAnkgfRALIISPTRELASQIHRELIKISEGTGFrihmihkaavaakkFGP 280
Cdd:COG1061  99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGK----RVLVLVPRRELLEQWAEELRRFLGDPLA--------------GGG 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  281 KSSKKFDILVTTPNRLIYLLKQD--PPGIDLasvewLVVDES--------DKLLKMQTgsetswlpfswPAH-------P 343
Cdd:COG1061 160 KKDSDAPITVATYQSLARRAHLDelGDRFGL-----VIIDEAhhagapsyRRILEAFP-----------AAYrlgltatP 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  344 TRSEE-PMFSATF---AYDV-------EQWCNSTWTMSSVCPLEARNSAVETVEQEL--LFVGSETGKLLAVRELVKK-G 409
Cdd:COG1061 224 FRSDGrEILLFLFdgiVYEYslkeaieDGYLAPPEYYGIRVDLTDERAEYDALSERLreALAADAERKDKILRELLREhP 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  410 FNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDfP 489
Cdd:COG1061 304 DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-P 382
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4689114  490 TSS-VEYIHRIGRTGR-AGNKGKAITF-FTEDDKPLLRSVAN 528
Cdd:COG1061 383 TGSpREFIQRLGRGLRpAPGKEDALVYdFVGNDVPVLEELAK 424
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
138-361 1.69e-22

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: 96.62  E-value: 1.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  138 EKINFLRNKHKIHVQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTL 217
Cdd:cd18049   1 QEVEQYRRSKEITVRGHNCPKPVLNFY----EANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  218 AFSIPILMQLK-QP---ANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAakkfGPKS---SKKFDILV 290
Cdd:cd18049  77 SYLLPAIVHINhQPfleRGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK----GPQIrdlERGVEICI 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4689114  291 TTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKMqtGSETSWLPFSWPAHPTRsEEPMFSATFAYDVEQ 361
Cdd:cd18049 153 ATPGRLIDFLEAGK--TNLRRCTYLVLDEADRMLDM--GFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRQ 218
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
168-363 1.14e-21

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: 93.56  E-value: 1.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELA 247
Cdd:cd17950   5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE-PVDGQVSVLVICHTRELA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  248 SQIHRELIKISE-------GTGFRIHMIHKAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDES 320
Cdd:cd17950  84 FQISNEYERFSKympnvktAVFFGGVPIKKDIEVLKNKCP------HIVVGTPGRILALVREK--KLKLSHVKHFVLDEC 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4689114  321 DKL---LKMQTGSETSWLpfswpAHPTRSEEPMFSATFAYDVEQWC 363
Cdd:cd17950 156 DKMleqLDMRRDVQEIFR-----ATPHDKQVMMFSATLSKEIRPVC 196
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
188-336 1.27e-21

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: 94.37  E-value: 1.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  188 PTPIQMQAIPVMLHGR----------------ELLASAPTGSGKTLAFSIPILMQLKQ----------------PANKGF 235
Cdd:cd17965  31 PSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesaKDTGRP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  236 RALIISPTRELASQIHRELIKISEGTGFRIHMI-HKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPgiDLASVEW 314
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPK--ILSRVTH 188
                       170       180
                ....*....|....*....|..
gi 4689114  315 LVVDESDKLLkmqtgsETSWLP 336
Cdd:cd17965 189 LVVDEADTLF------DRSFLQ 204
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
172-360 4.42e-21

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: 91.48  E-value: 4.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQ 249
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQALCLAPTRELARQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  250 IHRELIKISEGTGFRIHMihkaAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKMQTG 329
Cdd:cd17963  80 IGEVVEKMGKFTGVKVAL----AVPGNDVPRGKKITAQIVIGTPGTVLDWLKKR--QLDLKKIKILVLDEADVMLDTQGH 153
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4689114  330 SETS-----WLPFSWpahptrsEEPMFSATFAYDVE 360
Cdd:cd17963 154 GDQSirikrMLPRNC-------QILLFSATFPDSVR 182
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
169-325 7.96e-19

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: 85.07  E-value: 7.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  169 EYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKgFRALIISPTRELAS 248
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE-TQALVLAPTRELAQ 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  249 QIHRELIKISEGTGFRIH-MIHKAAVAAKKFgpKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLK 325
Cdd:cd17939  80 QIQKVVKALGDYMGVKVHaCIGGTSVREDRR--KLQYGPHIVVGTPGRVFDMLQRR--SLRTDKIKMFVLDEADEMLS 153
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
202-319 1.68e-17

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: 80.32  E-value: 1.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  202 GRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPK 281
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEKAK 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4689114  282 SSKKF-DILVTTPNRLIYLLKQDPPGIDLASVEWLVVDE 319
Cdd:cd17922  81 QLKNPpGILITTPESLELLLVNKKLRELFAGLRYVVVDE 119
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
189-506 2.88e-17

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 84.95  E-value: 2.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  189 TPIQMQAIP-VMLHGRELLASAPTGSGKTLAFSIPILMQLkqpaNKGFRALIISPTRELASQIHRELIKISEGTGFRIhm 267
Cdd:COG1204  24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL----LNGGKALYIVPLRALASEKYREFKRDFEELGIKV-- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  268 ihKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLlkmqtGSETSWlpfswpahPT--- 344
Cdd:COG1204  98 --GVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLR--DVDLVVVDEAHLI-----DDESRG--------PTlev 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  345 -----RSEEP----MF-SATF--AYDVEQWCN-----STWTmssvcplearnsaveTVEQELLFV---------GSETGK 398
Cdd:COG1204 161 llarlRRLNPeaqiVAlSATIgnAEEIAEWLDaelvkSDWR---------------PVPLNEGVLydgvlrfddGSRRSK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  399 ---LLAVRELVKKGfnPPVLVFVQSIERA-----------------------KELFHELIYEGINVDVI----------- 441
Cdd:COG1204 226 dptLALALDLLEEG--GQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSEETHTNekladclekgv 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  442 ---HAERTQQQRDNTVHSFRAGKIWVLICTALLArgidfKGVNL----VI--------NYDFPTSsvEYIHRIGRTGRAG 506
Cdd:COG1204 304 afhHAGLPSELRRLVEDAFREGLIKVLVATPTLA-----AGVNLparrVIirdtkrggMVPIPVL--EFKQMAGRAGRPG 376
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
176-326 3.35e-17

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: 80.20  E-value: 3.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd18045  10 LLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQALILSPTRELAVQIQKVLL 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4689114  256 KISEGTGFRIHmihkAAVAAKKFGPKSSK---KFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLLKM 326
Cdd:cd18045  89 ALGDYMNVQCH----ACIGGTSVGDDIRKldyGQHIVSGTPGRVFDMIRRR--SLRTRHIKMLVLDEADEMLNK 156
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
176-324 5.64e-17

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: 79.80  E-value: 5.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd18046  10 LLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKATQALVLAPTRELAQQIQKVVM 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  256 KISEGTGFRIHM-IHKAAVAAKKFGPKSSKKfdILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLL 324
Cdd:cd18046  89 ALGDYMGIKCHAcIGGTSVRDDAQKLQAGPH--IVVGTPGRVFDMINRR--YLRTDYIKMFVLDEADEML 154
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
185-319 1.93e-16

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 83.23  E-value: 1.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  185 FQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPANKGFRALIISPTRELASQIHRELIK--- 256
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELarrprPGELPDGLRVLYISPLKALANDIERNLRAple 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4689114  257 -ISEGTGFRIHMIhKAAV------AAKKfgpkssKKF-----DILVTTPNRLiYLLKQDPPGID-LASVEWLVVDE 319
Cdd:COG1201 102 eIGEAAGLPLPEI-RVGVrtgdtpASER------QRQrrrppHILITTPESL-ALLLTSPDARElLRGVRTVIVDE 169
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
188-512 1.01e-15

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 80.67  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHRELIKISEGTG-- 262
Cdd:TIGR04121  14 PRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLagpEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlp 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    263 FRIHM------IHKAAvAAKKFGPksskkfDILVTTPNRLIYLLKQ-DPPGI--DLASVewlVVDESDKLLKMQTGSET- 332
Cdd:TIGR04121  94 IRVETrtgdtsSSERA-RQRKKPP------DILLTTPESLALLLSYpDAARLfkDLRCV---VVDEWHELAGSKRGDQLe 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    333 ---SWLpfswpahptRSEEPMF-----SATFAyDVEQWCN-----STWTMSSVCPLEARNSAVETV--EQELLFVGSETG 397
Cdd:TIGR04121 164 lalARL---------RRLAPGLrrwglSATIG-NLEEARRvllgvGGAPAVLVRGKLPKAIEVISLlpESEERFPWAGHL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    398 KLLAVRELVKK-GFNPPVLVFVQSIERAKELFHELIYegINVD---VI---HAERTQQQRDNTVHSFRAGKIWVLICTAL 470
Cdd:TIGR04121 234 GLRALPEVYAEiDQARTTLVFTNTRSQAELWFQALWE--ANPEfalPIalhHGSLDREQRRWVEAAMAAGRLRAVVCTSS 311
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 4689114    471 LARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG-RAGNKGKAI 512
Cdd:TIGR04121 312 LDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL 354
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
189-319 1.10e-14

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: 72.29  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  189 TPIQMQAI-PVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELASQIHRELIKISEGTGFRIHM 267
Cdd:cd17921   3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4689114  268 IhkaaVAAKKFGPKSSKKFDILVTTPNRL-IYLLKqdPPGIDLASVEWLVVDE 319
Cdd:cd17921  80 L----TGDPSVNKLLLAEADILVATPEKLdLLLRN--GGERLIQDVRLVVVDE 126
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
147-355 1.93e-14

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: 73.13  E-value: 1.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  147 HKIHVQGTDLPDPIATFQQLdQEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPIL 224
Cdd:cd18048   1 HRVEVLQRDPTSPLFSVKSF-EELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  225 MQLKqpANKGF-RALIISPTRELASQIHR---ELIKISEGtgfrIHMIHkaAVAAKKFGPKSSKKFDILVTTPNRLI--- 297
Cdd:cd18048  80 SRVD--ALKLYpQCLCLSPTFELALQTGKvveEMGKFCVG----IQVIY--AIRGNRPGKGTDIEAQIVIGTPGTVLdwc 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  298 YLLKQdppgIDLASVEWLVVDESDKLLKMQTGSETSWLPFSwpAHPTRSEEPMFSATF 355
Cdd:cd18048 152 FKLRL----IDVTNISVFVLDEADVMINVQGHSDHSVRVKR--SMPKECQMLLFSATF 203
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
192-522 2.74e-14

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: 76.03  E-value: 2.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELASQIHRELIKISEGTGFRIHmihka 271
Cdd:COG1205  61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE--DPGATALYLYPTKALARDQLRRLRELAEALGLGVR----- 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  272 avAAKKFG--PKSSKKF-----DILVTTPNRLIY-LLKQDPPGID-LASVEWLVVDEsdkllkMQT-----GSETSWL-- 335
Cdd:COG1205 134 --VATYDGdtPPEERRWirehpDIVLTNPDMLHYgLLPHHTRWARfFRNLRYVVIDE------AHTyrgvfGSHVANVlr 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  336 ------PFsWPAHPTrseepmF---SATFAydveqwcNstwtmssvcPLE-ARN---SAVETV--------EQELLFV-- 392
Cdd:COG1205 206 rlrricRH-YGSDPQ------FilaSATIG-------N---------PAEhAERltgRPVTVVdedgsprgERTFVLWnp 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  393 -----------GSETGKLLAvrELVKKGFNppVLVFVQSI-------ERAKELFHELIYeGINVDVIHAERTQQQRDNTV 454
Cdd:COG1205 263 plvddgirrsaLAEAARLLA--DLVREGLR--TLVFTRSRrgaellaRYARRALREPDL-ADRVAAYRAGYLPEERREIE 337
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  455 HSFRAGKIWVLICT-AL-LarGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDdkPL 522
Cdd:COG1205 338 RGLRSGELLGVVSTnALeL--GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDD--PL 403
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
202-325 5.55e-14

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: 69.35  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  202 GRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELASQIHRELIKISeGTGFRIHMIHkaavAAKKFGPK 281
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK---KGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLV----GGSSAEER 72
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4689114  282 SSKKF---DILVTTPNRlIYLLKQDPPGIDLASVEWLVVDESDKLLK 325
Cdd:cd00046  73 EKNKLgdaDIIIATPDM-LLNLLLREDRLFLKDLKLIIVDEAHALLI 118
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
398-518 5.69e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 75.15  E-value: 5.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  398 KLLAVRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINVD--VIHAER------TQQQRDNTVHSFRAGKIWVL 465
Cdd:COG1111 336 KLSKLREILKEqlGTNPDsrIIVFTQYRDTAEMIVEFLSEPGIKAGrfVGQASKegdkglTQKEQIEILERFRAGEFNVL 415
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4689114  466 ICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAITFFTED 518
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAKG 467
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
190-326 1.79e-13

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: 69.49  E-value: 1.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  190 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK---QPANKGF--RALIISPTRELASQIHRELIKISEgtgfr 264
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqQPRKRGRapKVLVLAPTRELANQVTKDFKDITR----- 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4689114  265 ihmihKAAVAAKKFGPKSSKKF-------DILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLLKM 326
Cdd:cd17944  90 -----KLSVACFYGGTPYQQQIfairngiDILVGTPGRIKDHLQNGR--LDLTKLKHVVLDEVDQMLDM 151
PRK01172 PRK01172
ATP-dependent DNA helicase;
192-506 2.44e-13

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 72.99  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqpanKGFRALIISPTRELASQIHRELIKISEgTGFRIHMihka 271
Cdd:PRK01172  27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFL----AGLKSIYIVPLRSLAMEKYEELSRLRS-LGMRVKI---- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   272 AVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLlkmqtGSETSWLPFSWPAHPTRSEEP-- 349
Cdd:PRK01172  98 SIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIIN--DVGLIVADEIHII-----GDEDRGPTLETVLSSARYVNPda 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   350 ---MFSATF--AYDVEQWCNSTWTMSSVCPLEARNSAVetVEQELLFVGSETGKL---LAVRELVKKGFNppVLVFVQSI 421
Cdd:PRK01172 171 rilALSATVsnANELAQWLNASLIKSNFRPVPLKLGIL--YRKRLILDGYERSQVdinSLIKETVNDGGQ--VLVFVSSR 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   422 ERAK---------------------------ELFHELIYEGINVDviHAERTQQQRDNTVHSFRAGKIWVLICTALLARG 474
Cdd:PRK01172 247 KNAEdyaemliqhfpefndfkvssennnvydDSLNEMLPHGVAFH--HAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAG 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 4689114   475 IDFKGvNLVINYDF---------PTSSVEYIHRIGRTGRAG 506
Cdd:PRK01172 325 VNLPA-RLVIVRDItrygnggirYLSNMEIKQMIGRAGRPG 364
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
413-516 5.59e-12

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: 61.57  E-value: 5.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  413 PVLVFVQSIERAKELFHELIyeginvdvihaertqqqrdntvhsfragkiwVLICTALLARGIDFKGVNLVINYDFPTSS 492
Cdd:cd18785   5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
                        90       100
                ....*....|....*....|....
gi 4689114  493 VEYIHRIGRTGRAGNKGKAITFFT 516
Cdd:cd18785  54 ASYIQRVGRAGRGGKDEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
192-319 1.26e-11

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: 63.76  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELA-SQIhRELIKISEGTGFRIHMihk 270
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR--DPGSRALYLYPTKALAqDQL-RSLRELLEQLGLGIRV--- 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4689114  271 AAVAAKKfgPKSSKKF------DILVTTPNRLIYLLkqDPPGID----LASVEWLVVDE 319
Cdd:cd17923  79 ATYDGDT--PREERRAiirnppRILLTNPDMLHYAL--LPHHDRwarfLRNLRYVVLDE 133
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
190-319 2.81e-11

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: 62.35  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  190 PIQMQAI-PVMLHGRELLASAPTGSGKTLafsIPILMQLKQpANKGFRALIISPTRELASQIHRELiKISEGTGFRIhmi 268
Cdd:cd18028   4 PPQAEAVrAGLLKGENLLISIPTASGKTL---IAEMAMVNT-LLEGGKALYLVPLRALASEKYEEF-KKLEEIGLKV--- 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4689114  269 hkaAVAAKKF--GPKSSKKFDILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:cd18028  76 ---GISTGDYdeDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGV--VVVDE 123
PRK13767 PRK13767
ATP-dependent helicase; Provisional
189-319 3.25e-11

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 66.45  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   189 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKG-----FRALIISPTRELASQIHRELI-------K 256
Cdd:PRK13767  34 TPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGeledkVYCLYVSPLRALNNDIHRNLEeplteirE 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4689114   257 ISEGTGFRIHMIhKAAVaakKFGPKSS--------KKFDILVTTPNRLIYLL-----KQDppgidLASVEWLVVDE 319
Cdd:PRK13767 114 IAKERGEELPEI-RVAI---RTGDTSSyekqkmlkKPPHILITTPESLAILLnspkfREK-----LRTVKWVIVDE 180
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
168-333 4.84e-11

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: 62.43  E-value: 4.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRE 245
Cdd:cd18047   4 EELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-EPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  246 LASQIHRELIKISEgtgFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLI-YLLKQDPpgIDLASVEWLVVDESDKLL 324
Cdd:cd18047  83 LALQTGKVIEQMGK---FYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLdWCSKLKF--IDPKKIKVFVLDEADVMI 157

                ....*....
gi 4689114  325 KMQTGSETS 333
Cdd:cd18047 158 ATQGHQDQS 166
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
388-515 1.32e-10

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: 59.53  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  388 ELLFVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 467
Cdd:cd18794   7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4689114  468 TALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFF 515
Cdd:cd18794  87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
398-512 1.68e-10

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: 59.29  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  398 KLLAVRELVKKGF-------NPPVLVFVQSIERAKELFHELIYEGINVDVI----HAER------TQQQRDNTVHSFRAG 460
Cdd:cd18801  10 KLEKLEEIVKEHFkkkqegsDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKG 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4689114  461 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAI 512
Cdd:cd18801  90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
PRK13766 PRK13766
Hef nuclease; Provisional
398-518 5.61e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.20  E-value: 5.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   398 KLLAVRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINvdvihAER-------------TQQQRDNTVHSFRAG 460
Cdd:PRK13766 348 KLEKLREIVKEqlGKNPDsrIIVFTQYRDTAEKIVDLLEKEGIK-----AVRfvgqaskdgdkgmSQKEQIEILDKFRAG 422
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114   461 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAITFFTED 518
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVVVLIAKG 479
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
398-504 1.84e-09

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 60.27  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  398 KLLA-VRELVKKGFnpPVLVFVQSIERAKELFHEL--IYEGINVDVIHAErtQQQRDNTVHSFRAGKIWVLICTALLARG 474
Cdd:COG4098 307 KLLKwLKKRLKEGR--QLLIFVPTIELLEQLVALLqkLFPEERIAGVHAE--DPERKEKVQAFRDGEIPILVTTTILERG 382
                        90       100       110
                ....*....|....*....|....*....|....
gi 4689114  475 IDFKGVN-LVINYD---FPTSSVEYIHriGRTGR 504
Cdd:COG4098 383 VTFPNVDvAVLGADhpvFTEAALVQIA--GRVGR 414
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
418-522 3.34e-09

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: 55.81  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  418 VQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIH 497
Cdd:cd18810  35 IESIEKLATQLRQLVPE-ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLY 113
                        90       100
                ....*....|....*....|....*.
gi 4689114  498 RI-GRTGRAGNKGKAItFFTEDDKPL 522
Cdd:cd18810 114 QLrGRVGRSKERAYAY-FLYPDQKKL 138
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
397-500 1.62e-08

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 53.25  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  397 GKLLAVRELVKKGFNPP--VLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAG-KIWV-LICTALLA 472
Cdd:cd18793  11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
                        90       100       110
                ....*....|....*....|....*....|....
gi 4689114  473 RGIDFKGVNLVINYDFP-TSSVEY-----IHRIG 500
Cdd:cd18793  91 VGLNLTAANRVILYDPWwNPAVEEqaidrAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
395-502 1.87e-08

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 57.54  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  395 ETGKLLAVRELVKKGFNP--PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGK-IWV-LICTAL 470
Cdd:COG0553 531 RSAKLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKA 610
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4689114  471 LARGIDFKGVNLVINYDFP-TSSVEY-----IHRIGRT 502
Cdd:COG0553 611 GGEGLNLTAADHVIHYDLWwNPAVEEqaidrAHRIGQT 648
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
398-524 1.99e-08

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.07  E-value: 1.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  398 KLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 477
Cdd:COG0514 217 KLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDK 296
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4689114  478 KGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLR 524
Cdd:COG0514 297 PDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
444-508 3.31e-08

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 52.59  E-value: 3.31e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4689114  444 ERTQQQRdnTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNK 508
Cdd:cd18802  75 TQRKQKE--TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
414-507 5.39e-08

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: 52.27  E-value: 5.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  414 VLVFVQSIERAKELFHEL------IYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYD 487
Cdd:cd18796  41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
                        90       100
                ....*....|....*....|
gi 4689114  488 FPTSSVEYIHRIGRTGRAGN 507
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPG 140
PRK00254 PRK00254
ski2-like helicase; Provisional
169-319 1.68e-07

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 54.44  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   169 EYKINSRLLQNILDAGFQMPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELA 247
Cdd:PRK00254   5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR---EGGKAVYLVPLKALA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114   248 SQIHRELiKISEGTGFRIHMIHkaavaakkfGPKSSK-----KFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDE 319
Cdd:PRK00254  82 EEKYREF-KDWEKLGLRVAMTT---------GDYDSTdewlgKYDIIIATAEKFDSLLRHGSSWIK--DVKLVVADE 146
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
197-319 2.41e-07

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 51.45  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  197 PVMLHGRELLASAPTGSGKTLAFSipILMqLKQPANKGFRALIISPTRELASQIHRELIKISEGTGFRI--HMIHKaava 274
Cdd:cd18026  28 PGLLEGRNLVYSLPTSGGKTLVAE--ILM-LKRLLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVegYAGNK---- 100
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4689114  275 aKKFGPKSSKKFDILVTTP-------NRLIYLLKQDppgiDLASVewlVVDE 319
Cdd:cd18026 101 -GRSPPKRRKSLSVAVCTIekanslvNSLIEEGRLD----ELGLV---VVDE 144
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
398-512 3.95e-07

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 49.86  E-value: 3.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  398 KLLAVRELVKKGfnpPVLVFVQSieR------AKEL----FHeliyeginvdviHAERTQQQRDnTVHS-FRAGKIWVLI 466
Cdd:cd18795  33 VLLKIETVSEGK---PVLVFCSS--RkecektAKDLagiaFH------------HAGLTREDRE-LVEElFREGLIKVLV 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4689114  467 CTALLArgidfKGVNL----VI----------NYDFPTSSvEYIHRIGRTGRAG--NKGKAI 512
Cdd:cd18795  95 ATSTLA-----AGVNLpartVIikgtqrydgkGYRELSPL-EYLQMIGRAGRPGfdTRGEAI 150
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
200-325 5.48e-07

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: 50.40  E-value: 5.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  200 LHGRELLASAPTGSGKT---LAFSIPIlmqlkqpANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAK 276
Cdd:cd17924  30 LRGKSFAIIAPTGVGKTtfgLATSLYL-------ASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSRLKK 102
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  277 KFGPKSSKK-----FDILVTTpNRLIY----LLKQDPPGIdlasvewLVVDESDKLLK 325
Cdd:cd17924 103 KEKEELLEKiekgdFDILVTT-NQFLSknfdLLSNKKFDF-------VFVDDVDAVLK 152
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
190-319 1.22e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.46  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  190 PIQMQAIPVML---HGRELLASAPTGSGKTLaFSIPILMQLKQpankgFRALIISPTRELASQIHRELIKISEGtgfriH 266
Cdd:cd17926   3 PYQEEALEAWLahkNNRRGILVLPTGSGKTL-TALALIAYLKE-----LRTLIVVPTDALLDQWKERFEDFLGD-----S 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4689114  267 MIHkaavaakKFGPKSSKKFD---ILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:cd17926  72 SIG-------LIGGGKKKDFDdanVVVATYQSLSNLAEEEKDLFDQFGL--LIVDE 118
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
191-253 4.13e-06

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 47.74  E-value: 4.13e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114  191 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKG---FRALIISPTRELASQIHRE 253
Cdd:cd18023   5 IQSEVFPDLLYSDKnFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnRKVVYIAPIKALCSEKYDD 71
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
209-503 5.18e-06

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 49.92  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    209 APTGSGKTLA---FSIPILMQLKQPANK------GFRALIISPTRELASQIHRELIKISEGTG------------FRIHM 267
Cdd:PRK09751    3 APTGSGKTLAaflYALDRLFREGGEDTReahkrkTSRILYISPIKALGTDVQRNLQIPLKGIAderrrrgetevnLRVGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    268 IHKAAVAAKKFGpKSSKKFDILVTTPNRLiYLLKQDPPGIDLASVEWLVVDESDKLLKMQTGSEtswLPFSW----PAHP 343
Cdd:PRK09751   83 RTGDTPAQERSK-LTRNPPDILITTPESL-YLMLTSRARETLRGVETVIIDEVHAVAGSKRGAH---LALSLerldALLH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    344 TRSEEPMFSATF--AYDVEQWCNSTWTMSSVCPLEARNSAVETV-----EQELLFVGSETG------KLLAVRELVKKGF 410
Cdd:PRK09751  158 TSAQRIGLSATVrsASDVAAFLGGDRPVTVVNPPAMRHPQIRIVvpvanMDDVSSVASGTGedshagREGSIWPYIETGI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    411 NPPVL------VFVQS-------IERAKELFHELI------------YEGIN---------VDVI-----HAERTQQQRD 451
Cdd:PRK09751  238 LDEVLrhrstiVFTNSrglaeklTARLNELYAARLqrspsiavdaahFESTSgatsnrvqsSDVFiarshHGSVSKEQRA 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4689114    452 NTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG 503
Cdd:PRK09751  318 ITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
188-264 7.63e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 46.64  E-value: 7.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  188 PTPIQMQAIPVMLHG------RELLASAPTGSGKTLAFSIPILMQLkqpaNKGFRALIISPTRELASQIHREL------I 255
Cdd:cd17918  16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY----KNGKQVAILVPTEILAHQHYEEArkflpfI 91

                ....*....
gi 4689114  256 KISEGTGFR 264
Cdd:cd17918  92 NVELVTGGT 100
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
415-516 9.89e-06

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: 44.86  E-value: 9.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  415 LVFVQSIERAKELFHELIYEGINVDVIHAERTQQQR-DNTVHSFRAGKIW--VLICTALLARGIDFKGVNLVInYDFPT- 490
Cdd:cd18799  10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV-FLRPTe 88
                        90       100
                ....*....|....*....|....*..
gi 4689114  491 SSVEYIHRIGR-TGRAGNKgkaiTFFT 516
Cdd:cd18799  89 SRTLFLQMLGRgLRLHEGK----DFFT 111
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
394-512 1.03e-05

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: 45.71  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  394 SETGKLLAvrELVKKGFNppVLVFVQS---IER-AKELFHELIYEGINVDVIHAER---TQQQRDNTVHSFRAGKIWVLI 466
Cdd:cd18797  22 REAARLFA--DLVRAGVK--TIVFCRSrklAELlLRYLKARLVEEGPLASKVASYRagyLAEDRREIEAELFNGELLGVV 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4689114  467 CTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAI 512
Cdd:cd18797  98 ATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
418-527 1.10e-05

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 45.72  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  418 VQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIH 497
Cdd:cd18792  44 LKSIEALAEELKELVPE-ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLH 122
                        90       100       110
                ....*....|....*....|....*....|.
gi 4689114  498 RI-GRTGRAGNKGKAitFFTEDDKPLLRSVA 527
Cdd:cd18792 123 QLrGRVGRGKHQSYC--YLLYPDPKKLTETA 151
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
413-526 1.40e-05

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 46.85  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  413 PVLVFV----QSIERA-KELFHEliYEGINVDVIHAeRTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLV--IN 485
Cdd:cd18804  94 EDLVFKgigtERVEEElKTLFPE--ARIARIDRDTT-RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLN 170
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4689114  486 YDFPTSSVEY---------IHRI-GRTGRAGNKGKAI--TFFTEDdkPLLRSV 526
Cdd:cd18804 171 ADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTYNPEH--PLIQAA 221
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
359-517 1.76e-05

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 44.93  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  359 VEQWCNSTwtmssvcPLEARNSAVETVEQE--LLFVGSeTGKLLAVRELVKKGFNP-PVLVFVQSIERAKElfhelIYEG 435
Cdd:cd18789   2 AEIRCPMT-------PEFYREYLGLGAHRKrrLLAAMN-PNKLRALEELLKRHEQGdKIIVFTDNVEALYR-----YAKR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  436 INVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF--KGVNLVINYDFpTSSVEYIHRIGRTGRAGNKGKAIT 513
Cdd:cd18789  69 LLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHG-GSRRQEAQRLGRILRPKKGGGKNA 147

                ....
gi 4689114  514 FFTE 517
Cdd:cd18789 148 FFYS 151
PRK02362 PRK02362
ATP-dependent DNA helicase;
190-319 2.53e-05

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 47.26  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   190 PIQMQAIPV-MLHGRELLASAPTGSGKTLafsIPILMQLKQPANKGfRALIISPTRELASQIHRELIKISEgTGFRIhmi 268
Cdd:PRK02362  26 PPQAEAVEAgLLDGKNLLAAIPTASGKTL---IAELAMLKAIARGG-KALYIVPLRALASEKFEEFERFEE-LGVRV--- 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4689114   269 hkaAVAAKKFGPKSS--KKFDILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:PRK02362  98 ---GISTGDYDSRDEwlGDNDIIVATSEKVDSLLRNGAPWLDDITC--VVVDE 145
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
175-319 2.92e-05

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 45.32  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  175 RLLQNILdaGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIP-ILMQLKQPAnkgfRALIISPTREL-ASQIHR 252
Cdd:cd18018   2 KLLRRVF--GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPaLLLRRRGPG----LTLVVSPLIALmKDQVDA 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4689114  253 eLIKISEGTgfRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRL-----IYLLKQdPPGIDLasvewLVVDE 319
Cdd:cd18018  76 -LPRAIKAA--ALNSSLTREERRRILEKLRAGEVKILYVSPERLvnesfRELLRQ-TPPISL-----LVVDE 138
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
209-269 6.58e-05

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 45.75  E-value: 6.58e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4689114  209 APTGSGKTLAFSIPILMQLKqpanKGFRALIISPTRELASQIHRELIKisegTGFRIHMIH 269
Cdd:COG3505   6 GPTGSGKTVGLVIPNLTQLA----RGESVVVTDPKGDLAELTAGFRRR----AGYDVYVFD 58
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
184-242 9.92e-05

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 43.68  E-value: 9.92e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4689114  184 GFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqlkqpaNKGFrALIISP 242
Cdd:cd17920   9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL------LDGV-TLVVSP 60
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
402-512 1.31e-04

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: 43.00  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  402 VRELVKKGFNppVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVN 481
Cdd:cd18790  20 IRKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 97
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 4689114  482 LVINYD-----FPTSSVEYIHRIGRTGRAGNkGKAI 512
Cdd:cd18790  98 LVAILDadkegFLRSETSLIQTIGRAARNVN-GKVI 132
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
188-319 2.53e-04

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 42.42  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAfSIPILMQL--KQPANKGFRALIISPTRELASQIHRELIKISEGTGFRI 265
Cdd:cd17927   3 PRNYQLELAQPALKGKNTIICLPTGSGKTFV-AVLICEHHlkKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4689114  266 HMIhKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKqDPPGIDLASVEWLVVDE 319
Cdd:cd17927  82 TGL-SGDTSENVSVEQIVESSDVIIVTPQILVNDLK-SGTIVSLSDFSLLVFDE 133
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
190-293 3.39e-04

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 41.98  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  190 PIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELAsqihRELI-----KISEGTGF 263
Cdd:cd18022   4 PIQTQVFHTLYHTDNnVLLGAPTGSGKTIAAELAMFRAFNK--YPGSKVVYIAPLKALV----RERVddwkkRFEEKLGK 77
                        90       100       110
                ....*....|....*....|....*....|
gi 4689114  264 RIHMIHKAAVAakkfGPKSSKKFDILVTTP 293
Cdd:cd18022  78 KVVELTGDVTP----DMKALADADIIITTP 103
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
188-301 3.49e-04

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 42.08  E-value: 3.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ--PANKGFRALIISPTRELASQIHRELIKISEGtGFRI 265
Cdd:cd18036   3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKV 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 4689114  266 HMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLK 301
Cdd:cd18036  82 TGLS-GDSSHKVSFGQIVKASDVIICTPQILINNLL 116
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
190-297 4.56e-04

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 41.48  E-value: 4.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  190 PIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKgfRALIISPTRELASQIHRELikisegtgfrihmi 268
Cdd:cd18021   6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKG--RAVYIAPMQELVDARYKDW-------------- 69
                        90       100       110
                ....*....|....*....|....*....|..
gi 4689114  269 hkaavaAKKFGPKSSKKFDIL---VTTPNRLI 297
Cdd:cd18021  70 ------RAKFGPLLGKKVVKLtgeTSTDLKLL 95
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
191-319 6.31e-04

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 41.26  E-value: 6.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  191 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKG-------FRALIISPTRELASQIHREL-------- 254
Cdd:cd18020   5 IQSLVFPVAYKTNEnMLICAPTGAGKTNIAMLTILHEIRQHVNQGgvikkddFKIVYIAPMKALAAEMVEKFskrlaplg 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4689114  255 IKISEGTGfriHM-IHKAAVAAKKfgpksskkfdILVTTPNRLIYLLKQDPPGIDLAS-VEWLVVDE 319
Cdd:cd18020  85 IKVKELTG---DMqLTKKEIAETQ----------IIVTTPEKWDVVTRKSSGDVALSQlVRLLIIDE 138
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
175-242 7.10e-04

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 41.20  E-value: 7.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  175 RLLQNIldagFQMPT--PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqlkqpaNKGFrALIISP 242
Cdd:cd18015   8 DTLKNV----FKLEKfrPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC------SDGF-TLVVSP 66
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
201-319 8.60e-04

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 40.63  E-value: 8.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  201 HGRELLASAPtGSGKTLAfSIPILMQLKQPANKGFRALIISPtrelASQIH---RELIKISEGtgFRIHMIHKA-AVAAK 276
Cdd:cd17919  19 GPGGILADEM-GLGKTLQ-AIAFLAYLLKEGKERGPVLVVCP----LSVLEnweREFEKWTPD--LRVVVYHGSqRERAQ 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4689114  277 KFGPKSSKKFDILVTTPNRLIYLLKQdppgidLASVEW--LVVDE 319
Cdd:cd17919  91 IRAKEKLDKFDVVLTTYETLRRDKAS------LRKFRWdlVVVDE 129
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
190-257 9.89e-04

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 42.23  E-value: 9.89e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4689114  190 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpankGFRALIISPTRELASQIHRELIKI 257
Cdd:COG4581  28 PFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR----GRRSFYTAPIKALSNQKFFDLVER 91
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
209-246 1.18e-03

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 39.51  E-value: 1.18e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4689114  209 APTGSGKTLAFSIPILMQlkqpANKGFRALIISPTREL 246
Cdd:cd01127   6 GTTGSGKTTSIVIPLLDQ----AARGGSVIITDPKGEL 39
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
201-319 1.39e-03

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 40.01  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  201 HGRELLaSAPTGSGKTLAfsIPILMqLKQPANKGFRALIISPTRELASQIHRELIK-----ISEGTGFRIHMIHkaavaa 275
Cdd:cd17990  17 GGQVVL-EAPPGAGKTTR--VPLAL-LAELWIAGGKIIVLEPRRVAARAAARRLATllgeaPGETVGYRVRGES------ 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4689114  276 kkfgpKSSKKFDILVTTPNRLIYLLKQDPpgiDLASVEWLVVDE 319
Cdd:cd17990  87 -----RVGRRTRVEVVTEGVLLRRLQRDP---ELSGVGAVILDE 122
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
209-323 1.79e-03

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members 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: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 38.95  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  209 APTGSGKTLaFSIPILMQLkQPANKGFRALIISPTRELASQIHRELIKISEGTGFRihmihkaavaakkFGPKSSKKFDI 288
Cdd:cd17915   8 SPTGSGKTL-SLLCSALSY-QREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIR-------------ALALSSRDADI 72
                        90       100       110
                ....*....|....*....|....*....|....*
gi 4689114  289 LVTTPNRLIYLLKQDPPGIDLaSVEWLVVDESDKL 323
Cdd:cd17915  73 VVLPYPYLLDARIREFIGIDL-REQVVIIDEAHNL 106
ResIII pfam04851
Type III restriction enzyme, res subunit;
188-320 1.80e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.58  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114    188 PTPIQMQAI----PVMLHGRE-LLASAPTGSGKTL-AFSIPILMQLKQPANKgfrALIISPTRELASQIHRELIKISEGT 261
Cdd:pfam04851   4 LRPYQIEAIenllESIKNGQKrGLIVMATGSGKTLtAAKLIARLFKKGPIKK---VLFLVPRKDLLEQALEEFKKFLPNY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4689114    262 GFRIhmihkaAVAAKKFGPKSSKKFDILVTTPNRL--IYLLKQDPPGIDLASVewLVVDES 320
Cdd:pfam04851  81 VEIG------EIISGDKKDESVDDNKIVVTTIQSLykALELASLELLPDFFDV--IIIDEA 133
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
206-319 2.32e-03

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: 39.56  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114  206 LASAPTGSGKTLafsIPILM------QLKQPANKGFRALIISPTRELASQIHRElikISEGTGFRIHMIHKAAVAAKKFG 279
Cdd:cd18034  20 IVVLPTGSGKTL---IAVMLikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEMGVDKWTK 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4689114  280 PKSS---KKFDILVTTPNRLIYLLKQdppG-IDLASVEWLVVDE 319
Cdd:cd18034  94 ERWKeelEKYDVLVMTAQILLDALRH---GfLSLSDINLLIFDE 134
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
415-524 4.30e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.08  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4689114   415 LVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVE 494
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                         90       100       110
                 ....*....|....*....|....*....|
gi 4689114   495 YIHRIGRTGRAGNKGKAITFFTEDDKPLLR 524
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
 
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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