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Conserved domains on  [gi|299890779|ref|NP_001177729|]
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ATP-dependent RNA helicase DDX19B isoform 3 [Mus musculus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209184)

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

CATH:  3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 75-303 1.15e-143

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


The actual alignment was detected with superfamily member cd18048:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 229  Bit Score: 410.18  E-value: 1.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLS 154
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 155 QVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVSEQIVIGTPGTVLDWCSKLKFIDPK 234
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299890779 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 8.86e-52

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 171.15  E-value: 8.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299890779 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 75-303 1.15e-143

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: 410.18  E-value: 1.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLS 154
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 155 QVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVSEQIVIGTPGTVLDWCSKLKFIDPK 234
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299890779 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
93-460 1.06e-116

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 348.68  E-value: 1.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFA-QCLCLSPT 171
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 244
Cdd:COG0513   81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 245 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREeKFQAL 324
Cdd:COG0513  155 DRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 325 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG0513  233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299890779 405 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFK 460
Cdd:COG0513  313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIG 361
PTZ00424 PTZ00424
helicase 45; Provisional
 91-459 9.50e-96

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 294.43  E-value: 9.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSP 170
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 171 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDE 243
Cdd:PTZ00424 105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 244 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQA 323
Cdd:PTZ00424 179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 324 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 403
Cdd:PTZ00424 258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299890779 404 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHF 459
Cdd:PTZ00424 338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHY 386
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 8.86e-52

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 171.15  E-value: 8.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299890779 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-281 1.38e-36

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: 132.37  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  116 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  196 YAVRGN--KLERGQKVSEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 273
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 299890779  274 SATFEDSV 281
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
107-310 5.38e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.15  E-value: 5.38e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   107 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAVLSQVEPaNKFAQCLCLSPTYELALQTGKVIEQMG 186
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   187 KFYPELKLAYAVRGNKLERGQKVSE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 263
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 299890779   264 LPRNCQMLLFSATFEDSVWKFAQKVVPDPniIKLKREEETLDTIKQY 310
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 319-434 5.04e-32

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: 118.08  E-value: 5.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  319 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 396
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 299890779  397 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 434
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
348-434 7.50e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 103.06  E-value: 7.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   348 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 427
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 299890779   428 GRTGRFG 434
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
333-435 2.65e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.99  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 333 IAQAMIFCHTRKTASWLAAELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG1111  353 DSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432

                         90       100       110
                 ....*....|....*....|....*....|.
gi 299890779 405 VINFDlPVdkdgnPDNETYLHRIGRTGRFGK 435
Cdd:COG1111  433 VIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
 283-432 2.27e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.26  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 283 KFAQKVVPDPNIIKLKRE-----------EETLDTIKQyyVLCNNREEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 351
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 352 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 423
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                 ....*....
gi 299890779 424 LHRIGRTGR 432
Cdd:PRK13766 458 IQRKGRTGR 466
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 75-303 1.15e-143

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: 410.18  E-value: 1.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  75 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLS 154
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 155 QVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVSEQIVIGTPGTVLDWCSKLKFIDPK 234
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299890779 235 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEET 303
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 92-296 2.39e-134

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: 385.61  E-value: 2.39e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  92 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPT 171
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKVSEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 251
Cdd:cd18047   81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 299890779 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd18047  161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 99-296 2.75e-124

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: 359.58  E-value: 2.75e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYELALQT 178
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 179 GKVIEQMGKFyPELKLAYAVRGNKLERGQKVSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQSI 258
Cdd:cd17963   81 GEVVEKMGKF-TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSI 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 299890779 259 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17963  159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
93-460 1.06e-116

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 348.68  E-value: 1.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFA-QCLCLSPT 171
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 244
Cdd:COG0513   81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 245 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREeKFQAL 324
Cdd:COG0513  155 DRML-DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 325 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG0513  233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299890779 405 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFK 460
Cdd:COG0513  313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIG 361
PTZ00424 PTZ00424
helicase 45; Provisional
 91-459 9.50e-96

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 294.43  E-value: 9.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSP 170
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 171 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDE 243
Cdd:PTZ00424 105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 244 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNREEKFQA 323
Cdd:PTZ00424 179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 324 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 403
Cdd:PTZ00424 258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 299890779 404 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHF 459
Cdd:PTZ00424 338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHY 386
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 94-455 9.83e-73

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 235.99  E-value: 9.83e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVE--PANK--FAQCLCLS 169
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKsgPPRILILT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 170 PTYELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkvseQIVIGTPGTVLDWCSKLKFiDPKKIKVFV 240
Cdd:PRK11192  81 PTRELAMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DCRAVETLI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 241 LDEADVMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNIIKL---KREEETldtIKQYYVLC 314
Cdd:PRK11192 153 LDEADRMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---IHQWYYRA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 315 NNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCA 394
Cdd:PRK11192 227 DDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAA 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299890779 395 RGIDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRI 455
Cdd:PRK11192 307 RGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKI 360
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 90-460 6.54e-70

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 229.30  E-value: 6.54e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  90 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLS 169
Cdd:PRK11776   2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 170 PTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 242
Cdd:PRK11776  80 PTRELADQVAKEIRRLARFIPNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 243 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKrEEETLDTIKQYYVLCNNrEEKFQ 322
Cdd:PRK11776 155 EADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSP-DERLP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 323 ALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGIDVE 400
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIK 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 401 QVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFK 460
Cdd:PRK11776 310 ALEAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLG 362
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 94-441 2.42e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 202.06  E-value: 2.42e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVE----PANKF---AQCL 166
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLqtppPKERYmgePRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 167 CLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKVSEQ----IVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 242
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLD 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 243 EADVMIaTQGHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYyVLCNNREEK 320
Cdd:PRK01297 245 EADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQH-VYAVAGSDK 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 321 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 400
Cdd:PRK01297 323 YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 299890779 401 QVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAVN 441
Cdd:PRK01297 403 GISHVINFTLPED----PDD--YVHRIGRTGRAGASGVSIS 437
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 93-446 2.46e-57

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 200.07  E-value: 2.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTY 172
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 173 ELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQKVSEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIa 249
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 250 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQ-YYVLCNNReeKFQALCNLY 328
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 329 GAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINF 408
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 299890779 409 DLPVdkdgnpDNETYLHRIGRTGRFGKRGLAVNMVDSK 446
Cdd:PRK11634 321 DIPM------DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 92-458 2.78e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 187.10  E-value: 2.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  92 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAV----LSQVEPANKFA---Q 164
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTATfhylLSHPAPEDRKVnqpR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 165 CLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKVSEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVL 241
Cdd:PRK04837  86 ALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 242 DEADVMIATQGHQDqsIR--IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYYVLCNNrE 318
Cdd:PRK04837 164 DEADRMFDLGFIKD--IRwlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSN-E 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 319 EKFQALCNLYGAITIAQAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCA 394
Cdd:PRK04837 241 EKMRLLQTLIEEEWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299890779 395 RGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEH 458
Cdd:PRK04837 317 RGLHIPAVTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETY 373
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 87-451 2.72e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 187.85  E-value: 2.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  87 PLYSVkSFEELRLKPQLLQGVYAMGFNRPSKIQenALPLMLAEPPQNLIAQSQSGTGKTAAFVLAVLSQV---------E 157
Cdd:PRK04537   5 PLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQ--ALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 158 PANKFAqcLCLSPTYELALQTGKvieQMGKFYPELKLAYAV--RGNKLERGQKVSEQ---IVIGTPGTVLDWCSKLKFID 232
Cdd:PRK04537  82 PEDPRA--LILAPTRELAIQIHK---DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 233 PKKIKVFVLDEADVMIATQGHQDqsIR-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNiiKLKREEETLDTIK- 308
Cdd:PRK04537 157 LHACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARv 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 309 QYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLV 388
Cdd:PRK04537 233 RQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILV 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299890779 389 TTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNI 451
Cdd:PRK04537 313 ATDVAARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAMSL 369
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 307-443 8.86e-52

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 171.15  E-value: 8.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 307 IKQYYVLCNNREEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 386
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299890779 387 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 443
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 103-296 3.04e-51

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: 172.24  E-value: 3.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEP----ANKFAQCLCLSPTYELALQT 178
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 179 GKVIEQMGKfYPELKLAYAVRGNKLERgQKVSE----QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQ 254
Cdd:cd00268   79 AEVARKLGK-GTGLKVAAIYGGAPIKK-QIEALkkgpDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML-DMGFE 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 299890779 255 DQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd00268  155 EDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 93-443 2.26e-50

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 177.69  E-value: 2.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVL---SQVEPANKF---AQCL 166
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLqhlITRQPHAKGrrpVRAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 167 CLSPTYELALQTGKVIEQMGKFYPELKLAY--AVRGN----KLERGQKVseqiVIGTPGTVLDwCSKLKFIDPKKIKVFV 240
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVfgGVSINpqmmKLRGGVDV----LVATPGRLLD-LEHQNAVKLDQVEILV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 241 LDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKLKREEETLDTIKQYyVLCNNREEK 320
Cdd:PRK10590 155 LDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 321 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 400
Cdd:PRK10590 233 RELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 299890779 401 QVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAVNMV 443
Cdd:PRK10590 313 ELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSLV 349
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 96-295 3.51e-49

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 166.73  E-value: 3.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  96 ELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAEppqNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYEL 174
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTREL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 175 ALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKVSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17939   78 AQQIQKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 299890779 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17939  155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 94-292 7.62e-47

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: 160.93  E-value: 7.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYE 173
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 174 LALQTGKVIEQMGKFypeLKLAYAV-------RGNKLERGQKVseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADV 246
Cdd:cd17940   79 LALQTSQVCKELGKH---MGVKVMVttggtslRDDIMRLYQTV--HVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADK 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 299890779 247 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17940  153 LL-SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 94-292 9.14e-47

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: 160.69  E-value: 9.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTY 172
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 173 ELALQTGKVIEQMGkFYPELKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEAD 245
Cdd:cd18046   78 ELAQQIQKVVMALG-DYMGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEAD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 299890779 246 VMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd18046  152 EML-SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 94-295 2.11e-40

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: 143.76  E-value: 2.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTY 172
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIkPIIKG---RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 173 ELALQTGKVIEQMGKFYpELKLAYAVRGN-------KLERGQkvseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEAD 245
Cdd:cd18045   78 ELAVQIQKVLLALGDYM-NVQCHACIGGTsvgddirKLDYGQ----HIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEAD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 299890779 246 VMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd18045  152 EML-NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
PTZ00110 PTZ00110
helicase; Provisional
 91-439 5.98e-40

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 151.08  E-value: 5.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV--EPANKFAQ---C 165
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHInaQPLLRYGDgpiV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 166 LCLSPTYELALQtgkVIEQMGKFYPELKLAYAVR-GNKLERGQKVS----EQIVIGTPGTVLDW----CSKLKfidpkKI 236
Cdd:PTZ00110 207 LVLAPTRELAEQ---IREQCNKFGASSKIRNTVAyGGVPKRGQIYAlrrgVEILIACPGRLIDFlesnVTNLR-----RV 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 237 KVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNI------IKLKreeeTLDTIKQY 310
Cdd:PTZ00110 279 TYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVhvnvgsLDLT----ACHNIKQE 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 311 YVLCNNREEKFQaLCNLYGAITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLV 388
Cdd:PTZ00110 354 VFVVEEHEKRGK-LKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299890779 389 TTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 439
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGAS 477
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 67-444 4.50e-39

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 148.01  E-value: 4.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  67 RSNLVDNTNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTA 146
Cdd:PLN00206  99 QAELLRRKLEIHVKGEAVPPP---ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 147 AFVLAVLS-------QVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGN----KLERGQKVSEQIVi 215
Cdd:PLN00206 174 SFLVPIISrcctirsGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDampqQLYRIQQGVELIV- 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 216 GTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:PLN00206 252 GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML-ERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILI 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 296 KLKREEETLDTIKQYYVLCNNREEKFQalcnLYGAITIAQ-----AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMV 369
Cdd:PLN00206 329 SIGNPNRPNKAVKQLAIWVETKQKKQK----LFDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSM 404

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299890779 370 EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 444
Cdd:PLN00206 405 KERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 116-281 1.38e-36

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: 132.37  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  116 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 195
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  196 YAVRGN--KLERGQKVSEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 273
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 299890779  274 SATFEDSV 281
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 93-292 4.87e-36

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: 132.08  E-value: 4.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALP-LMLAEppqNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPT 171
Cdd:cd17950    3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPqAILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQTGKVIEQMGKFYPELKLAY-----AVRGNKlERGQKVSEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADV 246
Cdd:cd17950   80 RELAFQISNEYERFSKYMPNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 299890779 247 MIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17950  158 MLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 93-296 1.07e-35

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: 131.27  E-value: 1.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAVLS--QVEPANKFAQCLCLSP 170
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEklKAHSPTVGARALILSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 171 TYELALQTGKVIEQMGKFyPELKLAYAVRGNKLErgqkvsEQ---------IVIGTPGTVLDWCSKLKFiDPKKIKVFVL 241
Cdd:cd17959   80 TRELALQTLKVTKELGKF-TDLRTALLVGGDSLE------EQfealasnpdIIIATPGRLLHLLVEMNL-KLSSVEYVVF 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 299890779 242 DEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17959  152 DEADRLFE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEXDc smart00487
DEAD-like helicases superfamily;
107-310 5.38e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 129.15  E-value: 5.38e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   107 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAVLSQVEPaNKFAQCLCLSPTYELALQTGKVIEQMG 186
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   187 KFYPELKLAYAVRGNKLERGQKVSE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 263
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 299890779   264 LPRNCQMLLFSATFEDSVWKFAQKVVPDPniIKLKREEETLDTIKQY 310
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 103-296 4.81e-34

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: 126.22  E-value: 4.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYELALQTGKVI 182
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 183 EQMGKFYPELKLAYAVRG--NKLERGQKVSEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIR 259
Cdd:cd17943   79 KKIGKKLEGLKCEVFIGGtpVKEDKKKLKGCHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNW 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 299890779 260 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17943  156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 99-297 6.61e-34

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: 126.54  E-value: 6.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVL------SQVEPANKFAQCLCLSPTY 172
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIqkilkaKAESGEEQGTRALILVPTR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 173 ELALQTGKVIEQMGKFY-PELKLAyAVRGNKLERGQKV--SEQ--IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM 247
Cdd:cd17961   79 ELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRAllAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 299890779 248 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNIIKL 297
Cdd:cd17961  158 L-SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 103-285 3.03e-32

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: 121.59  E-value: 3.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV--EPANKFA-QCLCLSPTYELALQTG 179
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLlyRPKKKAAtRVLVLVPTRELAMQCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 180 KVIEQMGKFYPeLKLAYAVRGNKL---ERGQKVSEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQ 256
Cdd:cd17947   79 SVLQQLAQFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADE 156

                        170       180
                 ....*....|....*....|....*....
gi 299890779 257 SIRIQRMLPRNCQMLLFSATFEDSVWKFA 285
Cdd:cd17947  157 LKEILRLCPRTRQTMLFSATMTDEVKDLA 185
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 319-434 5.04e-32

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: 118.08  E-value: 5.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  319 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 396
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 299890779  397 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 434
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 94-292 8.20e-32

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: 120.89  E-value: 8.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVepankfaQCLCLSPTYE 173
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 174 LALQTGKVIEQMGKFY--PELKLAYAVRGNKLERGQKVSEQ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI 248
Cdd:cd17938   72 LAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299890779 249 aTQGHQDQSIRIQRMLP------RNCQMLLFSATFE-DSVWKFAQKVVPDP 292
Cdd:cd17938  151 -SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 93-292 1.90e-31

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: 119.73  E-value: 1.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTY 172
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 173 ELALQTGKVIEQMGKFyPELKLAYAVRG-----NKLERGQKvsEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM 247
Cdd:cd17954   79 ELAQQISEQFEALGSS-IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 299890779 248 IatqgHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17954  156 L----NMDFEPEIDKILkviPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 94-292 5.96e-30

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: 115.78  E-value: 5.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  94 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQ--VEPANKFAqcLCLSPT 171
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRlsEDPYGIFA--LVLTPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQtgkVIEQM---GKFyPELKLAYAVRG-NKLERGQKVSEQ--IVIGTPGTVLDW---CSKLKFiDPKKIKVFVLD 242
Cdd:cd17955   77 RELAYQ---IAEQFralGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLD 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 299890779 243 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17955  152 EADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 99-295 7.15e-29

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: 112.68  E-value: 7.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  99 LKPQLLQGVYAMGFNRPSKIQENALPLMLaEPPQNLIAQSQSGTGKTAAFVL----AVLSQVEPANKFA-QCLCLSPTYE 173
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 174 LALQTGKVIEQMGKFYPELKLAYAVRGNK----LERGQKVSEQIVIGTPG---TVLDWCSKLKFIdpKKIKVFVLDEADV 246
Cdd:cd17964   80 LALQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGrliDHLENPGVAKAF--TDLDYLVLDEADR 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299890779 247 MIaTQGHQDQSIRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNII 295
Cdd:cd17964  158 LL-DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 103-295 1.76e-27

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: 108.40  E-value: 1.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQCLCLSPTYELALQTGKVI 182
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 183 EQMGKFYPELKLAYAVRGNKLErGQ----KVSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 258
Cdd:cd17962   79 KELMKGLPPMKTALLVGGLPLP-PQlyrlQQGVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVL 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 299890779 259 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17962  156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
HELICc smart00490
helicase superfamily c-terminal domain;
348-434 7.50e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 103.06  E-value: 7.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779   348 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 427
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 299890779   428 GRTGRFG 434
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 77-287 1.32e-26

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: 108.13  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  77 VEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV 156
Cdd:cd18052   31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 157 E----PANKFA-----QCLCLSPTYELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkvseQIVIG 216
Cdd:cd18052  106 MkeglTASSFSevqepQALIVAPTRELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVA 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299890779 217 TPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 287
Cdd:cd18052  177 TPGRLLDFIGRGK-ISLSKLKYLILDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 93-286 7.77e-26

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: 104.88  E-value: 7.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  93 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV----EPANKFA----- 163
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLledgPPSVGRGrrkay 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 164 -QCLCLSPTYELALQTgkvieqmgkfYPE-LKLAY-------AVRGNKLERGQKVSEQ----IVIGTPGTVLDWCSKLKf 230
Cdd:cd17967   79 pSALILAPTRELAIQI----------YEEaRKFSYrsgvrsvVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR- 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299890779 231 IDPKKIKVFVLDEADVMIaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 286
Cdd:cd17967  148 ISLSSIKFLVLDEADRML-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 103-281 1.28e-25

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: 103.42  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV---EPANKFAQ--CLCLSPTYELALQ 177
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 178 TGKVIEQMGKFY-PELKLAYAVRGNKLERGQK----VSEQIVIGTPGTVLD-WCSKLKFIDPKKIKVFVLDEADVMIATq 251
Cdd:cd17960   79 IYEVLQSFLEHHlPKLKCQLLIGGTNVEEDVKkfkrNGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL- 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 299890779 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSV 281
Cdd:cd17960  158 GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 104-295 1.86e-22

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: 94.66  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 104 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEpANKFAQ-----CLCLSPTYELALQT 178
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLY-RERWTPedglgALIISPTRELAMQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 179 GKVIEQMGKfYPELKLAYAVRGN--KLERGQKVSEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQ 256
Cdd:cd17941   79 FEVLRKVGK-YHSFSAGLIIGGKdvKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKET 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 299890779 257 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17941  157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 110-296 3.39e-20

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: 88.80  E-value: 3.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 110 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQ------CLCLSPTYELALQTGKVIE 183
Cdd:cd17949    9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 184 QMGKFYPELKLAYAVRGNKlergqKVSEQ--------IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQD 255
Cdd:cd17949   87 KLLKPFHWIVPGYLIGGEK-----RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299890779 256 QSIRIQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNIIK 296
Cdd:cd17949  161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 103-292 3.40e-20

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: 88.42  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEPpqNLIAQSQSGTGKTAAFVLAVLSQVEPANKFA--QCLCLSPTYELALQTGK 180
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 181 VIEQMGKFYPeLKLAYAVRGN--KLERGQKVSEQ--IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATqGHQDQ 256
Cdd:cd17957   79 ELLKLSKGTG-LRIVLLSKSLeaKAKDGPKSITKydILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFREQ 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 299890779 257 SIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17957  156 TDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 91-292 9.38e-20

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: 87.82  E-value: 9.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  91 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV--EPANKFAQ---C 165
Cdd:cd17953   11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPGEgpiG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 166 LCLSPTYELALQtgkVIEQMGKFYPELKL-AYAVRGnklerGQKVSEQI---------VIGTPGTVLDW--CSKLKFIDP 233
Cdd:cd17953   89 LIMAPTRELALQ---IYVECKKFSKALGLrVVCVYG-----GSGISEQIaelkrgaeiVVCTPGRMIDIltANNGRVTNL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299890779 234 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17953  161 RRVTYVVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 103-292 1.44e-19

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: 86.31  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV--EPANKFAQ---CLCLSPTYELALQ 177
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKGEgpiAVIVAPTRELAQQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 178 TGKVIEQMGKFYPELKLAYAVRGNKLERGQKVSE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQD 255
Cdd:cd17952   79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFEY 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 299890779 256 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17952  157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 103-277 1.86e-19

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: 87.29  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAF-------VLAVLSQVEPANKFAQCLCL--SPTYE 173
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFgipilerLLSQKSSNGVGGKQKPLRALilTPTRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 174 LALQTGKVIEQMGKfYPELKLAYAVRG---NKLERGQKVSEQIVIGTPGTVLDW----CSKLKFIdpKKIKVFVLDEADV 246
Cdd:cd17946   80 LAVQVKDHLKAIAK-YTNIKIASIVGGlavQKQERLLKKRPEIVVATPGRLWELiqegNEHLANL--KSLRFLVLDEADR 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 299890779 247 MIaTQGHQDQSIRIQRMLPRNC-------QMLLFSATF 277
Cdd:cd17946  157 ML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 103-295 2.88e-19

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: 86.22  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFV---LAVLSQVEPANKFA-----QCLCLSPTYEL 174
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLiplLVYISRLPPLDEETkddgpYALILAPTREL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 175 ALQTGKVIEQMGKFYPeLKLAYAVRGNKLE-RGQKVSE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17945   79 AQQIEEETQKFAKPLG-IRVVSIVGGHSIEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DM 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299890779 252 GHQDQSIRIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17945  156 GFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 103-295 3.27e-19

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: 85.59  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVE--PANKFAQ----CLCLSPTYELAL 176
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREQRngpgVLVLTPTRELAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 177 QtgkVIEQMGKF-YPELKLA--YAvRGNKLERGQKVSE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQ 251
Cdd:cd17958   79 Q---IEAECSKYsYKGLKSVcvYG-GGNRNEQIEDLSKgvDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-DM 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 299890779 252 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17958  153 GFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 90-277 1.45e-18

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: 85.09  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  90 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV---EPANKFAQ-- 164
Cdd:cd18051   19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSes 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 165 -----------CLCLSPTYELALQtgkVIEQMGKFypelklAY--AVRGNKLERGQKVSEQI---------VIGTPGTVL 222
Cdd:cd18051   97 gyygrrkqyplALVLAPTRELASQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLV 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 299890779 223 DWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 277
Cdd:cd18051  168 DMLERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 104-276 1.53e-18

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: 83.56  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 104 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEpANKFAQ-----CLCLSPTYELALQT 178
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLY-KLKFKPrngtgVIIISPTRELALQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 179 GKVIEQMGKFYPE---LKLAYAVRGNKLERGQKvSEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQD 255
Cdd:cd17942   79 YGVAKELLKYHSQtfgIVIGGANRKAEAEKLGK-GVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEE 156

                        170       180
                 ....*....|....*....|.
gi 299890779 256 QSIRIQRMLPRNCQMLLFSAT 276
Cdd:cd17942  157 EMRQIIKLLPKRRQTMLFSAT 177
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 103-295 1.49e-17

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: 80.85  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQ-VEPANKFAQC-------LCLSPTYEL 174
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLIMFaLEQEKKLPFIkgegpygLIVCPSREL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 175 ALQTGKVIEQMGKF-----YPELKLAYAVRGNKLERGQKVSEQ---IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADV 246
Cdd:cd17951   79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 299890779 247 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNII 295
Cdd:cd17951  158 MI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 103-292 4.88e-17

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: 79.34  E-value: 4.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQ-----CLCLSPTYELALQ 177
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 178 tgkVIEQMGKFYPELKL----AY--AVRGNK---LERGQkvseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI 248
Cdd:cd17966   79 ---IQQEANKFGGSSRLrntcVYggAPKGPQirdLRRGV----EICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 299890779 249 aTQGHQDQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 292
Cdd:cd17966  151 -DMGFEPQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 133-276 1.06e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 68.20  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 133 NLIAQSQSGTGKTAAFVLAVLSQVEPANKFAqcLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKV-- 209
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlg 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 299890779 210 SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 276
Cdd:cd00046   79 DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
141-406 1.18e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 141 GTGKT--AAFVLAVLSQVEPAnkfaqcLCLSPTYELALQTGKVIEQMgkfypeLKLAYAVRGNKlergqKVSEQIVIGTP 218
Cdd:COG1061  110 GTGKTvlALALAAELLRGKRV------LVLVPRRELLEQWAEELRRF------LGDPLAGGGKK-----DSDAPITVATY 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 219 GTVldwcSKLKFID--PKKIKVFVLDEAdvmiatqgHQDQSIRIQRMLPR--NCQMLLFSAT--FEDSVWKF-------- 284
Cdd:COG1061  173 QSL----ARRAHLDelGDRFGLVIIDEA--------HHAGAPSYRRILEAfpAAYRLGLTATpfRSDGREILlflfdgiv 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 285 ---------AQKVVPDPNII----KLKREEETLDTIKQ--YYVLCNNREEKFQALCNLYGAIT-IAQAMIFCHTRKTASW 348
Cdd:COG1061  241 yeyslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299890779 349 LAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 406
Cdd:COG1061  321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 74-291 1.31e-13

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: 70.04  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  74 TNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVL 153
Cdd:cd18049    9 SKEITVRGHNCPKP---VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 154 SQVEpANKFAQ------CLCLSPTYELALQTGKVIEQMGK--------FYPELKLAYAVRgnKLERGQkvseQIVIGTPG 219
Cdd:cd18049   84 VHIN-HQPFLErgdgpiCLVLAPTRELAQQVQQVAAEYGRacrlkstcIYGGAPKGPQIR--DLERGV----EICIATPG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299890779 220 TVLDW--CSKLKFidpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 291
Cdd:cd18049  157 RLIDFleAGKTNL---RRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 112-291 1.40e-13

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: 70.81  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 112 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQVEPANKFAQ-----CLCLSPTYELALQTGKVIEQMG 186
Cdd:cd18050   82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgdgpiCLVLAPTRELAQQVQQVADDYG 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 187 KfYPELKLAYAVRG-------NKLERGQkvseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIR 259
Cdd:cd18050  160 K-SSRLKSTCIYGGapkgpqiRDLERGV----EICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRK 232

                        170       180       190
                 ....*....|....*....|....*....|..
gi 299890779 260 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 291
Cdd:cd18050  233 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
333-435 2.65e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.99  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 333 IAQAMIFCHTRKTASWLAAELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 404
Cdd:COG1111  353 DSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432

                         90       100       110
                 ....*....|....*....|....*....|.
gi 299890779 405 VINFDlPVdkdgnPDNETYLHRIGRTGRFGK 435
Cdd:COG1111  433 VIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 132-287 2.83e-12

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: 65.64  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 132 QNLIAQSQSGTGKTAAFVLAVL------SQVEPANKFAQCLCLSPTYELALQTGKVIEQMGKfypelKLAYAVRGNKLER 205
Cdd:cd17944   28 KDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 206 GQKVSE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSAT 276
Cdd:cd17944  103 QQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSAT 181

                        170
                 ....*....|.
gi 299890779 277 FEDSVWKFAQK 287
Cdd:cd17944  182 CPDWVYNVAKK 192
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 338-434 4.34e-12

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: 63.26  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 415
Cdd:cd18793   32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107

                         90
                 ....*....|....*....
gi 299890779 416 GNPDNEtyLHRIGRTGRFG 434
Cdd:cd18793  108 WNPAVE--EQAIDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 338-434 9.59e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.09  E-value: 9.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 415
Cdd:COG0553  554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630

                         90
                 ....*....|....*....
gi 299890779 416 gNPDNEtyLHRIGRTGRFG 434
Cdd:COG0553  631 -NPAVE--EQAIDRAHRIG 646
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 317-411 2.40e-10

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 58.37  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 317 REEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 377
Cdd:cd18802    5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 299890779 378 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 411
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 103-276 7.53e-10

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: 59.18  E-value: 7.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAE-------PPQNLIAQSQSGTGKTAAFVL----AVLSQVEPAnkfAQCLCLSPT 171
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVPR---LRALIVVPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 172 YELALQTGKVIEQMGK--------------FYPELKLAYAVRGNKLErgqkVSEQIVIGTPGTVLDWCSKLKFIDPKKIK 237
Cdd:cd17956   78 KELVQQVYKVFESLCKgtglkvvslsgqksFKKEQKLLLVDTSGRYL----SRVDILVATPGRLVDHLNSTPGFTLKHLR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299890779 238 VFVLDEAD-------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 276
Cdd:cd17956  154 FLVIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 338-435 8.22e-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: 56.83  E-value: 8.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 417
Cdd:cd18794   35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108

                         90
                 ....*....|....*...
gi 299890779 418 PDNETYLHRIGRTGRFGK 435
Cdd:cd18794  109 KSMESYYQESGRAGRDGL 126
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
338-440 2.88e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 338 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 415
Cdd:COG0514  235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308

                         90       100
                 ....*....|....*....|....*
gi 299890779 416 GNPdnETYLHRIGRTGRFGKRGLAV 440
Cdd:COG0514  309 KSI--EAYYQEIGRAGRDGLPAEAL 331
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 103-290 5.20e-09

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: 56.61  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 103 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAVLSQV-----EPANKF--AQCLCLSPTYELA 175
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLlryklLAEGPFnaPRGLVITPSRELA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 176 LQTGKVIEQMGKFYPeLKlAYAVRGNKLERGQKVSEQ----IVIGTPGTVldwcSKL---KFIDPKKIKVFVLDEADVMI 248
Cdd:cd17948   79 EQIGSVAQSLTEGLG-LK-VKVITGGRTKRQIRNPHFeevdILVATPGAL----SKLltsRIYSLEQLRHLVLDEADTLL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 299890779 249 -------------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 290
Cdd:cd17948  153 ddsfneklshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 336-432 3.54e-08

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: 52.36  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 336 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 405
Cdd:cd18801   33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112

                         90       100
                 ....*....|....*....|....*..
gi 299890779 406 INFdlpvdkDGNPDNETYLHRIGRTGR 432
Cdd:cd18801  113 ICY------DASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 334-440 2.06e-07

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: 53.30  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 334 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 407
Cdd:COG1205  289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368

                         90       100       110
                 ....*....|....*....|....*....|....
gi 299890779 408 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 440
Cdd:COG1205  369 -------AGYPGTRAsFWQQAGRAGRRGQDSLVV 395
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 323-440 4.84e-07

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: 49.18  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 323 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 395
Cdd:cd18797   29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 299890779 396 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 440
Cdd:cd18797  105 GIDIGGLDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 385-437 1.70e-06

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: 45.77  E-value: 1.70e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 299890779 385 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 437
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
PRK13766 PRK13766
Hef nuclease; Provisional
 283-432 2.27e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.26  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 283 KFAQKVVPDPNIIKLKRE-----------EETLDTIKQyyVLCNNREEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 351
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 352 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 423
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                 ....*....
gi 299890779 424 LHRIGRTGR 432
Cdd:PRK13766 458 IQRKGRTGR 466
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 114-276 7.03e-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: 46.26  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 114 RPSKIQENALPL----MLAEPPQNLIAQSQSGTGKTAAFVLAVLSQVEPAnkfAQCLCLSPTYELALQTGKVIEqmgKFY 189
Cdd:cd17918   15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNG---KQVAILVPTEILAHQHYEEAR---KFL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 190 PELKLAYAVRGNKlergQKVSEQI--VIGTpgtvldwcSKLKFIDPKKikvfvlDEADVMIATQGHQ---DQSIRIQRMl 264
Cdd:cd17918   89 PFINVELVTGGTK----AQILSGIslLVGT--------HALLHLDVKF------KNLDLVIVDEQHRfgvAQREALYNL- 149

                        170
                 ....*....|..
gi 299890779 265 pRNCQMLLFSAT 276
Cdd:cd17918  150 -GATHFLEATAT 160
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 337-434 1.01e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 337 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 416
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317

                         90
                 ....*....|....*...
gi 299890779 417 npdnETYLHRIGRTGRFG 434
Cdd:PRK11057 318 ----ESYYQETGRAGRDG 331
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 360-450 1.90e-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: 44.95  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 438
Cdd:cd18792   63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136

                         90
                 ....*....|..
gi 299890779 439 AVNMVDSKHSMN 450
Cdd:cd18792  137 CYLLYPDPKKLT 148
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 335-444 2.14e-05

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: 44.47  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 335 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 414
Cdd:cd18795   45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 299890779 415 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 444
Cdd:cd18795  121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 342-432 2.77e-05

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: 44.54  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 342 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 421
Cdd:cd18790   36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113

                         90
                 ....*....|..
gi 299890779 422 TYL-HRIGRTGR 432
Cdd:cd18790  114 TSLiQTIGRAAR 125
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 344-406 3.34e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 3.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299890779 344 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 406
Cdd:PRK10917 490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 360-456 5.05e-05

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.49  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 438
Cdd:cd18811   64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137

                         90
                 ....*....|....*...
gi 299890779 439 AVNMVDSKHSMNILNRIQ 456
Cdd:cd18811  138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 334-406 1.22e-04

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: 44.48  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299890779 334 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 406
Cdd:COG4098  320 RQLLIFVPTIELLEQLVALLQKLFPEERIAG----VhaedPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAV 392
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 349-454 1.61e-04

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


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 42.29  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 349 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 423
Cdd:cd18798   43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 299890779 424 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNR 454
Cdd:cd18798  110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKK 144
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 338-432 2.39e-04

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: 41.48  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 338 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 411
Cdd:cd18796   43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119

                         90       100
                 ....*....|....*....|..
gi 299890779 412 vdkdGNPDNET-YLHRIGRTGR 432
Cdd:cd18796  120 ----GSPKSVArLLQRLGRSGH 137
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 132-244 3.39e-04

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 41.87  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 132 QNLIAQSQSGTGKT--AAFVL-AVLSQV---EPANKFaqCLCLSPTYELALQTGKVIEQ-----MGKFYPELKLAYAVRG 200
Cdd:cd18034   17 RNTIVVLPTGSGKTliAVMLIkEMGELNrkeKNPKKR--AVFLVPTVPLVAQQAEAIRShtdlkVGEYSGEMGVDKWTKE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 299890779 201 NKLERGQKVseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 244
Cdd:cd18034   95 RWKEELEKY--DVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 337-440 4.80e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779  337 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 416
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763

                          90       100
                  ....*....|....*....|....
gi 299890779  417 npdnetYLHRIGRTGRFGKRGLAV 440
Cdd:PLN03137  764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 360-450 8.93e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 39.63  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 360 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 438
Cdd:cd18810   54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127

                         90
                 ....*....|..
gi 299890779 439 AVNMVDSKHSMN 450
Cdd:cd18810  128 AYFLYPDQKKLT 139
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
344-399 2.10e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.42  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 299890779 344 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 399
Cdd:COG1200  488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 238-436 3.51e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 39.34  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 238 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpniiklkREEETLDTI---KQYYVL 313
Cdd:cd09639  126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 314 CNNRE-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 385
Cdd:cd09639  197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299890779 386 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 436
Cdd:cd09639  277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 333-412 7.14e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 36.38  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890779 333 IAQAMIFCHTRKTASWLAAELSKEG-HQVALLSGEMMVEQRAAVIER--FREGKEKVLVTTNVCARGIDVEQVSVVInFD 409
Cdd:cd18799    6 EIKTLIFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDEALILlfFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84


                 ...
gi 299890779 410 LPV 412
Cdd:cd18799   85 RPT 87
 
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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