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Conserved domains on  [gi|380503835|ref|NP_001244101|]
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ATP-dependent RNA helicase DDX19B isoform 4 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13208438)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
80-277 7.79e-116

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: 452890 [Multi-domain]  Cd Length: 229  Bit Score: 338.92  E-value: 7.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  80 NQVEVLQRDPNSPLYSVKSFEELRL-------------------------------PQNLIAQSQSGTGKTAAFVLAMLS 128
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLkeellrgiyamgfnrpskiqenalpmmladpPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 129 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 208
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380503835 209 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 277
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
106-452 4.49e-98

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


:

Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 303.64  E-value: 4.49e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NK 176
Cdd:COG0513   67 RDVLGQAQTGTGKTAAFLLPLLQKIlkSVERKYVSALILAPTRELAVQIAEELRKLGKNLGGLRVAVVYGGvsirkqiEA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 177 LERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVW 256
Cdd:COG0513  147 LKRGV----DIVVATPGRLLDLIKR-GKLDLSGVETLVLDEAD-RMLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIR 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 257 KFAQKVVPDPNVIKLKRE--EETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQV 334
Cdd:COG0513  221 ELARRYLNDPVEIEVSVEklERTLKKIKQFYLEVESEEEKLELLLKLLKDEDEGRVIVFVRTKRLVEELAESLRKRGFKV 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 335 ALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAV 414
Cdd:COG0513  301 AALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVSHVINYDLPLDP------EDYVHRIGRTGRAGRKGVAI 374
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 380503835 415 NMVDSKHSMNILNRIQEHFNKKIE---RLDTDDLDEIEKIA 452
Cdd:COG0513  375 SFVTEEEEVKKLKRIEKRLERKLPsavLLPLDEPEDAKLLK 415
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
80-277 7.79e-116

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: 338.92  E-value: 7.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  80 NQVEVLQRDPNSPLYSVKSFEELRL-------------------------------PQNLIAQSQSGTGKTAAFVLAMLS 128
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLkeellrgiyamgfnrpskiqenalpmmladpPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 129 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 208
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380503835 209 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 277
Cdd:cd18048  161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
106-452 4.49e-98

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


Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 303.64  E-value: 4.49e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NK 176
Cdd:COG0513   67 RDVLGQAQTGTGKTAAFLLPLLQKIlkSVERKYVSALILAPTRELAVQIAEELRKLGKNLGGLRVAVVYGGvsirkqiEA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 177 LERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVW 256
Cdd:COG0513  147 LKRGV----DIVVATPGRLLDLIKR-GKLDLSGVETLVLDEAD-RMLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIR 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 257 KFAQKVVPDPNVIKLKRE--EETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQV 334
Cdd:COG0513  221 ELARRYLNDPVEIEVSVEklERTLKKIKQFYLEVESEEEKLELLLKLLKDEDEGRVIVFVRTKRLVEELAESLRKRGFKV 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 335 ALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAV 414
Cdd:COG0513  301 AALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVSHVINYDLPLDP------EDYVHRIGRTGRAGRKGVAI 374
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 380503835 415 NMVDSKHSMNILNRIQEHFNKKIE---RLDTDDLDEIEKIA 452
Cdd:COG0513  375 SFVTEEEEVKKLKRIEKRLERKLPsavLLPLDEPEDAKLLK 415
PTZ00424 PTZ00424
helicase 45; Provisional
109-443 3.40e-85

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 266.69  E-value: 3.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 109 IAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQ 181
Cdd:PTZ00424  69 IGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 kiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQK 261
Cdd:PTZ00424 148 ----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTK 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 262 VVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEM 341
Cdd:PTZ00424 222 FMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDM 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 342 MVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKh 421
Cdd:PTZ00424 302 DQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD- 374
                        330       340
                 ....*....|....*....|..
gi 380503835 422 SMNILNRIQEHFNKKIERLDTD 443
Cdd:PTZ00424 375 DIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
281-417 3.62e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 169.23  E-value: 3.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 281 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 360
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380503835 361 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 417
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
97-255 3.14e-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: 131.21  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   97 KSFEELRLPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLAYAVRGN- 175
Cdd:pfam00270   6 EAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASLLGGDs 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  176 -KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDS 254
Cdd:pfam00270  85 rKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLLSATLPRN 161

                  .
gi 380503835  255 V 255
Cdd:pfam00270 162 L 162
DEXDc smart00487
DEAD-like helicases superfamily;
102-284 6.79e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.67  E-value: 6.79e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   102 LRLPQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQ 181
Cdd:smart00487  21 LSGLRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   182 KISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:smart00487 100 KLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKLLPKNVQLLLLSATPPEEIENL 177
                          170       180
                   ....*....|....*....|....*.
gi 380503835   259 AQKVVPDPNVIklKREEETLDTIKQY 284
Cdd:smart00487 178 LELFLNDPVFI--DVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
293-408 2.26e-31

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: 425571 [Multi-domain]  Cd Length: 109  Bit Score: 116.16  E-value: 2.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  293 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 370
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380503835  371 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 408
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
322-408 2.32e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.52  E-value: 2.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   322 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 401
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 380503835   402 GRTGRFG 408
Cdd:smart00490  76 GRAGRAG 82
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
91-419 4.33e-12

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


Pssm-ID: 224126 [Multi-domain]  Cd Length: 851  Bit Score: 68.20  E-value: 4.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  91 SPLYS--VKSFEELRLPQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYpqcLCLSPTYELAL-QTGKVIEQMGKFYPE 165
Cdd:COG1205   69 ERLYShqVDALRLIREGRNVVVTTGTGSGKTESFLLPILDHLlrDPSARA---LLLYPTNALANdQAERLRELISDLPGK 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 166 LKLA-Y--AVRGNklERGQKISEQ--IVIGTPgTVLDW------------CSKLKFIdpkkikvfVLDEADVMIATQGhq 228
Cdd:COG1205  146 VTFGrYtgDTPPE--ERRAIIRNPpdILLTNP-DMLHYlllrnhdawlwlLRNLKYL--------VVDELHTYRGVQG-- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 229 dqSI------RIQRML---PRNCQMLLFSAT-------FEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRD 292
Cdd:COG1205  213 --SEvalllrRLLRRLrryGSPLQIICTSATlanpgefAEELFGRDFEVPVDEDGSPRGLRYFVRREPPIRELAESIRRS 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 293 -----EKFQALCNLYGAITIAqamiFCHTRK----TASWLAAELSKEGH--QVALLS--GEMMVEQRAAVIERFREGKEK 359
Cdd:COG1205  291 alaelATLAALLVRNGIQTLV----FFRSRKqvelLYLSPRRRLVREGGklLDAVSTyrAGLHREERRRIEAEFKEGELL 366
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380503835 360 VLVTTNVCARGIDVEQVSVVINfdlpvdkDGNPDNETYLH--RIGRTGRFGKRGLAVNMVDS 419
Cdd:COG1205  367 GVIATNALELGIDIGSLDAVIA-------YGYPGVSVLSFrqRAGRAGRRGQESLVLVVLRS 421
PRK13766 PRK13766
Hef nuclease; Provisional
257-406 1.59e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.64  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 257 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 325
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 326 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 397
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                 ....*....
gi 380503835 398 LHRIGRTGR 406
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 ...
80-277 7.79e-116

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: 338.92  E-value: 7.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  80 NQVEVLQRDPNSPLYSVKSFEELRL-------------------------------PQNLIAQSQSGTGKTAAFVLAMLS 128
Cdd:cd18048    1 HRVEVLQRDPTSPLFSVKSFEELHLkeellrgiyamgfnrpskiqenalpmmladpPQNLIAQSQSGTGKTAAFVLAMLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 129 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 208
Cdd:cd18048   81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380503835 209 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 277
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 ...
105-270 5.19e-106

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: 312.81  E-value: 5.19e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 105 PQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKIS 184
Cdd:cd18047   40 PQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKIS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 185 EQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVP 264
Cdd:cd18047  120 EQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVP 199

                 ....*.
gi 380503835 265 DPNVIK 270
Cdd:cd18047  200 DPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
105-270 4.09e-101

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: 299.88  E-value: 4.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 105 PQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERGQKIS 184
Cdd:cd17963   33 PENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEVVEKMGKF-TGVKVALAVPGNDVPRGKKIT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 185 EQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVP 264
Cdd:cd17963  112 AQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAP 190

                 ....*.
gi 380503835 265 DPNVIK 270
Cdd:cd17963  191 NANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
106-452 4.49e-98

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


Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 303.64  E-value: 4.49e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NK 176
Cdd:COG0513   67 RDVLGQAQTGTGKTAAFLLPLLQKIlkSVERKYVSALILAPTRELAVQIAEELRKLGKNLGGLRVAVVYGGvsirkqiEA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 177 LERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVW 256
Cdd:COG0513  147 LKRGV----DIVVATPGRLLDLIKR-GKLDLSGVETLVLDEAD-RMLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIR 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 257 KFAQKVVPDPNVIKLKRE--EETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQV 334
Cdd:COG0513  221 ELARRYLNDPVEIEVSVEklERTLKKIKQFYLEVESEEEKLELLLKLLKDEDEGRVIVFVRTKRLVEELAESLRKRGFKV 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 335 ALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAV 414
Cdd:COG0513  301 AALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVSHVINYDLPLDP------EDYVHRIGRTGRAGRKGVAI 374
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 380503835 415 NMVDSKHSMNILNRIQEHFNKKIE---RLDTDDLDEIEKIA 452
Cdd:COG0513  375 SFVTEEEEVKKLKRIEKRLERKLPsavLLPLDEPEDAKLLK 415
PTZ00424 PTZ00424
helicase 45; Provisional
109-443 3.40e-85

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 266.69  E-value: 3.40e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 109 IAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQ 181
Cdd:PTZ00424  69 IGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 kiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQK 261
Cdd:PTZ00424 148 ----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTK 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 262 VVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEM 341
Cdd:PTZ00424 222 FMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDM 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 342 MVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKh 421
Cdd:PTZ00424 302 DQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD- 374
                        330       340
                 ....*....|....*....|..
gi 380503835 422 SMNILNRIQEHFNKKIERLDTD 443
Cdd:PTZ00424 375 DIEQLKEIERHYNTQIEEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
106-446 1.52e-63

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 211.97  E-value: 1.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NKLE 178
Cdd:PRK11776  42 KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFIPNIKVLTLCGGvpmgpqiDSLE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:PRK11776 122 HGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLDEADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAI 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 259 AQKVVPDPNVIKLKrEEETLDTIKQYYVLCSsRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLS 338
Cdd:PRK11776 196 SQRFQRDPVEVKVE-STHDLPAIEQRFYEVS-PDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALH 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 339 GEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNM 416
Cdd:PRK11776 274 GDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSL 345
                        330       340       350
                 ....*....|....*....|....*....|
gi 380503835 417 VdSKHSMNILNRIQEHFNKKIERLDTDDLD 446
Cdd:PRK11776 346 V-APEEMQRANAIEDYLGRKLNWEPLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
115-445 8.84e-59

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 199.01  E-value: 8.84e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 115 GTGKTAAFVLAMLSQVE--PANK--YPQCLCLSPTYELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQ 181
Cdd:PRK11192  48 GTGKTAAFLLPALQHLLdfPRRKsgPPRILILTPTRELAMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 kiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKF 258
Cdd:PRK11192 125 ----DIVVATPGRLLQYIKEENF-DCRAVETLILDEADRMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDF 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 259 AQKVVPDPNVIKL---KREEETldtIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVA 335
Cdd:PRK11192 197 AERLLNDPVEVEAepsRRERKK---IHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCC 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 336 LLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVN 415
Cdd:PRK11192 274 YLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAIS 347
                        330       340       350
                 ....*....|....*....|....*....|
gi 380503835 416 MVDSkHSMNILNRIQEHFNKKIERLDTDDL 445
Cdd:PRK11192 348 LVEA-HDHLLLGKIERYIEEPLKARVIDEL 376
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
106-438 1.63e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 188.58  E-value: 1.63e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVE----PANKY---PQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLE 178
Cdd:PRK01297 125 HDAIGRAQTGTGKTAAFLISIINQLLqtppPKERYmgePRALIIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFD 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQKISEQ----IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC--QMLLFSATFE 252
Cdd:PRK01297 204 KQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLDEADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFT 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 253 DSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGH 332
Cdd:PRK01297 282 DDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGI 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 333 QVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGL 412
Cdd:PRK01297 361 NAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPED----PDD--YVHRIGRTGRAGASGV 434
                        330       340
                 ....*....|....*....|....*.
gi 380503835 413 AVNMVDSKHSMNiLNRIQEHFNKKIE 438
Cdd:PRK01297 435 SISFAGEDDAFQ-LPEIEELLGRKIS 459
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
281-417 3.62e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 169.23  E-value: 3.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 281 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 360
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380503835 361 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 417
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
106-420 7.33e-51

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 181.97  E-value: 7.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQK 182
Cdd:PRK11634  44 RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 183 ISEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKV 262
Cdd:PRK11634 124 QGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML-RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRF 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 263 VPDPNVIKLKREEETLDTIKQ-YYVLCSSRdeKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEM 341
Cdd:PRK11634 202 MKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDM 279
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380503835 342 MVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVdkdgnpDNETYLHRIGRTGRFGKRGLAVNMVDSK 420
Cdd:PRK11634 280 NQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM------DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
102-437 5.87e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 169.77  E-value: 5.87e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 102 LRLP-----QNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY---PQCLCLSPTYELALQTGKVIEQMGKfYPELKLA 169
Cdd:PRK04837  37 LALPltlagRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPRALIMAPTRELAVQIHADAEPLAQ-ATGLKLG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 170 YAVRGNKLERGQKISEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATQGHQDqsIR--IQRMLPRNCQM 244
Cdd:PRK04837 116 LAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVLDEADRMFDLGFIKD--IRwlFRRMPPANQRL 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 245 -LLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ--YYvlcSSRDEKFQALCNLYGAITIAQAMIFCHTR---- 317
Cdd:PRK04837 193 nMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PSNEEKMRLLQTLIEEEWPDRAIIFANTKhrce 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 318 KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETY 397
Cdd:PRK04837 270 EIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLP------DDCEDY 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 380503835 398 LHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 437
Cdd:PRK04837 340 VHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSI 378
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
104-437 7.98e-48

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 172.83  E-value: 7.98e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 104 LPQNLIA-QSQSGTGKTAAFVLA----MLSQVEPANKYPQ---CLCLSPTYELALQTGKvieQMGKFYPELKLAYAV--R 173
Cdd:PRK04537  44 LPGGDVAgQAQTGTGKTLAFLVAvmnrLLSRPALADRKPEdprALILAPTRELAIQIHK---DAVKFGADLGLRFALvyG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 174 GNKLERGQKISEQ---IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDqsIR-IQRMLPRNC--QMLLF 247
Cdd:PRK04537 121 GVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLF 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 248 SATFEDSVWKFAQKVVPDPNviKLKREEETLDTIK-QYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAE 326
Cdd:PRK04537 199 SATLSHRVLELAYEHMNEPE--KLVVETETITAARvRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVART 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 327 LSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGR 406
Cdd:PRK04537 277 LERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTAR 350
                        330       340       350
                 ....*....|....*....|....*....|.
gi 380503835 407 FGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 437
Cdd:PRK04537 351 LGEEGDAISFACERYAMS-LPDIEAYIEQKI 380
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
106-270 2.15e-43

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: 151.06  E-value: 2.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEP----ANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKlAYAVRGnklerGQ 181
Cdd:cd00268   28 RDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAEVARKLGK-GTGLK-VAAIYG-----GA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 KISEQ---------IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFE 252
Cdd:cd00268  101 PIKKQiealkkgpdIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML-DMGFEEDVEKILSALPKDRQTLLFSATLP 178
                        170
                 ....*....|....*...
gi 380503835 253 DSVWKFAQKVVPDPNVIK 270
Cdd:cd00268  179 EEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
106-417 9.96e-42

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 153.81  E-value: 9.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAML-----SQVEPANKYP-QCLCLSPTYELALQTGKVIEQMGKFYPELKLAyaVRGnkler 179
Cdd:PRK10590  39 RDLMASAQTGTGKTAGFTLPLLqhlitRQPHAKGRRPvRALILTPTRELAAQIGENVRDYSKYLNIRSLV--VFG----- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKISEQ---------IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSAT 250
Cdd:PRK10590 112 GVSINPQmmklrggvdVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSAT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 251 FEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYyVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKE 330
Cdd:PRK10590 190 FSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKD 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 331 GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGK 409
Cdd:PRK10590 269 GIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPnVPED-------YVHRIGRTGRAAA 341

                 ....*...
gi 380503835 410 RGLAVNMV 417
Cdd:PRK10590 342 TGEALSLV 349
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
109-269 2.43e-38

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: 137.84  E-value: 2.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 109 IAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKISE 185
Cdd:cd17939   38 IAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGP 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 186 QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 265
Cdd:cd17939  117 HIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRD 194

                 ....
gi 380503835 266 PNVI 269
Cdd:cd17939  195 PVRI 198
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
97-255 3.14e-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: 131.21  E-value: 3.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   97 KSFEELRLPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLAYAVRGN- 175
Cdd:pfam00270   6 EAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASLLGGDs 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  176 -KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDS 254
Cdd:pfam00270  85 rKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLLSATLPRN 161

                  .
gi 380503835  255 V 255
Cdd:pfam00270 162 L 162
PTZ00110 PTZ00110
helicase; Provisional
106-413 2.49e-35

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 137.60  E-value: 2.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQtgkVIEQMGKFYPELKLAYAV-RGNKLER 179
Cdd:PTZ00110 168 RDMIGIAETGSGKTLAFLLPAIVHInaQPLLRYgdgPIVLVLAPTRELAEQ---IREQCNKFGASSKIRNTVaYGGVPKR 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKIS----EQIVIGTPGTVLDW----CSKLKfidpkKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATF 251
Cdd:PTZ00110 245 GQIYAlrrgVEILIACPGRLIDFlesnVTNLR-----RVTYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATW 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 252 EDSVWKFAQKVVPDP----NV--IKLKreeeTLDTIKQYYVLCSSRdEKFQALCNLYGAITI--AQAMIFCHTRKTASWL 323
Cdd:PTZ00110 319 PKEVQSLARDLCKEEpvhvNVgsLDLT----ACHNIKQEVFVVEEH-EKRGKLKMLLQRIMRdgDKILIFVETKKGADFL 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 324 AAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGR 403
Cdd:PTZ00110 394 TKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGR 467
                        330
                 ....*....|
gi 380503835 404 TGRFGKRGLA 413
Cdd:PTZ00110 468 TGRAGAKGAS 477
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
107-266 1.23e-34

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: 127.95  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGkFYPELKLAYAVRG-------NKLER 179
Cdd:cd18046   38 DVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALG-DYMGIKCHACIGGtsvrddaQKLQA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 259
Cdd:cd18046  117 GP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEML-SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVT 190

                 ....*..
gi 380503835 260 QKVVPDP 266
Cdd:cd18046  191 TKFMRDP 197
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
106-418 1.73e-34

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 134.92  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLS-------QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGN--- 175
Cdd:PLN00206 159 RSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDamp 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 176 -KLERGQKISEQIViGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNcQMLLFSATFEDS 254
Cdd:PLN00206 238 qQLYRIQQGVELIV-GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML-ERGFRDQVMQIFQALSQP-QVLLFSATVSPE 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 255 VWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQalcnLYGAITIAQ-----AMIFCHTRKTASWLAAELSK 329
Cdd:PLN00206 314 VEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----LFDILKSKQhfkppAVVFVSSRLGADLLANAITV 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 330 -EGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFG 408
Cdd:PLN00206 390 vTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMG 463
                        330
                 ....*....|
gi 380503835 409 KRGLAVNMVD 418
Cdd:PLN00206 464 EKGTAIVFVN 473
DEXDc smart00487
DEAD-like helicases superfamily;
102-284 6.79e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.67  E-value: 6.79e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   102 LRLPQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQ 181
Cdd:smart00487  21 LSGLRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   182 KISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:smart00487 100 KLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKLLPKNVQLLLLSATPPEEIENL 177
                          170       180
                   ....*....|....*....|....*.
gi 380503835   259 AQKVVPDPNVIklKREEETLDTIKQY 284
Cdd:smart00487 178 LELFLNDPVFI--DVGFTPLEPIEQF 201
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
106-269 8.87e-32

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: 120.10  E-value: 8.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKL-ERGQKIS 184
Cdd:cd17940   37 RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKELGK-HMGVKVMVTTGGTSLrDDIMRLY 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 185 E--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKV 262
Cdd:cd17940  116 QtvHVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADKLL-SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRH 193

                 ....*..
gi 380503835 263 VPDPNVI 269
Cdd:cd17940  194 MHNPYEI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
293-408 2.26e-31

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: 425571 [Multi-domain]  Cd Length: 109  Bit Score: 116.16  E-value: 2.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  293 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 370
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380503835  371 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 408
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
106-269 3.89e-30

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: 115.64  E-value: 3.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLAYAVRGN-------KLE 178
Cdd:cd18045   37 RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYM-NVQCHACIGGTsvgddirKLD 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:cd18045  116 YGQ----HIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEML-NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEM 189
                        170
                 ....*....|.
gi 380503835 259 AQKVVPDPNVI 269
Cdd:cd18045  190 TNKFMTDPIRI 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
108-270 1.14e-27

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: 108.89  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 108 LIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERG-QKISE- 185
Cdd:cd17943   30 LIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLEGLKCEVFIGGTPVKEDkKKLKGc 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 186 QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVP 264
Cdd:cd17943  110 HIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMR 186

                 ....*.
gi 380503835 265 DPNVIK 270
Cdd:cd17943  187 KPVLVR 192
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
104-266 2.02e-27

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: 108.59  E-value: 2.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 104 LPQ-----NLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAY-----AVR 173
Cdd:cd17950   33 IPQailgmDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNVKTAVffggvPIK 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 174 GNKlERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFED 253
Cdd:cd17950  113 KDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKMLEQLDMRRDVQEIFRATPHDKQVMMFSATLSK 190
                        170
                 ....*....|...
gi 380503835 254 SVWKFAQKVVPDP 266
Cdd:cd17950  191 EIRPVCKKFMQDP 203
HELICc smart00490
helicase superfamily c-terminal domain;
322-408 2.32e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.52  E-value: 2.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835   322 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 401
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 380503835   402 GRTGRFG 408
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
105-270 1.60e-25

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: 103.15  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 105 PQNLIAQSQSGTGKTAAFVLAMLS--QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERG-Q 181
Cdd:cd17959   38 GRDVVAMARTGSGKTAAFLIPMIEklKAHSPTVGARALILSPTRELALQTLKVTKELGKF-TDLRTALLVGGDSLEEQfE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 KISEQ--IVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 259
Cdd:cd17959  117 ALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRLFE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFA 194
                        170
                 ....*....|.
gi 380503835 260 QKVVPDPNVIK 270
Cdd:cd17959  195 KAGLNEPVLIR 205
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
106-271 3.09e-25

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: 102.28  E-value: 3.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY-PELKLAyAVRGNKLE 178
Cdd:cd17961   32 KDILARARTGSGKTAAYALPIIqkilkaKAESGEEQGTRALILVPTRELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQK--ISEQ--IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDS 254
Cdd:cd17961  111 SVQRalLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVL-SYGYEEDLKSLLSYLPKNYQTFLMSATLSED 189
                        170
                 ....*....|....*..
gi 380503835 255 VWKFAQKVVPDPNVIKL 271
Cdd:cd17961  190 VEALKKLVLHNPAILKL 206
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
104-266 7.42e-25

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: 101.09  E-value: 7.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 104 LPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGN----KLER 179
Cdd:cd17962   26 LGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLPPMKTALLVGGLplppQLYR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKiSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 259
Cdd:cd17962  106 LQQ-GVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVLDILENISHDHQTILVSATIPRGIEQLA 182

                 ....*..
gi 380503835 260 QKVVPDP 266
Cdd:cd17962  183 GQLLQNP 189
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
108-259 7.13e-24

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: 98.48  E-value: 7.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 108 LIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGNKL---ERGQ 181
Cdd:cd17947   30 ICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFTD-ITFALAVGGLSLkaqEAAL 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380503835 182 KISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 259
Cdd:cd17947  109 RARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADELKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
102-269 4.25e-23

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: 96.50  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 102 LRLPQNLIAQSQSGTGKTAAFVL----AMLSQVEPANKYP-QCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNK 176
Cdd:cd17964   29 LSTGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRELALQIAAEAKKLLQGLRKLRVQSAVGGTS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 177 ----LERGQKISEQIVIGTPG---TVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC----QML 245
Cdd:cd17964  109 rraeLNRLRRGRPDILVATPGrliDHLENPGVAKAF--TDLDYLVLDEADRLL-DMGFRPDLEQILRHLPEKNadprQTL 185
                        170       180
                 ....*....|....*....|....*
gi 380503835 246 LFSATFEDSVWKFAQKVV-PDPNVI 269
Cdd:cd17964  186 LFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
109-266 1.71e-22

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: 94.70  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 109 IAQSQSGTGKTAAFVLAMLSQVepankypQCLCLSPTYELALQTGKVIEQMGKFY--PELKLAYAVRGNKLERGQKISEQ 186
Cdd:cd17938   40 LMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLES 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 187 ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLP------RNCQMLLFSATFE-DSVW 256
Cdd:cd17938  113 gvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL-SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHsFEVK 190
                        170
                 ....*....|
gi 380503835 257 KFAQKVVPDP 266
Cdd:cd17938  191 KLADKIMHFP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
107-266 1.82e-20

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: 88.91  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFyPELKLAYAVRG-----NKLERGQ 181
Cdd:cd17954   39 DIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELAQQISEQFEALGSS-IGLKSAVLVGGmdmmaQAIALAK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 182 KisEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIatqgHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKF 258
Cdd:cd17954  118 K--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLL----NMDFEPEIDKILkviPRERTTYLFSATMTTKVAKL 191

                 ....*...
gi 380503835 259 AQKVVPDP 266
Cdd:cd17954  192 QRASLKNP 199
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
106-266 1.91e-20

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: 88.82  E-value: 1.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYpqCLCLSPTYELALQtgkVIEQM---GKFyPELKLAYAVRG-NKLER 179
Cdd:cd17955   37 RDVIGGAKTGSGKTAAFALPILQRlsEDPYGIF--ALVLTPTRELAYQ---IAEQFralGAP-LGLRCCVIVGGmDMVKQ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKISEQ--IVIGTPGTVLDW---CSKLKFiDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDS 254
Cdd:cd17955  111 ALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLDEADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDA 188
                        170
                 ....*....|..
gi 380503835 255 VWKFAQKVVPDP 266
Cdd:cd17955  189 LKALKELFGNKP 200
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
108-260 7.21e-20

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: 87.93  E-value: 7.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 108 LIAQSQSGTGKTAAFVLAMLSQV--EPANK--------YPQCLCLSPTYELALQTgkvieqmgkfYPE-LKLAY------ 170
Cdd:cd17967   40 LMACAQTGSGKTAAFLLPIISKLleDGPPSvgrgrrkaYPSALILAPTRELAIQI----------YEEaRKFSYrsgvrs 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 171 -AVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQsirIQRML------- 238
Cdd:cd17967  110 vVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR-ISLSSIKFLVLDEADRML-DMGFEPQ---IRKIVehpdmpp 184
                        170       180
                 ....*....|....*....|..
gi 380503835 239 PRNCQMLLFSATFEDSVWKFAQ 260
Cdd:cd17967  185 KGERQTLMFSATFPREIQRLAA 206
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
106-255 1.88e-19

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: 86.09  E-value: 1.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQ--CLCLSPTYELALQTGKVIEQMGKFY-PELKLAYAVRGNKLER 179
Cdd:cd17960   28 KDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIYEVLQSFLEHHlPKLKCQLLIGGTNVEE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKI----SEQIVIGTPGTVLD-WCSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDS 254
Cdd:cd17960  108 DVKKfkrnGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL-GFEADLNRILSKLPKQRRTGLFSATQTDA 186

                 .
gi 380503835 255 V 255
Cdd:cd17960  187 V 187
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
82-261 3.38e-18

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: 83.86  E-value: 3.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  82 VEVLQRDPNSPlysVKSFEELRLPQ-----------------------------NLIAQSQSGTGKTAAFVLAMLSQ--- 129
Cdd:cd18052   31 VEVTGRNPPPA---ILTFEEANLCEtllknirkagyekptpvqkyaipiilagrDLMACAQTGSGKTAAFLLPVLTGmmk 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 130 --VEPAN----KYPQCLCLSPTYELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIGTP 192
Cdd:cd18052  108 egLTASSfsevQEPQALIVAPTRELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVATP 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380503835 193 GTVLDWCSKLKfIDPKKIKVFVLDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 261
Cdd:cd18052  179 GRLLDFIGRGK-ISLSKLKYLILDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
106-269 1.04e-16

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: 78.23  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERG 180
Cdd:cd17952   28 RDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 181 QKISE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:cd17952  108 KALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQL 185
                        170
                 ....*....|.
gi 380503835 259 AQKVVPDPNVI 269
Cdd:cd17952  186 ARDILSDPIRV 196
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
106-269 1.05e-16

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: 78.10  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQVEpANKYPQ-----CLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERG 180
Cdd:cd17941   28 RDILGAAKTGSGKTLAFLVPLLEKLY-RERWTPedglgALIISPTRELAMQIFEVLRKVGK-YHSFSAGLIIGGKDVKEE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 181 Q-KISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKF 258
Cdd:cd17941  106 KeRINRmNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDL 184
                        170
                 ....*....|.
gi 380503835 259 AQKVVPDPNVI 269
Cdd:cd17941  185 ARLSLKNPEYI 195
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
106-266 1.34e-16

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: 78.57  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQtgkVIEQMGKFYPELKL-AYAVRGnkler 179
Cdd:cd17953   50 RDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIGLIMAPTRELALQ---IYVECKKFSKALGLrVVCVYG----- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKISEQ---------IVIGTPGTVLDW--CSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFS 248
Cdd:cd17953  122 GSGISEQiaelkrgaeIVVCTPGRMIDIltANNGRVTNLRRVTYVVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFS 200
                        170
                 ....*....|....*...
gi 380503835 249 ATFEDSVWKFAQKVVPDP 266
Cdd:cd17953  201 ATFPRKVEALARKVLHKP 218
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
107-251 2.18e-15

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: 75.46  E-value: 2.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQV------EPA----------NKYPQCLCLSPTYELALQtgkVIEQMGKFypelklAY 170
Cdd:cd18051   60 DLMACAQTGSGKTAAFLLPILSQIyeqgpgESLpsesgyygrrKQYPLALVLAPTRELASQ---IYDEARKF------AY 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 171 --AVRGNKLERGQKISEQI---------VIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI--QRM 237
Cdd:cd18051  131 rsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLVDMLERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDT 208
                        170
                 ....*....|....*.
gi 380503835 238 LPRNC--QMLLFSATF 251
Cdd:cd18051  209 MPPTGerQTLMFSATF 224
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
105-261 5.65e-15

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: 73.89  E-value: 5.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 105 PQNLIAQSQSGTGKTAAFVLAML---SQVEPANKY-----PQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGNK 176
Cdd:cd17945   27 NRDIIGIAETGSGKTAAFLIPLLvyiSRLPPLDEEtkddgPYALILAPTRELAQQIEEETQKFAKPLG-IRVVSIVGGHS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 177 LE-RGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLP-------------- 239
Cdd:cd17945  106 IEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DMGFEPQVTKILDAMPvsnkkpdteeaekl 183
                        170       180
                 ....*....|....*....|....*...
gi 380503835 240 ------RNCQMLLFSATFEDSVWKFAQK 261
Cdd:cd17945  184 aasgkhRYRQTMMFTATMPPAVEKIAKG 211
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
108-251 6.70e-15

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: 73.81  E-value: 6.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 108 LIAQSQSGTGKTAAFVLAM----LSQVE-----PANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLE 178
Cdd:cd17946   31 VIGAAETGSGKTLAFGIPIlerlLSQKSsngvgGKQKPLRALILTPTRELAVQVKDHLKAIAK-YTNIKIASIVGGLAVQ 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQKISEQ---IVIGTPGTVLDW----CSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNC-------QM 244
Cdd:cd17946  110 KQERLLKKrpeIVVATPGRLWELiqegNEHLANL--KSLRFLVLDEADRML-EKGHFAELEKILELLNKDRagkkrkrQT 186

                 ....*..
gi 380503835 245 LLFSATF 251
Cdd:cd17946  187 FVFSATL 193
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
107-266 8.74e-15

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: 72.62  E-value: 8.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEP--ANKYPQCLCLSPTYELALQTGKVIEQMGKFYPE-----LKLAYAVRGNKLER 179
Cdd:cd17957   29 DLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYRELLKLSKGTGLrivllSKSLEAKAKDGPKS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKISeqIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPRNC-QMLLFSATFEDSVWKF 258
Cdd:cd17957  109 ITKYD--ILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFREQTDEILAACTNPNlQRSLFSATIPSEVEEL 184

                 ....*...
gi 380503835 259 AQKVVPDP 266
Cdd:cd17957  185 ARSVMKDP 192
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
96-261 9.06e-15

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: 72.57  E-value: 9.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  96 VKSFEELRLPQNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfypelKLA 169
Cdd:cd17944   18 VKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR-----KLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 170 YAVRGNKLERGQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPR 240
Cdd:cd17944   93 VACFYGGTPYQQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSED 171
                        170       180
                 ....*....|....*....|.
gi 380503835 241 NCQMLLFSATFEDSVWKFAQK 261
Cdd:cd17944  172 NPQTLLFSATCPDWVYNVAKK 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
106-266 3.35e-14

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: 70.96  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY--PQCLCLSPTYELALQtgkVIEQMGKF-YPELKlAYAVRGNKlE 178
Cdd:cd17958   28 IDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRngPGVLVLTPTRELALQ---IEAECSKYsYKGLK-SVCVYGGG-N 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 179 RGQKISEQ-----IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFED 253
Cdd:cd17958  103 RNEQIEDLskgvdIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-DMGFEPQIRKILLDIRPDRQTIMTSATWPD 180
                        170
                 ....*....|...
gi 380503835 254 SVWKFAQKVVPDP 266
Cdd:cd17958  181 GVRRLAQSYLKDP 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
107-269 9.73e-14

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: 69.68  E-value: 9.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYPQC-------LCLSPTYELALQTGKVIEQMGKF-----YPELKLAYAVR 173
Cdd:cd17951   29 DMIGIAFTGSGKTLVFTLPLIMFaLEQEKKLPFIkgegpygLIVCPSRELARQTHEVIEYYCKAlqeggYPQLRCLLCIG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 174 GNKLERGQKISEQ---IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSAT 250
Cdd:cd17951  109 GMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADRMI-DMGFEEDIRTIFSYFKGQRQTLLFSAT 186
                        170
                 ....*....|....*....
gi 380503835 251 FEDSVWKFAQKVVPDPNVI 269
Cdd:cd17951  187 MPKKIQNFAKSALVKPVTV 205
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
107-250 1.41e-13

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: 69.31  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQK 182
Cdd:cd17942   29 DVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEK 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 183 ISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRMLPRNCQMLLFSAT 250
Cdd:cd17942  109 LGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEEEMRQIIKLLPKRRQTMLFSAT 177
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
107-250 1.58e-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: 67.81  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEPanKYPQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKI-- 183
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlg 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380503835 184 SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 250
Cdd:cd00046   79 DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
202-445 2.44e-13

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


Pssm-ID: 223588 [Multi-domain]  Cd Length: 590  Bit Score: 71.94  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 202 LKFIDPKKIKVFVLDEADVmIATQGHQ-----DQSIRIQRMLPrNCQMLLFSATFEdsvwkfaQKVVPD---------PN 267
Cdd:COG0514  124 LELLKRLPISLVAIDEAHC-ISQWGHDfrpdyRRLGRLRAGLP-NPPVLALTATAT-------PRVRDDireqlglqdAN 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 268 VIK--LKRE------EETLDTIKQYYVLcSSRDEKFQAlcnlyGAItiaqamIFCHTRKTASWLAAELSKEGHQVALLSG 339
Cdd:COG0514  195 IFRgsFDRPnlalkvVEKGEPSDQLAFL-ATVLPQLSK-----SGI------IYCLTRKKVEELAEWLRKNGISAGAYHA 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 340 EMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDS 419
Cdd:COG0514  263 GLSNEERERVQQAFLNDEIKVMVATNAFGMGIDKPDVRFVIHYDLP------GSIESYYQETGRAGRDGLPAEAILLYSP 336
                        250       260       270
                 ....*....|....*....|....*....|
gi 380503835 420 KHSMNILNRIQEHFN----KKIERLDTDDL 445
Cdd:COG0514  337 EDIRWQRYLIEQSKPdeeqKQIELAKLRQM 366
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
107-270 3.45e-13

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: 68.38  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQVEPA------NKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKlerg 180
Cdd:cd17949   30 DVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdrSDGTLALVLVPTRELALQIYEVLEKLLKPFHWIVPGYLIGGEK---- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 181 qKISEQ--------IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRML-------------P 239
Cdd:cd17949  106 -RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEKDITKILELLddkrskaggekskP 183
                        170       180       190
                 ....*....|....*....|....*....|.
gi 380503835 240 RNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 270
Cdd:cd17949  184 SRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
107-266 8.53e-13

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: 67.01  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQV------EPANKyPQCLCLSPTYELALQtgkVIEQMGKFYPELKL----AY--AVRG 174
Cdd:cd17966   29 DMVGIAQTGSGKTLAFLLPAIVHInaqpplERGDG-PIVLVLAPTRELAQQ---IQQEANKFGGSSRLrntcVYggAPKG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 175 NK---LERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQ------SIRIQRmlprncQML 245
Cdd:cd17966  105 PQirdLRRGV----EICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML-DMGFEPQirkivdQIRPDR------QTL 172
                        170       180
                 ....*....|....*....|.
gi 380503835 246 LFSATFEDSVWKFAQKVVPDP 266
Cdd:cd17966  173 MWSATWPKEVRRLAEDFLKDY 193
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
91-419 4.33e-12

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


Pssm-ID: 224126 [Multi-domain]  Cd Length: 851  Bit Score: 68.20  E-value: 4.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  91 SPLYS--VKSFEELRLPQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYpqcLCLSPTYELAL-QTGKVIEQMGKFYPE 165
Cdd:COG1205   69 ERLYShqVDALRLIREGRNVVVTTGTGSGKTESFLLPILDHLlrDPSARA---LLLYPTNALANdQAERLRELISDLPGK 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 166 LKLA-Y--AVRGNklERGQKISEQ--IVIGTPgTVLDW------------CSKLKFIdpkkikvfVLDEADVMIATQGhq 228
Cdd:COG1205  146 VTFGrYtgDTPPE--ERRAIIRNPpdILLTNP-DMLHYlllrnhdawlwlLRNLKYL--------VVDELHTYRGVQG-- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 229 dqSI------RIQRML---PRNCQMLLFSAT-------FEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRD 292
Cdd:COG1205  213 --SEvalllrRLLRRLrryGSPLQIICTSATlanpgefAEELFGRDFEVPVDEDGSPRGLRYFVRREPPIRELAESIRRS 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 293 -----EKFQALCNLYGAITIAqamiFCHTRK----TASWLAAELSKEGH--QVALLS--GEMMVEQRAAVIERFREGKEK 359
Cdd:COG1205  291 alaelATLAALLVRNGIQTLV----FFRSRKqvelLYLSPRRRLVREGGklLDAVSTyrAGLHREERRRIEAEFKEGELL 366
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380503835 360 VLVTTNVCARGIDVEQVSVVINfdlpvdkDGNPDNETYLH--RIGRTGRFGKRGLAVNMVDS 419
Cdd:COG1205  367 GVIATNALELGIDIGSLDAVIA-------YGYPGVSVLSFrqRAGRAGRRGQESLVLVVLRS 421
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
312-408 5.41e-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: 62.88  E-value: 5.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 312 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 389
Cdd:cd18793   32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107
                         90
                 ....*....|....*....
gi 380503835 390 GNPDNEtyLHRIGRTGRFG 408
Cdd:cd18793  108 WNPAVE--EQAIDRAHRIG 124
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
93-426 2.79e-11

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


Pssm-ID: 224125 [Multi-domain]  Cd Length: 766  Bit Score: 65.48  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  93 LYSVKSFEELRLPQ------------NLIAQSQSGTGKTAAFVLAMLSQVEPANKypQCLCLSPTYELALQTgkvIEQMG 160
Cdd:COG1204   23 ILKGDGIDELFNPQqeavekgllsdeNVLISAPTGSGKTLIALLAILSTLLEGGG--KVVYIVPLKALAEEK---YEEFS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 161 KFYpELKLAYAVR-GNKLERGQKISE-QIVIGTPgtvldwcSKL-----KFIDP-KKIKVFVLDEAdvmiatqgHQ-DQS 231
Cdd:COG1204   98 RLE-ELGIRVGIStGDYDLDDERLARyDVIVTTP-------EKLdsltrKRPSWiEEVDLVVIDEI--------HLlGDR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 232 IR-------IQRMLPRN--CQMLLFSAT---FED-----------SVWKFAQKVVPDPNVIKLKREEETLDTIKQyyvlc 288
Cdd:COG1204  162 TRgpvlesiVARMRRLNelIRIVGLSATlpnAEEvadwlnaklveSDWRPVPLRRGVPYVGAFLGADGKKKTWPL----- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 289 sSRDEKFQALCnlygAITIA---QAMIFCHTRKTASWLAAELSK------------EGHQVA------------------ 335
Cdd:COG1204  237 -LIDNLALELV----LESLAeggQVLVFVHSRKEAEKTAKKLRIkmsatlsddekiVLDEGAspilipetptsedeelae 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 336 LLSGEMMV-------EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN---FDLPVDKDGNPDNETYLHRIGRTG 405
Cdd:COG1204  312 LVLRGVAFhhaglprEDRQLVEDAFRKGKIKVLVSTPTLAAGVNLPARTVIIKdtrRYDPKGGIVDIPVLDVLQMAGRAG 391
                        410       420
                 ....*....|....*....|...
gi 380503835 406 R--FGKRGLAVNMVDSKHSMNIL 426
Cdd:COG1204  392 RpgYDDYGEAIILATSHDELEYL 414
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
106-265 5.84e-11

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: 62.72  E-value: 5.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 106 QNLIAQSQSGTGKTAAFVLAMLSQV--EP---ANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG------ 174
Cdd:cd18050  100 RDMVGIAQTGSGKTLAYLLPAIVHInhQPyleRGDGPICLVLAPTRELAQQVQQVADDYGK-SSRLKSTCIYGGapkgpq 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 175 -NKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFED 253
Cdd:cd18050  179 iRDLERGV----EICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPK 252
                        170
                 ....*....|..
gi 380503835 254 SVWKFAQKVVPD 265
Cdd:cd18050  253 EVRQLAEDFLRD 264
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
107-265 1.44e-10

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: 61.18  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 107 NLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQTGKVIEQMGK--------FYPELKLAYAVR 173
Cdd:cd18049   63 DMVGVAQTGSGKTLSYLLPAIVHInhQPFLERgdgPICLVLAPTRELAQQVQQVAAEYGRacrlkstcIYGGAPKGPQIR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 174 gnKLERGQkiseQIVIGTPGTVLDW--CSKLKFidpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATF 251
Cdd:cd18049  143 --DLERGV----EICIATPGRLIDFleAGKTNL---RRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATW 212
                        170
                 ....*....|....
gi 380503835 252 EDSVWKFAQKVVPD 265
Cdd:cd18049  213 PKEVRQLAEDFLKD 226
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
291-385 3.84e-10

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 57.99  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 291 RDEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 351
Cdd:cd18802    5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 380503835 352 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 385
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
312-409 9.68e-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: 56.45  E-value: 9.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 312 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 391
Cdd:cd18794   35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108
                         90
                 ....*....|....*...
gi 380503835 392 PDNETYLHRIGRTGRFGK 409
Cdd:cd18794  109 KSMESYYQESGRAGRDGL 126
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
308-406 5.73e-09

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


Pssm-ID: 224036 [Multi-domain]  Cd Length: 542  Bit Score: 58.12  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 308 AQAMIFCHTRKTASWLAAELSKEG-HQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 378
Cdd:COG1111  367 SRVIVFTEYRDTAEEIVNFLKKIGiKARVRFIGQasregdkgMSQKEQKEIIDQFRKGEYNVLVATSVGEEGLDIPEVDL 446
                         90       100
                 ....*....|....*....|....*...
gi 380503835 379 VINFDlPVdkdgnPDNETYLHRIGRTGR 406
Cdd:COG1111  447 VIFYE-PV-----PSEIRSIQRKGRTGR 468
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
95-269 1.32e-08

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 55.46  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  95 SVKSFEELRLPQNLIAqSQSGTGKTAAFVLAMLS---------------QVEPANKY--PQCLCLSPTYELALQTGKVIE 157
Cdd:cd17965   52 KQTSNEEPKLEVFLLA-AETGSGKTLAYLAPLLDylkrqeqepfeeaeeEYESAKDTgrPRSVILVPTHELVEQVYSVLK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 158 QMGKFYP----ELKLAYAVRGNKLERGQKISEQIVIGTPGTVLdwcsKLKFIDPK---KIKVFVLDEADVMIATQGHQDQ 230
Cdd:cd17965  131 KLSHTVKlgikTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLA----SLAKSRPKilsRVTHLVVDEADTLFDRSFLQDT 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 380503835 231 SIRIQRMLPRNCqMLLFSATFEDSVWKFAQKVVPDPNVI 269
Cdd:cd17965  207 TSIIKRAPKLKH-LILCSATIPKEFDKTLRKLFPDVVRI 244
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
310-406 5.24e-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: 51.59  E-value: 5.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 310 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 379
Cdd:cd18801   33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
                         90       100
                 ....*....|....*....|....*..
gi 380503835 380 INFdlpvdkDGNPDNETYLHRIGRTGR 406
Cdd:cd18801  113 ICY------DASPSPIRMIQRMGRTGR 133
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];
109-453 5.76e-08

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


Pssm-ID: 223989 [Multi-domain]  Cd Length: 442  Bit Score: 54.75  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 109 IAQSQSGTGKT--AAFVLAMLsqvepankYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAvrGNKLERGQKIseq 186
Cdd:COG1061   59 VIVLPTGAGKTvvAAEAIAEL--------KRSTLVLVPTKELLDQWAEALKKFLLLNDEIGIYGG--GEKELEPAKV--- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 187 iVIGTPGTVLdWCSKLKFIDPKKIKVFVLDEADVMIAtqghqDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKV--VP 264
Cdd:COG1061  126 -TVATVQTLA-RRQLLDEFLGNEFGLIIFDEVHHLPA-----PSYRRILELLSAAYPRLGLTATPEREDGGRIGDLfdLI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 265 DPNVIK-----------------------LKREEET--LDTIKQYYVLCSSRDEKFQALCNLYGAITI------------ 307
Cdd:COG1061  199 GPIVYEvslkelidegylapykyveikvtLTEDEEReyAKESARFRELLRARGTLRAENEARRIAIASerkiaavrglll 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 308 -----AQAMIFCHTRKTASWLAAELSKEGhQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINf 382
Cdd:COG1061  279 khargDKTLIFASDVEHAYEIAKLFLAPG-IVEAITGETPKEEREAILERFRTGGIKVLVTVKVLDEGVDIPDADVLII- 356
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380503835 383 dlpVDKDGNPDneTYLHRIGRTGRF--GKRGLAVNMVDSKHSMNILNRIQEHFNKKIERL----DTDDLDEIEKIAN 453
Cdd:COG1061  357 ---LRPTGSRR--LFIQRLGRGLRPaeGKEDTLALDYSLVPDDLGEEDIARRRRLFLIRKgytyRLLTADEEGELIP 428
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
94-218 7.42e-08

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: 52.65  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  94 YSVKSFEELrLPQNLIAQSQSGTGKT--AAFVL-AMLSQV-EPANKYPQCLCLSPTYELALQTGKVIEQ-----MGKFYP 164
Cdd:cd18034    6 YQLELFEAA-LKRNTIVVLPTGSGKTliAVMLIkEMGELNrKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlkVGEYSG 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 380503835 165 ELKLAYAVRGNKLERGQKIseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 218
Cdd:cd18034   85 EMGVDKWTKERWKEELEKY--DVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
115-250 1.35e-07

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: 52.25  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 115 GTGKTAAFVL----AMLSQVEPAnkyPQCLCLSPTYELALQTGKVIEQMGKFYPeLKLAyAVRGNK-----------LER 179
Cdd:cd17956   46 GSGKTLAYVLpivqALSKRVVPR---LRALIVVPTKELVQQVYKVFESLCKGTG-LKVV-SLSGQKsfkkeqklllvDTS 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 180 GQKISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEAD-------------VMIATQGHQDQ------SIRIQRMLP 239
Cdd:cd17956  121 GRYLSRvDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSV 200
                        170
                 ....*....|.
gi 380503835 240 RNCQMLLFSAT 250
Cdd:cd17956  201 RPLQKLLFSAT 211
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
108-264 2.61e-07

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: 51.21  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 108 LIAqSQSGTGKTAAFVLAMLSQV-----EPANKY--PQCLCLSPTYELALQTGKVIEQMGKFYPeLKlAYAVRGNKLERG 180
Cdd:cd17948   31 LCA-AETGSGKTLTYLLPIIQRLlryklLAEGPFnaPRGLVITPSRELAEQIGSVAQSLTEGLG-LK-VKVITGGRTKRQ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 181 QKISEQ----IVIGTPGTVldwcSKL---KFIDPKKIKVFVLDEADVMI-------------ATQGHQDQSIRIQRmLPR 240
Cdd:cd17948  108 IRNPHFeevdILVATPGAL----SKLltsRIYSLEQLRHLVLDEADTLLddsfneklshflrRFPLASRRSENTDG-LDP 182
                        170       180
                 ....*....|....*....|....
gi 380503835 241 NCQMLLFSATFEDSVWKFAQKVVP 264
Cdd:cd17948  183 GTQLVLVSATMPSGVGEVLSKVID 206
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
297-414 4.48e-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: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 297 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 369
Cdd:cd18797   29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 380503835 370 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 414
Cdd:cd18797  105 GIDIGGLDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
316-436 1.20e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.40  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 316 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 395
Cdd:cd18790   36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 380503835 396 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 436
Cdd:cd18790  114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
PRK13766 PRK13766
Hef nuclease; Provisional
257-406 1.59e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.64  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 257 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 325
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 326 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 397
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                 ....*....
gi 380503835 398 LHRIGRTGR 406
Cdd:PRK13766 458 IQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
359-411 2.47e-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: 45.00  E-value: 2.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 380503835 359 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 411
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
311-408 9.41e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 9.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 311 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 390
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                         90
                 ....*....|....*...
gi 380503835 391 npdnETYLHRIGRTGRFG 408
Cdd:PRK11057 318 ----ESYYQETGRAGRDG 331
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
323-450 1.54e-05

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: 45.37  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 323 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 397
Cdd:cd18798   43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380503835 398 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 450
Cdd:cd18798  110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
318-380 1.68e-05

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


Pssm-ID: 224121 [Multi-domain]  Cd Length: 677  Bit Score: 47.21  E-value: 1.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380503835 318 KTASWLAAELSK--EGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 380
Cdd:COG1200  492 QAAEELYEELKSflPELKVGLVHGRMKPAEKDAVMEAFKEGEIDILVATTVIEVGVDVPNATVMV 556
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
309-418 1.98e-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: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 309 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 388
Cdd:cd18795   45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 380503835 389 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 418
Cdd:cd18795  121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
334-424 2.03e-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: 44.57  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 334 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 412
Cdd:cd18792   63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136
                         90
                 ....*....|..
gi 380503835 413 AVNMVDSKHSMN 424
Cdd:cd18792  137 CYLLYPDPKKLT 148
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
318-380 3.05e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 3.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380503835 318 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 380
Cdd:PRK10917 490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
334-430 4.80e-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: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 334 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 412
Cdd:cd18811   64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137
                         90
                 ....*....|....*...
gi 380503835 413 AVNMVDSKHSMNILNRIQ 430
Cdd:cd18811  138 CLLVYKDPLTETAKQRLR 155
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
104-250 1.96e-04

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: 42.02  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 104 LPQNLIAQSQSGTGKTAAFVLAMLSQVEpANKypQCLCLSPTYELALQTGKVIEqmgKFYPELKLAYAVRGNKlergQKI 183
Cdd:cd17918   35 EPMDRLLSGDVGSGKTLVALGAALLAYK-NGK--QVAILVPTEILAHQHYEEAR---KFLPFINVELVTGGTK----AQI 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380503835 184 SEQI--VIGTpgtvldwcSKLKFIDPKKikvfvlDEADVMIATQGHQ---DQSIRIQRMlpRNCQMLLFSAT 250
Cdd:cd17918  105 LSGIslLVGT--------HALLHLDVKF------KNLDLVIVDEQHRfgvAQREALYNL--GATHFLEATAT 160
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
312-406 2.27e-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: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 312 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 385
Cdd:cd18796   43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119
                         90       100
                 ....*....|....*....|..
gi 380503835 386 vdkdGNPDNET-YLHRIGRTGR 406
Cdd:cd18796  120 ----GSPKSVArLLQRLGRSGH 137
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
311-414 4.32e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835  311 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 390
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                          90       100
                  ....*....|....*....|....
gi 380503835  391 npdnetYLHRIGRTGRFGKRGLAV 414
Cdd:PLN03137  764 ------YHQECGRAGRDGQRSSCV 781
comFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) ...
311-428 8.07e-04

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


Pssm-ID: 226583 [Multi-domain]  Cd Length: 441  Bit Score: 41.68  E-value: 8.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 311 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInfdlpVDKDG 390
Cdd:COG4098  309 LIFFPEIETMEQVAAALKKKLPKETIASVHSEDQHRKEKVEAFRDGKITLLITTTILERGVTFPNVDVFV-----LGAEH 383
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 380503835 391 NPDNETYLHRI-GRTGR----------FGKRGLAVNMVDSKHSMNILNR 428
Cdd:COG4098  384 RVFTESALVQIaGRVGRslerptgdvlFFHYGKSKAMKQARKEIKEMNK 432
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
334-424 9.79e-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: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 334 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 412
Cdd:cd18810   54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127
                         90
                 ....*....|..
gi 380503835 413 AVNMVDSKHSMN 424
Cdd:cd18810  128 AYFLYPDQKKLT 139
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
212-410 1.64e-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: 40.49  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 212 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpnviklkREEETLDTI---KQYYVL 287
Cdd:cd09639  126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503835 288 CSSRD-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 359
Cdd:cd09639  197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 380503835 360 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 410
Cdd:cd09639  277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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