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Conserved domains on  [gi|1001624453|ref|NP_001307454|]
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ATP-dependent RNA helicase DDX19A isoform 3 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209184)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
 9-212 2.94e-130

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


The actual alignment was detected with superfamily member cd18048:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 229  Bit Score: 373.20  E-value: 2.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd18048    26 KEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168
Cdd:cd18048   106 KVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVR 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 212
Cdd:cd18048   186 VKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 216-352 3.04e-52

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 3.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 216 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 295
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624453 296 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 352
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 9-212 2.94e-130

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: 373.20  E-value: 2.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd18048    26 KEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168
Cdd:cd18048   106 KVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVR 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 212
Cdd:cd18048   186 VKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
9-385 7.68e-120

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 353.68  E-value: 7.68e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPS-DRYPQCLCLSPTYELALQT 87
Cdd:COG0513    10 SPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTRELALQV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQ 160
Cdd:COG0513    88 AEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD-M 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAI 240
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 241 TIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 320
Cdd:COG0513   240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624453 321 VDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 385
Cdd:COG0513   320 EDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 12-378 2.68e-95

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 290.57  E-value: 2.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVI 91
Cdd:PTZ00424   39 LLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  92 EQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQD 164
Cdd:PTZ00424  117 LALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 165 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQ 244
Cdd:PTZ00424  190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQ 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 245 AMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKd 324
Cdd:PTZ00424  270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP- 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624453 325 gnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 378
Cdd:PTZ00424  349 -----ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 216-352 3.04e-52

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 3.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 216 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 295
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624453 296 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 352
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 25-190 2.88e-39

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: 137.76  E-value: 2.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  25 SKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 104
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 105 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 182
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 1001624453 183 SATFEDSV 190
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
16-219 1.58e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.85  E-value: 1.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   16 VYAMGFNRPSKIQENALPMMLAEPpQNLIAQSQSGTGKTAAFVLAMLSRVEPSDrYPQCLCLSPTYELALQTGKVIEQMG 95
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   96 KFYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 172
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1001624453  173 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 219
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 228-343 5.83e-32

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.54  E-value: 5.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 228 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 305
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1001624453 306 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 343
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
257-343 8.32e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.90  E-value: 8.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  257 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 336
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 1001624453  337 GRTGRFG 343
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
192-344 1.19e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 69.37  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 192 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 265
Cdd:COG1111   309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 266 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 337
Cdd:COG1111   377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450


                  ....*..
gi 1001624453 338 RTGRFGK 344
Cdd:COG1111   451 RTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
 192-341 8.49e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 192 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 260
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 261 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 332
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                  ....*....
gi 1001624453 333 LHRIGRTGR 341
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 ...
 9-212 2.94e-130

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: 373.20  E-value: 2.94e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd18048    26 KEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168
Cdd:cd18048   106 KVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVR 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 212
Cdd:cd18048   186 VKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 9-205 1.76e-129

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: 370.20  E-value: 1.76e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd18047     9 KPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168
Cdd:cd18047    89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd18047   169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 9-205 1.70e-127

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: 364.59  E-value: 1.70e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd17963     2 KPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFyPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQSIR 168
Cdd:cd17963    82 EVVEKMGKF-TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSIR 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd17963   160 IKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
9-385 7.68e-120

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 353.68  E-value: 7.68e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPS-DRYPQCLCLSPTYELALQT 87
Cdd:COG0513    10 SPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTRELALQV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQ 160
Cdd:COG0513    88 AEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD-M 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAI 240
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 241 TIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 320
Cdd:COG0513   240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1001624453 321 VDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 385
Cdd:COG0513   320 EDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 12-378 2.68e-95

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 290.57  E-value: 2.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVI 91
Cdd:PTZ00424   39 LLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  92 EQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQD 164
Cdd:PTZ00424  117 LALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 165 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQ 244
Cdd:PTZ00424  190 QIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQ 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 245 AMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKd 324
Cdd:PTZ00424  270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP- 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624453 325 gnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 378
Cdd:PTZ00424  349 -----ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 9-381 9.02e-72

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 231.61  E-value: 9.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:PRK11776   12 PPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQG 161
Cdd:PRK11776   90 KEIRRLARFIPNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLDEADRML-DMG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 162 HQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKrEEETLDTIKQYYVLCSsRDEKFQALCNLYGAIT 241
Cdd:PRK11776  164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVS-PDERLPALQRLLLHHQ 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 242 IAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDL 319
Cdd:PRK11776  242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001624453 320 PvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLD 381
Cdd:PRK11776  320 A------RDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLGRKLNWEPLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 10-380 4.31e-69

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 224.05  E-value: 4.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLS------RVEPSDryPQCLCLSPTYEL 83
Cdd:PRK11192   10 ESLLEALQDKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQhlldfpRRKSGP--PRILILTPTREL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  84 ALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEAD 154
Cdd:PRK11192   86 AMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DCRAVETLILDEAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 155 VMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNVIKL---KREEETldtIKQYYVLCSSRDE 228
Cdd:PRK11192  158 RMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---IHQWYYRADDLEH 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 229 KFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 308
Cdd:PRK11192  232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001624453 309 EQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRIQEHFNKKIERLDTDDL 380
Cdd:PRK11192  312 DDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKIERYIEEPLKARVIDEL 376
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 10-373 3.17e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 202.06  E-value: 3.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVE----PSDRY---PQCLCLSPTYE 82
Cdd:PRK01297   96 PELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLqtppPKERYmgePRALIIAPTRE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  83 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIa 158
Cdd:PRK01297  174 LVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLDEADRML- 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 159 TQGHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNL 236
Cdd:PRK01297  251 DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLLYNL 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 237 YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 316
Cdd:PRK01297  330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624453 317 FDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKIE 373
Cdd:PRK01297  410 FTLPED----PDD--YVHRIGRTGRAGASGVSISFAGEDDAFQ-LPEIEELLGRKIS 459
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 12-355 1.52e-57

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 198.15  E-value: 1.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVI 91
Cdd:PRK11634   17 ILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAM 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  92 EQMGKFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIR 168
Cdd:PRK11634   95 TDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML-RMGFIEDVET 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ-YYVLCSSRdeKFQALCNLYGAITIAQAMI 247
Cdd:PRK11634  173 IMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFLEAEDFDAAII 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 248 FCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVdkdgnp 327
Cdd:PRK11634  251 FVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM------ 324

                         330       340
                  ....*....|....*....|....*...
gi 1001624453 328 DNETYLHRIGRTGRFGKRGLAVNMVDSK 355
Cdd:PRK11634  325 DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 10-372 2.36e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 194.01  E-value: 2.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLaePPQNLIAQSQSGTGKTAAFVLA----MLSRVEPSDRYPQ---CLCLSPTYE 82
Cdd:PRK04537   18 PALLAGLESAGFTRCTPIQALTLPVAL--PGGDVAGQAQTGTGKTLAFLVAvmnrLLSRPALADRKPEdprALILAPTRE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  83 LALQTGKvieQMGKFYPELKLAYAV--RGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMI 157
Cdd:PRK04537   96 LAIQIHK---DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMF 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 158 ATQGHQDqsIR-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNviKLKREEETLDTIK-QYYVLCSSRDEKFQAL 233
Cdd:PRK04537  173 DLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARvRQRIYFPADEEKQTLL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 234 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 313
Cdd:PRK04537  249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624453 314 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 372
Cdd:PRK04537  329 VYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAMS-LPDIEAYIEQKI 380
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 10-372 2.48e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 187.49  E-value: 2.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLA----MLSRVEPSDRY---PQCLCLSPTYE 82
Cdd:PRK04837   17 PQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPRALIMAPTRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  83 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIAT 159
Cdd:PRK04837   95 LAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVLDEADRMFDL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 160 QGHQDqsIR--IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ--YYvlcSSRDEKFQALC 234
Cdd:PRK04837  173 GFIKD--IRwlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PSNEEKMRLLQ 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 235 NLYGAITIAQAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQ 310
Cdd:PRK04837  248 TLIEEEWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPA 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1001624453 311 VSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 372
Cdd:PRK04837  324 VTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSI 378
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 12-205 1.29e-52

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: 173.40  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSD----RYPQCLCLSPTYELALQT 87
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGKfYPELKlAYAVRGnklerGQKISEQ---------IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIa 158
Cdd:cd00268    79 AEVARKLGK-GTGLK-VAAIYG-----GAPIKKQiealkkgpdIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1001624453 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd00268   150 DMGFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 216-352 3.04e-52

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 3.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 216 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 295
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624453 296 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 352
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 1-352 1.73e-50

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 175.77  E-value: 1.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   1 MSGTFLIRKPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-----EPSDRYP-QC 74
Cdd:PRK10590    1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLitrqpHAKGRRPvRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  75 LCLSPTYELALQTGKVIEQMGKFYPELKLAyaVRGnklerGQKISEQ---------IVIGTPGTVLDwCSKLKFIDPKKI 145
Cdd:PRK10590   79 LILTPTRELAAQIGENVRDYSKYLNIRSLV--VFG-----GVSINPQmmklrggvdVLVATPGRLLD-LEHQNAVKLDQV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 146 KVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYyVLCSS 225
Cdd:PRK10590  151 EILVLDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVD 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 226 RDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 305
Cdd:PRK10590  229 KKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARG 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1001624453 306 IDVEQVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAVNMV 352
Cdd:PRK10590  309 LDIEELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSLV 349
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 9-204 5.76e-48

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: 161.72  E-value: 5.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENA-LPMMLAEppqNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQT 87
Cdd:cd17939     5 SEDLLRGIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGkFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQD 164
Cdd:cd17939    82 QKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SRGFKD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1001624453 165 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd17939   159 QIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 9-201 4.49e-45

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: 154.14  E-value: 4.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENA-LPMMLAeppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQT 87
Cdd:cd18046     7 KESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGkFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQ 160
Cdd:cd18046    84 QKVVMALG-DYMGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEML-SR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1001624453 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd18046   157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 9-204 4.68e-44

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: 151.68  E-value: 4.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd17940     7 KRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKfYPELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQ 165
Cdd:cd17940    85 QVCKELGK-HMGVKVMVTTGGTSLrDDIMRLYQtvHVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADKLL-SQDFQPI 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1001624453 166 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd17940   162 IEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PTZ00110 PTZ00110
helicase; Provisional
 12-348 1.52e-41

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 153.39  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVL-AMLS-RVEPSDRY---PQCLCLSPTYELALQ 86
Cdd:PTZ00110  141 ILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLpAIVHiNAQPLLRYgdgPIVLVLAPTRELAEQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  87 tgkVIEQMGKFYPELKLAYAVR-GNKLERGQKIS----EQIVIGTPGTVLDW----CSKLKfidpkKIKVFVLDEADVMI 157
Cdd:PTZ00110  219 ---IREQCNKFGASSKIRNTVAyGGVPKRGQIYAlrrgVEILIACPGRLIDFlesnVTNLR-----RVTYLVLDEADRML 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP----NV--IKLKreeeTLDTIKQYYVLCSSRdEKFQ 231
Cdd:PTZ00110  291 -DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpvhvNVgsLDLT----ACHNIKQEVFVVEEH-EKRG 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 232 ALCNLYGAITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 309
Cdd:PTZ00110  365 KLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVK 444

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1001624453 310 QVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 348
Cdd:PTZ00110  445 DVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGAS 477
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 10-353 1.83e-41

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 152.63  E-value: 1.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-------EPSDRYPQCLCLSPTYE 82
Cdd:PLN00206  130 PKLLLNLETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMVLTPTRE 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  83 LALQTGKVIEQMGKFYPeLKLAYAVRGN----KLERGQKISEQIViGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIa 158
Cdd:PLN00206  208 LCVQVEDQAKVLGKGLP-FKTALVVGGDampqQLYRIQQGVELIV-GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML- 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 159 TQGHQDQSIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQalcnLYG 238
Cdd:PLN00206  284 ERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----LFD 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 239 AITIAQ-----AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 312
Cdd:PLN00206  359 ILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1001624453 313 VVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 353
Cdd:PLN00206  439 QVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 9-204 9.87e-40

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 140.30  E-value: 9.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   9 KPQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTG 88
Cdd:cd18045     7 REDLLRGIYAYGFEKPSAIQQRAIKPIIKG--RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYpELKLAYAVRGN-------KLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQG 161
Cdd:cd18045    85 KVLLALGDYM-NVQCHACIGGTsvgddirKLDYGQ----HIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEML-NKG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1001624453 162 HQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd18045   158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 25-190 2.88e-39

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: 137.76  E-value: 2.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  25 SKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 104
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 105 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 182
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 1001624453 183 SATFEDSV 190
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 12-205 2.68e-37

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: 133.54  E-value: 2.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVI 91
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  92 EQMGKFYPELKLAYAVRG--NKLERGQKISEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIR 168
Cdd:cd17943    79 KKIGKKLEGLKCEVFIGGtpVKEDKKKLKGCHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNW 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1001624453 169 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd17943   156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEXDc smart00487
DEAD-like helicases superfamily;
16-219 1.58e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.85  E-value: 1.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   16 VYAMGFNRPSKIQENALPMMLAEPpQNLIAQSQSGTGKTAAFVLAMLSRVEPSDrYPQCLCLSPTYELALQTGKVIEQMG 95
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   96 KFYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 172
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1001624453  173 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 219
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 10-205 2.06e-35

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 128.96  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAepPQNLIAQSQSGTGKTAAFVLAMLSRVEpsDRYPQ----CLCLSPTYELAL 85
Cdd:cd17959    10 PPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEKLK--AHSPTvgarALILSPTRELAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  86 QTGKVIEQMGKFyPELKLAYAVRGNKLERG-QKISEQ--IVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMIAtQGH 162
Cdd:cd17959    86 QTLKVTKELGKF-TDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRLFE-MGF 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1001624453 163 QDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd17959   163 AEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 10-206 2.58e-34

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 126.16  E-value: 2.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV------EPSDRYPQCLCLSPTYEL 83
Cdd:cd17961     3 PRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  84 ALQTGKVIEQMGKFY-PELKLAyAVRGNKLERGQK--ISEQ--IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIa 158
Cdd:cd17961    81 AQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRalLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVL- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1001624453 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKL 206
Cdd:cd17961   159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 12-194 4.02e-33

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: 122.36  E-value: 4.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDR---YPQCLCLSPTYELALQTG 88
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLLYRPKkkaATRVLVLVPTRELAMQCF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPeLKLAYAVRGNKL---ERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQ 165
Cdd:cd17947    79 SVLQQLAQFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADE 156

                         170       180
                  ....*....|....*....|....*....
gi 1001624453 166 SIRIQRMLPRNCQMLLFSATFEDSVWKFA 194
Cdd:cd17947   157 LKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 5-201 5.67e-33

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: 122.45  E-value: 5.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453   5 FLIrKPQLLQGVYAMGFNRPSKIQENALPM-MLAEppqNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYEL 83
Cdd:cd17950     7 FLL-KPELLRAIVDCGFEHPSEVQHECIPQaILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  84 ALQTGKVIEQMGKFYPELKLAY-----AVRGNKlERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIA 158
Cdd:cd17950    83 AFQISNEYERFSKYMPNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKMLE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1001624453 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17950   161 QLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 228-343 5.83e-32

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.54  E-value: 5.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 228 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 305
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1001624453 306 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 343
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 10-201 4.01e-30

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: 114.72  E-value: 4.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGK 89
Cdd:cd17954     9 EELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELAQQISE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  90 VIEQMGKFyPELKLAYAVRG-----NKLERGQKisEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIatqgHQD 164
Cdd:cd17954    87 QFEALGSS-IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLL----NMD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1001624453 165 QSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17954   160 FEPEIDKILkviPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 12-201 2.21e-29

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: 112.64  E-value: 2.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVI 91
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  92 EQMGKFYPELKLAYAVRGN----KLERGQKiSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 167
Cdd:cd17962    79 KELMKGLPPMKTALLVGGLplppQLYRLQQ-GVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVL 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1001624453 168 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17962   156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 10-204 2.70e-29

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


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 112.68  E-value: 2.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLaEPPQNLIAQSQSGTGKTAAFVL----AMLSRVEPSDRYP-QCLCLSPTYELA 84
Cdd:cd17964     3 PSLLKALTRMGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  85 LQTGKVIEQMGKFYPELKLAYAVRGNK----LERGQKISEQIVIGTPG---TVLDWCSKLKFIdpKKIKVFVLDEADVMI 157
Cdd:cd17964    82 LQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGrliDHLENPGVAKAF--TDLDYLVLDEADRLL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1001624453 158 aTQGHQDQSIRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNVI 204
Cdd:cd17964   160 -DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 10-201 7.38e-29

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: 111.26  E-value: 7.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAepPQNLIAQSQSGTGKTAAFVLAMLSRVepsdrypQCLCLSPTYELALQTGK 89
Cdd:cd17938     8 PELIKAVEELDWLLPTDIQAEAIPLILG--GGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  90 VIEQMGKFY--PELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQD 164
Cdd:cd17938    79 CIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL-SQGNLE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1001624453 165 QSIRIQRMLP------RNCQMLLFSATFE-DSVWKFAQKVVPDP 201
Cdd:cd17938   157 TINRIYNRIPkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 12-201 3.68e-27

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: 106.92  E-value: 3.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSR--VEPSDRYpqCLCLSPTYELALQtgk 89
Cdd:cd17955    10 LVKQCASLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRlsEDPYGIF--ALVLTPTRELAYQ--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  90 VIEQM---GKFyPELKLAYAVRG-NKLERGQKISEQ--IVIGTPGTVLDW---CSKLKFiDPKKIKVFVLDEADVMIaTQ 160
Cdd:cd17955    83 IAEQFralGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLDEADRLL-TG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1001624453 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17955   160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
HELICc smart00490
helicase superfamily c-terminal domain;
257-343 8.32e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.90  E-value: 8.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  257 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 336
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 1001624453  337 GRTGRFG 343
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 12-190 1.42e-25

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 102.27  E-value: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-----EPSDRYPQCLCLSPTYELALQ 86
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  87 TGKVIEQMGKFY-PELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLD-WCSKLKFIDPKKIKVFVLDEADVMIATq 160
Cdd:cd17960    79 IYEVLQSFLEHHlPKLKCQLLIGGTNVEEDVKKfkrnGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL- 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1001624453 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSV 190
Cdd:cd17960   158 GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 10-195 3.13e-25

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: 102.18  E-value: 3.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-----EPSDR-----YPQCLCLSP 79
Cdd:cd17967     9 ELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLledgpPSVGRgrrkaYPSALILAP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  80 TYELALQTgkvieqmgkfYPE-LKLAY-------AVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKLKfIDPKKIKV 147
Cdd:cd17967    87 TRELAIQI----------YEEaRKFSYrsgvrsvVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR-ISLSSIKF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1001624453 148 FVLDEADVMIaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 195
Cdd:cd17967   156 LVLDEADRML-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 10-196 4.04e-23

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: 97.35  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  10 PQLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSR-----VEPSD----RYPQCLCLSPT 80
Cdd:cd18052    52 ETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGmmkegLTASSfsevQEPQALIVAPT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  81 YELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFV 149
Cdd:cd18052   130 RELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVATPGRLLDFIGRGK-ISLSKLKYLI 199

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624453 150 LDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 196
Cdd:cd18052   200 LDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 13-204 1.70e-22

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 93.89  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  13 LQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-----EPSDRYpQCLCLSPTYELALQT 87
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLyrerwTPEDGL-GALIISPTRELAMQI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  88 GKVIEQMGKfYPELKLAYAVRGNKLERGQ-KISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQ 165
Cdd:cd17941    79 FEVLRKVGK-YHSFSAGLIIGGKDVKEEKeRINRmNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKET 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1001624453 166 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd17941   157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 12-204 5.64e-22

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: 92.48  E-value: 5.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV------EPSDRyPQCLCLSPTYELAL 85
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHImdqrelEKGEG-PIAVIVAPTRELAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  86 QTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQ 163
Cdd:cd17952    78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1001624453 164 DQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd17952   156 YQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 12-196 9.87e-22

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: 92.38  E-value: 9.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAepPQNLIAQSQSGTGKTAAFVLAMLSRV--------EPSDRYPQCLCLSPTYEL 83
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLVYIsrlppldeETKDDGPYALILAPTREL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  84 ALQTGKVIEQMGKFYPeLKLAYAVRGNKLE-RGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQ 160
Cdd:cd17945    79 AQQIEEETQKFAKPLG-IRVVSIVGGHSIEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DM 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624453 161 GHQDQSIRIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQK 196
Cdd:cd17945   156 GFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKG 211
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 12-186 7.31e-21

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: 90.38  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEPpQNLIAQSQSGTGKTAAFVLAMLSR---------VEPSDRYPQCLCLSPTYE 82
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPILERllsqkssngVGGKQKPLRALILTPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  83 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDW----CSKLKFIdpKKIKVFVLDEADV 155
Cdd:cd17946    80 LAVQVKDHLKAIAK-YTNIKIASIVGGLAVQKQERLLKKrpeIVVATPGRLWELiqegNEHLANL--KSLRFLVLDEADR 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1001624453 156 MIaTQGHQDQSIRIQRMLPRNC-------QMLLFSATF 186
Cdd:cd17946   157 ML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 12-201 8.97e-21

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: 89.19  E-value: 8.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEPpqNLIAQSQSGTGKTAAFVLAMLSRVEP--SDRYPQCLCLSPTYELALQTGK 89
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  90 VIEQMGKFYPE-----LKLAYAVRGNKLERGQKISeqIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATqGHQD 164
Cdd:cd17957    79 ELLKLSKGTGLrivllSKSLEAKAKDGPKSITKYD--ILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFRE 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1001624453 165 QSIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17957   155 QTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 11-201 1.48e-20

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 89.36  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  11 QLLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV------EPSDRyPQCLCLSPTYELA 84
Cdd:cd17953    22 KVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIkdqrpvKPGEG-PIGLIMAPTRELA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  85 LQtgkVIEQMGKFYPELKL-AYAVRGnklerGQKISEQI---------VIGTPGTVLDW--CSKLKFIDPKKIKVFVLDE 152
Cdd:cd17953    99 LQ---IYVECKKFSKALGLrVVCVYG-----GSGISEQIaelkrgaeiVVCTPGRMIDIltANNGRVTNLRRVTYVVLDE 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1001624453 153 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17953   171 ADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 19-205 1.58e-20

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 88.80  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  19 MGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRY------PQCLCLSPTYELALQTGKVIE 92
Cdd:cd17949     9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsdgTLALVLVPTRELALQIYEVLE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  93 QMGKFYPELKLAYAVRGNKlergqKISEQ--------IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQD 164
Cdd:cd17949    87 KLLKPFHWIVPGYLIGGEK-----RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624453 165 QSIRIQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
Cdd:cd17949   161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 12-201 2.06e-19

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: 85.50  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAML------SRVEPSDRyPQCLCLSPTYELAL 85
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERGDG-PIVLVLAPTRELAQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  86 QtgkVIEQMGKFYPELKL-AYAVRGNkLERGQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaT 159
Cdd:cd17966    78 Q---IQQEANKFGGSSRLrNTCVYGG-APKGPQIRDlrrgvEICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML-D 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1001624453 160 QGHQDQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17966   152 MGFEPQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 12-201 2.73e-19

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


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 85.21  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRVE--PSDRY----PQCLCLSPTYELAL 85
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREqrngPGVLVLTPTRELAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  86 QtgkVIEQMGKF-YPELKlAYAVRGNKlERGQKISEQ-----IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaT 159
Cdd:cd17958    79 Q---IEAECSKYsYKGLK-SVCVYGGG-NRNEQIEDLskgvdIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-D 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1001624453 160 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
Cdd:cd17958   152 MGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 21-186 9.37e-19

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: 84.71  E-value: 9.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  21 FNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV--------EPSD--------RYPQCLCLSPTYELA 84
Cdd:cd18051    41 YTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIyeqgpgesLPSEsgyygrrkQYPLALVLAPTRELA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  85 LQtgkVIEQMGKFypelklAY--AVRGNKLERGQKISEQI---------VIGTPGTVLDWCSKLKfIDPKKIKVFVLDEA 153
Cdd:cd18051   119 SQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLVDMLERGK-IGLDYCKYLVLDEA 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1001624453 154 DVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 186
Cdd:cd18051   189 DRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 12-204 7.49e-18

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: 81.23  E-value: 7.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAM-LSRVEPSDRYPQC-------LCLSPTYEL 83
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIkgegpygLIVCPSREL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  84 ALQTGKVIEQMGKF-----YPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADV 155
Cdd:cd17951    79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1001624453 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
Cdd:cd17951   158 MI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 13-185 1.04e-17

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: 80.48  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  13 LQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFV---LAMLSRVEPSDRY-PQCLCLSPTYELALQTG 88
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLipaIELLYKLKFKPRNgTGVIIISPTRELALQIY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  89 KVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQS 166
Cdd:cd17942    80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEEEM 158

                         170
                  ....*....|....*....
gi 1001624453 167 IRIQRMLPRNCQMLLFSAT 185
Cdd:cd17942   159 RQIIKLLPKRRQTMLFSAT 177
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 41-196 2.91e-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: 73.73  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  41 QNLIAQSQSGTGKTAAFVLAMLSRVEPSD------RYPQCLCLSPTYELALQTGKVIEQMGKfypelKLAYAVRGNKLER 114
Cdd:cd17944    28 KDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 115 GQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSAT 185
Cdd:cd17944   103 QQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSAT 181

                         170
                  ....*....|.
gi 1001624453 186 FEDSVWKFAQK 196
Cdd:cd17944   182 CPDWVYNVAKK 192
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
50-386 3.18e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.91  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  50 GTGKT--AAFVLAMLSRVEPsdrypqCLCLSPTYELALQTGKVIEQMgkfypeLKLAYAVRGNKlergqKISEQIVIGTP 127
Cdd:COG1061   110 GTGKTvlALALAAELLRGKR------VLVLVPRRELLEQWAEELRRF------LGDPLAGGGKK-----DSDAPITVATY 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 128 GTVldwcSKLKFID--PKKIKVFVLDEAdvmiatqgHQDQSIRIQRMLPR--NCQMLLFSAT--FEDSVWKF-------- 193
Cdd:COG1061   173 QSL----ARRAHLDelGDRFGLVIIDEA--------HHAGAPSYRRILEAfpAAYRLGLTATpfRSDGREILlflfdgiv 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 194 ---------AQKVVPDPNVI----KLKREEETLDTIKQ--YYVLCSSRDEKFQALCNLYGAIT-IAQAMIFCHTRKTASW 257
Cdd:COG1061   241 yeyslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 258 LAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdGNPDneTYLHRIG 337
Cdd:COG1061   321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT---GSPR--EFIQRLG 394

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1001624453 338 R---TGRFGKRGLAVNMVDSKHSM--NILNRIQEHFNKKIERLDTDDLDEIEKI 386
Cdd:COG1061   395 RglrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 42-185 5.32e-14

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 68.58  E-value: 5.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  42 NLIAQSQSGTGKTAAFVLAMLSRVEPsdRYPQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKI-- 118
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlg 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624453 119 SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 185
Cdd:cd00046    79 DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 21-200 6.85e-14

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: 71.20  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  21 FNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV------EPSDRyPQCLCLSPTYELALQTGKVIEQM 94
Cdd:cd18050    82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHInhqpylERGDG-PICLVLAPTRELAQQVQQVADDY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  95 GKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSI 167
Cdd:cd18050   159 GK-SSRLKSTCIYGGapkgpqiRDLERGV----EICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIR 231

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1001624453 168 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
Cdd:cd18050   232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 12-200 6.55e-13

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 67.73  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV------EPSDRyPQCLCLSPTYELAL 85
Cdd:cd18049    35 VMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHInhqpflERGDG-PICLVLAPTRELAQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  86 QTGKVIEQMGK--------FYPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDW--CSKLKFidpKKIKVFVLDEADV 155
Cdd:cd18049   112 QVQQVAAEYGRacrlkstcIYGGAPKGPQIR--DLERGV----EICIATPGRLIDFleAGKTNL---RRCTYLVLDEADR 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1001624453 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
Cdd:cd18049   183 ML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
192-344 1.19e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 69.37  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 192 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 265
Cdd:COG1111   309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 266 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 337
Cdd:COG1111   377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450


                  ....*..
gi 1001624453 338 RTGRFGK 344
Cdd:COG1111   451 RTGRKRE 457
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 12-185 3.07e-12

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: 65.73  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAE-------PPQNLIAQSQSGTGKTAAFVL----AMLSRVEPSDRypqCLCLSPT 80
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVPRLR---ALIVVPT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  81 YELALQTGKVIEQMGKFYPeLKLAyAVRGNK-----------LERGQKISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVF 148
Cdd:cd17956    78 KELVQQVYKVFESLCKGTG-LKVV-SLSGQKsfkkeqklllvDTSGRYLSRvDILVATPGRLVDHLNSTPGFTLKHLRFL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624453 149 VLDEAD-------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 185
Cdd:cd17956   156 VIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 247-343 3.75e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 63.26  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 247 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 324
Cdd:cd18793    32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107

                          90
                  ....*....|....*....
gi 1001624453 325 GNPDNEtyLHRIGRTGRFG 343
Cdd:cd18793   108 WNPAVE--EQAIDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 247-343 4.36e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.48  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 247 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 324
Cdd:COG0553   554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630

                          90
                  ....*....|....*....
gi 1001624453 325 gNPDNEtyLHRIGRTGRFG 343
Cdd:COG0553   631 -NPAVE--EQAIDRAHRIG 646
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 12-199 9.05e-11

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: 61.23  E-value: 9.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  12 LLQGVYAMGFNRPSKIQENALPMMLAEppQNLIAQSQSGTGKTAAFVLAMLSRV-------EPSDRYPQCLCLSPTYELA 84
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  85 LQTGKVIEQMGKFYPeLKlAYAVRGNKLERGQKISEQ----IVIGTPGTVldwcSKL---KFIDPKKIKVFVLDEADVMI 157
Cdd:cd17948    79 EQIGSVAQSLTEGLG-LK-VKVITGGRTKRQIRNPHFeevdILVATPGAL----SKLltsRIYSLEQLRHLVLDEADTLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1001624453 158 -------------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 199
Cdd:cd17948   153 ddsfneklshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 226-320 3.38e-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: 57.60  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 226 RDEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 286
Cdd:cd18802     5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1001624453 287 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 320
Cdd:cd18802    85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 247-344 1.16e-09

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: 56.06  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 247 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 326
Cdd:cd18794    35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108

                          90
                  ....*....|....*...
gi 1001624453 327 PDNETYLHRIGRTGRFGK 344
Cdd:cd18794   109 KSMESYYQESGRAGRDGL 126
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
247-349 2.12e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 247 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 324
Cdd:COG0514   235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308

                          90       100
                  ....*....|....*....|....*
gi 1001624453 325 GNPdnETYLHRIGRTGRFGKRGLAV 349
Cdd:COG0514   309 KSI--EAYYQEIGRAGRDGLPAEAL 331
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 245-341 6.44e-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: 51.20  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 245 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 314
Cdd:cd18801    33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112

                          90       100
                  ....*....|....*....|....*..
gi 1001624453 315 INFdlpvdkDGNPDNETYLHRIGRTGR 341
Cdd:cd18801   113 ICY------DASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 243-349 1.43e-07

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 53.30  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 243 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 316
Cdd:COG1205   289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1001624453 317 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 349
Cdd:COG1205   369 -------AGYPGTRAsFWQQAGRAGRRGQDSLVV 395
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 232-349 3.85e-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: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 232 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 304
Cdd:cd18797    29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1001624453 305 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 349
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) ...
 251-371 7.41e-07

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: 48.78  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 251 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 330
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1001624453 331 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 371
Cdd:cd18790   114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
PRK13766 PRK13766
Hef nuclease; Provisional
 192-341 8.49e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 192 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 260
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 261 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 332
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457


                  ....*....
gi 1001624453 333 LHRIGRTGR 341
Cdd:PRK13766  458 IQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 294-346 2.36e-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: 2.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1001624453 294 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 346
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 23-185 3.01e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 47.03  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  23 RPSKIQENALPM----MLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVepsDRYPQCLCLSPTYELALQTGKVIEqmgKFY 98
Cdd:cd17918    15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAY---KNGKQVAILVPTEILAHQHYEEAR---KFL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  99 PELKLAYAVRGNKlergQKISEQI--VIGTpgtvldwcSKLKFIDPKKikvfvlDEADVMIATQGHQ---DQSIRIQRMl 173
Cdd:cd17918    89 PFINVELVTGGTK----AQILSGIslLVGT--------HALLHLDVKF------KNLDLVIVDEQHRfgvAQREALYNL- 149

                         170
                  ....*....|..
gi 1001624453 174 pRNCQMLLFSAT 185
Cdd:cd17918   150 -GATHFLEATAT 160
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 246-343 7.47e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 7.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 246 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 325
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317

                          90
                  ....*....|....*...
gi 1001624453 326 npdnETYLHRIGRTGRFG 343
Cdd:PRK11057  318 ----ESYYQETGRAGRDG 331
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
 258-385 9.06e-06

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: 45.76  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 258 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 332
Cdd:cd18798    43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1001624453 333 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 385
Cdd:cd18798   110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 41-153 1.55e-05

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: 45.34  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  41 QNLIAQSQSGTGKTaaFVLAMLSR------VEPSDRYPQCLCLSPTYELALQTGKVIEQ-----MGKFYPELKLAYAVRG 109
Cdd:cd18034    17 RNTIVVLPTGSGKT--LIAVMLIKemgelnRKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlkVGEYSGEMGVDKWTKE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1001624453 110 NKLERGQKIseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 153
Cdd:cd18034    95 RWKEELEKY--DVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 269-359 1.69e-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: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 269 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 347
Cdd:cd18792    63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136

                          90
                  ....*....|..
gi 1001624453 348 AVNMVDSKHSMN 359
Cdd:cd18792   137 CYLLYPDPKKLT 148
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 244-353 2.13e-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: 44.08  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 244 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 323
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1001624453 324 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 353
Cdd:cd18795   121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 253-315 2.43e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 2.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1001624453 253 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 315
Cdd:PRK10917  490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 269-365 4.32e-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: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 269 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 347
Cdd:cd18811    64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137

                          90
                  ....*....|....*...
gi 1001624453 348 AVNMVDSKHSMNILNRIQ 365
Cdd:cd18811   138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 243-315 9.18e-05

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


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 44.48  E-value: 9.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1001624453 243 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 315
Cdd:COG4098   320 RQLLIFVPTIELLEQLVALLQKLFPEERIAG----VhaedPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAV 392
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 247-341 1.90e-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: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 247 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 320
Cdd:cd18796    43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119

                          90       100
                  ....*....|....*....|..
gi 1001624453 321 vdkdGNPDNET-YLHRIGRTGR 341
Cdd:cd18796   120 ----GSPKSVArLLQRLGRSGH 137
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 246-349 2.68e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 43.35  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453  246 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 325
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763

                           90       100
                   ....*....|....*....|....
gi 1001624453  326 npdnetYLHRIGRTGRFGKRGLAV 349
Cdd:PLN03137   764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 269-359 6.98e-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: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 269 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 347
Cdd:cd18810    54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127

                          90
                  ....*....|..
gi 1001624453 348 AVNMVDSKHSMN 359
Cdd:cd18810   128 AYFLYPDQKKLT 139
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
 147-345 1.37e-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: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 147 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpnviklkREEETLDTI---KQYYVL 222
Cdd:cd09639   126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1001624453 223 CSSRD-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 294
Cdd:cd09639   197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1001624453 295 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 345
Cdd:cd09639   277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
253-308 1.58e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.42  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1001624453 253 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 308
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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