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Conserved domains on  [gi|1394533528|ref|NP_001350867|]
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ATP-dependent RNA helicase DDX19B isoform 6 [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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
80-308 1.35e-145

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: 415.96  E-value: 1.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  80 NQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 160 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 239
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 240 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 308
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 2.60e-51

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 312 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 391
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533528 392 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 448
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 ...
80-308 1.35e-145

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: 415.96  E-value: 1.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  80 NQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 160 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 239
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 240 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 308
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
98-481 1.07e-121

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 362.16  E-value: 1.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANKYPQCLCLSPT 176
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 249
Cdd:COG0513    81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 250 DVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQAL 329
Cdd:COG0513   155 DRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 330 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 409
Cdd:COG0513   233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533528 410 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 481
Cdd:COG0513   313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
96-474 6.13e-97

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 297.89  E-value: 6.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  96 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSP 175
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 176 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDE 248
Cdd:PTZ00424  105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 249 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQA 328
Cdd:PTZ00424  179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 329 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 408
Cdd:PTZ00424  258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 409 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 474
Cdd:PTZ00424  338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 2.60e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 312 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 391
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533528 392 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 448
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-286 2.51e-38

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: 137.37  E-value: 2.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 121 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 200
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 201 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 278
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 1394533528 279 SATFEDSV 286
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
112-315 3.24e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 133.00  E-value: 3.24e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  112 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMG 191
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  192 KFYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 268
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1394533528  269 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 315
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
324-439 1.62e-31

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.93  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 324 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 401
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1394533528 402 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 439
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
353-439 1.79e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.29  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  353 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 432
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 1394533528  433 GRTGRFG 439
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
288-440 2.67e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.99  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 288 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 361
Cdd:COG1111   309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 362 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 433
Cdd:COG1111   377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450

                  ....*..
gi 1394533528 434 RTGRFGK 440
Cdd:COG1111   451 RTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
288-437 1.55e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.64  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 288 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 356
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 357 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 428
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                  ....*....
gi 1394533528 429 LHRIGRTGR 437
Cdd:PRK13766  458 IQRKGRTGR 466
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
80-308 1.35e-145

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: 415.96  E-value: 1.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  80 NQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLS 159
Cdd:cd18048     1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 160 QVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPK 239
Cdd:cd18048    81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 240 KIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 308
Cdd:cd18048   161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
97-301 1.99e-134

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 386.38  E-value: 1.99e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  97 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 176
Cdd:cd18047     1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 256
Cdd:cd18047    81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1394533528 257 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd18047   161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
104-301 2.35e-126

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: 365.36  E-value: 2.35e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 104 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQT 183
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 184 GKVIEQMGKFyPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQSI 263
Cdd:cd17963    81 GEVVEKMGKF-TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSI 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1394533528 264 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd17963   159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
98-481 1.07e-121

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 362.16  E-value: 1.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANKYPQCLCLSPT 176
Cdd:COG0513     3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQTGKVIEQMGKFYPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 249
Cdd:COG0513    81 RELALQVAEELRKLAKYLG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 250 DVMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQAL 329
Cdd:COG0513   155 DRMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 330 CNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV 409
Cdd:COG0513   233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533528 410 VINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 481
Cdd:COG0513   313 VINYDLPEDP------EDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
96-474 6.13e-97

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 297.89  E-value: 6.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  96 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSP 175
Cdd:PTZ00424   27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 176 TYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDE 248
Cdd:PTZ00424  105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 249 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQA 328
Cdd:PTZ00424  179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 329 LCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVS 408
Cdd:PTZ00424  258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 409 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 474
Cdd:PTZ00424  338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
95-477 1.61e-72

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 236.62  E-value: 1.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  95 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLS 174
Cdd:PRK11776    2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 175 PTYELALQTGKVIEQMGKFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 247
Cdd:PRK11776   80 PTRELADQVAKEIRRLARFIPNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 248 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKrEEETLDTIKQYYVLCSsRDEKFQ 327
Cdd:PRK11776  155 EADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVS-PDERLP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 328 ALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGIDVE 405
Cdd:PRK11776  232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIK 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533528 406 QVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLD 477
Cdd:PRK11776  310 ALEAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLGRKLNWEPLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
99-476 1.51e-71

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 233.30  E-value: 1.51e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANK--YPQCLCLS 174
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKsgPPRILILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 175 PTYELALQtgkVIEQMGKFYPELKL---------AYAVRGNKLERGQkiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFV 245
Cdd:PRK11192   81 PTRELAMQ---VADQARELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DCRAVETLI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 246 LDEADVMIATQGHQD-QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNVIKL---KREEETldtIKQYYVLC 319
Cdd:PRK11192  153 LDEADRMLDMGFAQDiETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---IHQWYYRA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 320 SSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCA 399
Cdd:PRK11192  227 DDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAA 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533528 400 RGIDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRIQEHFNKKIERLDTDDL 476
Cdd:PRK11192  307 RGIDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKIERYIEEPLKARVIDEL 376
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
99-469 6.02e-61

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 206.69  E-value: 6.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKY---PQCL 171
Cdd:PRK01297   89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLqtppPKERYmgePRAL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 172 CLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 247
Cdd:PRK01297  167 IIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 248 EADVMIaTQGHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeK 325
Cdd:PRK01297  245 EADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-K 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 326 FQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVE 405
Cdd:PRK01297  323 YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533528 406 QVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKIE 469
Cdd:PRK01297  403 GISHVINFTLPED----PDD--YVHRIGRTGRAGASGVSISFAGEDDAFQ-LPEIEELLGRKIS 459
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
98-451 2.53e-58

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 203.16  E-value: 2.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 177
Cdd:PRK11634    7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 178 ELALQTGKVIEQMGKFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIa 254
Cdd:PRK11634   85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 255 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ-YYVLCSSRdeKFQALCNLY 333
Cdd:PRK11634  163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 334 GAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINF 413
Cdd:PRK11634  241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1394533528 414 DLPVdkdgnpDNETYLHRIGRTGRFGKRGLAVNMVDSK 451
Cdd:PRK11634  321 DIPM------DSESYVHRIGRTGRAGRAGRALLFVENR 352
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
97-468 3.24e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 192.88  E-value: 3.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  97 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY---PQ 169
Cdd:PRK04837    8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 170 CLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVL 246
Cdd:PRK04837   86 ALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 247 DEADVMIATQGHQDqsIR--IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ--YYvlcSS 321
Cdd:PRK04837  164 DEADRMFDLGFIKD--IRwlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 322 RDEKFQALCNLYGAITIAQAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNV 397
Cdd:PRK04837  239 NEEKMRLLQTLIEEEWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533528 398 CARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 468
Cdd:PRK04837  315 AARGLHIPAVTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSI 378
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
90-468 3.63e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 196.32  E-value: 3.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  90 NSPLYSVkSFEELRLKPQLLQGVYAMGFNRPSKIQenALPLMLAEPPQNLIAQSQSGTGKTAAFVLA----MLSQVEPAN 165
Cdd:PRK04537    3 DKPLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQ--ALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnrLLSRPALAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 166 KYPQ---CLCLSPTYELALQTGKvieQMGKFYPELKLAYAV--RGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKFID 237
Cdd:PRK04537   80 RKPEdprALILAPTRELAIQIHK---DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 238 PKKIKVFVLDEADVMIATQGHQDqsIR-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNviKLKREEETLDTIK- 313
Cdd:PRK04537  157 LHACEICVLDEADRMFDLGFIKD--IRfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARv 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 314 QYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLV 393
Cdd:PRK04537  233 RQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILV 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533528 394 TTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 468
Cdd:PRK04537  313 ATDVAARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAMS-LPDIEAYIEQKI 380
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
108-301 5.25e-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: 174.55  E-value: 5.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP----ANKYPQCLCLSPTYELALQT 183
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 184 GKVIEQMGKfYPELKlAYAVRGnklerGQKISEQ---------IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIa 254
Cdd:cd00268    79 AEVARKLGK-GTGLK-VAAIYG-----GAPIKKQiealkkgpdIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML- 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533528 255 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd00268   150 DMGFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
312-448 2.60e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.38  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 312 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 391
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533528 392 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 448
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
98-448 1.01e-50

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 178.85  E-value: 1.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML-----SQVEPANKYP-QCL 171
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLqhlitRQPHAKGRRPvRAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 172 CLSPTYELALQTGKVIEQMGKFYPELKLAyaVRGnklerGQKISEQ---------IVIGTPGTVLDwCSKLKFIDPKKIK 242
Cdd:PRK10590   80 ILTPTRELAAQIGENVRDYSKYLNIRSLV--VFG-----GVSINPQmmklrggvdVLVATPGRLLD-LEHQNAVKLDQVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 243 VFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYyVLCSSR 322
Cdd:PRK10590  152 ILVLDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 323 DEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGI 402
Cdd:PRK10590  230 KRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533528 403 DVEQVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAVNMV 448
Cdd:PRK10590  310 DIEELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSLV 349
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
101-300 3.30e-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: 164.80  E-value: 3.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 101 ELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYEL 179
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTREL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 180 ALQTGKVIEQMGkFYPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQ 256
Cdd:cd17939    78 AQQIQKVVKALG-DYMGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1394533528 257 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
Cdd:cd17939   155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
99-297 1.31e-46

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 160.69  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 177
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 178 ELALQTGKVIEQMGkFYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEAD 250
Cdd:cd18046    78 ELAQQIQKVVMALG-DYMGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEAD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533528 251 VMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd18046   152 EML-SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
99-300 1.78e-46

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 160.16  E-value: 1.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 178
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 179 LALQTGKVIEQMGKfYPELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaT 255
Cdd:cd17940    79 LALQTSQVCKELGK-HMGVKVMVTTGGTSLrDDIMRLYQtvHVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADKLL-S 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1394533528 256 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
Cdd:cd17940   156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
99-300 4.16e-41

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: 146.07  E-value: 4.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 177
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIkPIIKG---RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 178 ELALQTGKVIEQMGKFYpELKLAYAVRGN-------KLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEAD 250
Cdd:cd18045    78 ELAVQIQKVLLALGDYM-NVQCHACIGGTsvgddirKLDYGQ----HIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEAD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533528 251 VMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
Cdd:cd18045   152 EML-NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
PTZ00110 PTZ00110
helicase; Provisional
96-444 6.83e-41

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 153.78  E-value: 6.83e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  96 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQC 170
Cdd:PTZ00110  129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHInaQPLLRYgdgPIV 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 171 LCLSPTYELALQtgkVIEQMGKFYPELKLAYAV-RGNKLERGQKIS----EQIVIGTPGTVLDW----CSKLKfidpkKI 241
Cdd:PTZ00110  207 LVLAPTRELAEQ---IREQCNKFGASSKIRNTVaYGGVPKRGQIYAlrrgVEILIACPGRLIDFlesnVTNLR-----RV 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 242 KVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNV------IKLKreeeTLDTIKQY 315
Cdd:PTZ00110  279 TYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVhvnvgsLDLT----ACHNIKQE 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 316 YVLCSSRdEKFQALCNLYGAITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLV 393
Cdd:PTZ00110  354 VFVVEEH-EKRGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533528 394 TTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 444
Cdd:PTZ00110  433 ATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGAS 477
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
98-449 3.20e-40

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 151.48  E-value: 3.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS-------QVEPANKYPQC 170
Cdd:PLN00206  122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLA 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 171 LCLSPTYELALQTGKVIEQMGKFYPeLKLAYAVRGN----KLERGQKISEQIViGTPGTVLDWCSKLKfIDPKKIKVFVL 246
Cdd:PLN00206  200 MVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDampqQLYRIQQGVELIV-GTPGRLIDLLSKHD-IELDNVSVLVL 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 247 DEADVMIaTQGHQDQSIRIQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKF 326
Cdd:PLN00206  277 DEVDCML-ERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQ 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 327 QalcnLYGAITIAQ-----AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCAR 400
Cdd:PLN00206  355 K----LFDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533528 401 GIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 449
Cdd:PLN00206  431 GVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
121-286 2.51e-38

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: 137.37  E-value: 2.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 121 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 200
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 201 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 278
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 1394533528 279 SATFEDSV 286
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
98-301 2.90e-36

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: 133.20  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLS--QVEPANKYPQCLCLSP 175
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEklKAHSPTVGARALILSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 176 TYELALQTGKVIEQMGKFyPELKLAYAVRGNKLERG-QKISEQ--IVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVM 252
Cdd:cd17959    80 TRELALQTLKVTKELGKF-TDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533528 253 IAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd17959   158 FE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEXDc smart00487
DEAD-like helicases superfamily;
112-315 3.24e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 133.00  E-value: 3.24e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  112 VYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMG 191
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  192 KFYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRM 268
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1394533528  269 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 315
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
108-301 1.97e-35

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: 130.46  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVI 187
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 188 EQMGKFYPELKLAYAVRGNKLERG-QKISE-QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIR 264
Cdd:cd17943    79 KKIGKKLEGLKCEVFIGGTPVKEDkKKLKGcHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNW 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1394533528 265 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd17943   156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
98-297 3.49e-34

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: 127.46  E-value: 3.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALP-LMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 176
Cdd:cd17950     3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPqAILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQTGKVIEQMGKFYPELKLAY-----AVRGNKlERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADV 251
Cdd:cd17950    80 RELAFQISNEYERFSKYMPNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDK 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533528 252 MIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17950   158 MLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
104-302 4.49e-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: 127.31  E-value: 4.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 104 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTY 177
Cdd:cd17961     1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIqkilkaKAESGEEQGTRALILVPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 178 ELALQTGKVIEQMGKFY-PELKLAyAVRGNKLERGQK--ISEQ--IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM 252
Cdd:cd17961    79 ELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRalLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533528 253 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKL 302
Cdd:cd17961   158 L-SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
108-290 9.23e-32

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 120.44  E-value: 9.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLSPTYELALQTG 184
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 185 KVIEQMGKFYPeLKLAYAVRGNKL---ERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQ 261
Cdd:cd17947    79 SVLQQLAQFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADE 156
                         170       180
                  ....*....|....*....|....*....
gi 1394533528 262 SIRIQRMLPRNCQMLLFSATFEDSVWKFA 290
Cdd:cd17947   157 LKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
98-297 1.16e-31

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 120.50  E-value: 1.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 177
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 178 ELALQTGKVIEQMGKFyPELKLAYAVRG-----NKLERGQKisEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM 252
Cdd:cd17954    79 ELAQQISEQFEALGSS-IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1394533528 253 IatqgHQDQSIRIQRML---PRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17954   156 L----NMDFEPEIDKILkviPRERTTYLFSATMTTKVAKLQRASLKNP 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
324-439 1.62e-31

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.93  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 324 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 401
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1394533528 402 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 439
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
99-297 2.13e-31

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: 119.73  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVepankypQCLCLSPTYE 178
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 179 LALQTGKVIEQMGKFY--PELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI 253
Cdd:cd17938    72 LAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533528 254 aTQGHQDQSIRIQRMLP------RNCQMLLFSATFE-DSVWKFAQKVVPDP 297
Cdd:cd17938   151 -SQGNLETINRIYNRIPkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
99-297 4.36e-29

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: 113.47  E-value: 4.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  99 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYpqCLCLSPT 176
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILA--GRDVIGGAKTGSGKTAAFALPILQRlsEDPYGIF--ALVLTPT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQtgkVIEQM---GKFyPELKLAYAVRG-NKLERGQKISEQ--IVIGTPGTVLDW---CSKLKFiDPKKIKVFVLD 247
Cdd:cd17955    77 RELAYQ---IAEQFralGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533528 248 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17955   152 EADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
104-300 1.11e-28

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: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 104 LKPQLLQGVYAMGFNRPSKIQENALPLMLaEPPQNLIAQSQSGTGKTAAFVL----AMLSQVEPANKYP-QCLCLSPTYE 178
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 179 LALQTGKVIEQMGKFYPELKLAYAVRGNK----LERGQKISEQIVIGTPG---TVLDWCSKLKFIdpKKIKVFVLDEADV 251
Cdd:cd17964    80 LALQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGrliDHLENPGVAKAF--TDLDYLVLDEADR 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533528 252 MIaTQGHQDQSIRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNVI 300
Cdd:cd17964   158 LL-DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
98-291 2.23e-28

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: 111.81  E-value: 2.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  98 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANK--------Y 167
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLleDGPPSvgrgrrkaY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 168 PQCLCLSPTYELALQTgkvieqmgkfYPE-LKLAY-------AVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKLKf 235
Cdd:cd17967    79 PSALILAPTRELAIQI----------YEEaRKFSYrsgvrsvVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533528 236 IDPKKIKVFVLDEADVMIaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 291
Cdd:cd17967   148 ISLSSIKFLVLDEADRML-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
108-297 6.02e-28

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: 109.95  E-value: 6.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVI 187
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 188 EQMGKFYPELKLAYAVRGN----KLERGQKiSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 263
Cdd:cd17962    79 KELMKGLPPMKTALLVGGLplppQLYRLQQ-GVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVL 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1394533528 264 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17962   156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
82-292 2.61e-27

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: 110.44  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  82 VEVLQRDPNSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ- 160
Cdd:cd18052    31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGm 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 161 ----VEPAN----KYPQCLCLSPTYELALQTGKvieQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIG 221
Cdd:cd18052   106 mkegLTASSfsevQEPQALIVAPTRELANQIFL---EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVA 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533528 222 TPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATQGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 292
Cdd:cd18052   177 TPGRLLDFIGRGK-ISLSKLKYLILDEADRMLDMGFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
HELICc smart00490
helicase superfamily c-terminal domain;
353-439 1.79e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.29  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  353 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 432
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 1394533528  433 GRTGRFG 439
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, ...
108-286 4.34e-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: 4.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQ--CLCLSPTYELALQ 182
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 183 TGKVIEQMGKFY-PELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLD-WCSKLKFIDPKKIKVFVLDEADVMIATq 256
Cdd:cd17960    79 IYEVLQSFLEHHlPKLKCQLLIGGTNVEEDVKKfkrnGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL- 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 1394533528 257 GHQDQSIRIQRMLPRNCQMLLFSATFEDSV 286
Cdd:cd17960   158 GFEADLNRILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
108-300 1.39e-21

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: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQ 182
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 183 TGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQD 260
Cdd:cd17952    79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFEY 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1394533528 261 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
Cdd:cd17952   157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
96-297 1.56e-21

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: 92.83  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  96 VKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQC 170
Cdd:cd17953    11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 171 LCLSPTYELALQtgkVIEQMGKFYPELKL-AYAVRGnklerGQKISEQ---------IVIGTPGTVLDW--CSKLKFIDP 238
Cdd:cd17953    89 LIMAPTRELALQ---IYVECKKFSKALGLrVVCVYG-----GSGISEQiaelkrgaeIVVCTPGRMIDIltANNGRVTNL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 239 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17953   161 RRVTYVVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
109-300 3.61e-21

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: 91.20  E-value: 3.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 109 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEpANKYPQ-----CLCLSPTYELALQT 183
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLY-RERWTPedglgALIISPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 184 GKVIEQMGKfYPELKLAYAVRGNKLERGQ-KISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQ 261
Cdd:cd17941    79 FEVLRKVGK-YHSFSAGLIIGGKDVKEEKeRINRmNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKET 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1394533528 262 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
Cdd:cd17941   157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
108-292 4.03e-21

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: 91.61  E-value: 4.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAML---SQVEPANKY-----PQCLCLSPTYEL 179
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLvyiSRLPPLDEEtkddgPYALILAPTREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 180 ALQTGKVIEQMGKFYPeLKLAYAVRGNKLE-RGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQ 256
Cdd:cd17945    79 AQQIEEETQKFAKPLG-IRVVSIVGGHSIEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DM 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 257 GHQDQSIRIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQK 292
Cdd:cd17945   156 GFEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKG 211
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
108-297 8.78e-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: 89.96  E-value: 8.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEPpqNLIAQSQSGTGKTAAFVLAMLSQVEP--ANKYPQCLCLSPTYELALQTGK 185
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 186 VIEQMGKFYPE-----LKLAYAVRGNKLERGQKISeqIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATqGHQD 260
Cdd:cd17957    79 ELLKLSKGTGLrivllSKSLEAKAKDGPKSITKYD--ILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFRE 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1394533528 261 QSIRIQRMLPRNC-QMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17957   155 QTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
108-282 2.12e-20

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: 89.99  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAM----LSQVE-----PANKYPQCLCLSPTYE 178
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPIlerlLSQKSsngvgGKQKPLRALILTPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 179 LALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDW----CSKLKFIdpKKIKVFVLDEADV 251
Cdd:cd17946    80 LAVQVKDHLKAIAK-YTNIKIASIVGGLAVQKQERLLKKrpeIVVATPGRLWELiqegNEHLANL--KSLRFLVLDEADR 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1394533528 252 MIaTQGHQDQSIRIQRMLPRNC-------QMLLFSATF 282
Cdd:cd17946   157 ML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
82-282 2.13e-20

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: 90.48  E-value: 2.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  82 VEVLQRDPNSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV 161
Cdd:cd18051     9 VEATGENCPPH---IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 162 ------EPA----------NKYPQCLCLSPTYELALQtgkVIEQMGKFypelklAY--AVRGNKLERGQKISEQI----- 218
Cdd:cd18051    84 yeqgpgESLpsesgyygrrKQYPLALVLAPTRELASQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdler 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533528 219 ----VIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 282
Cdd:cd18051   155 gchlLVATPGRLVDMLERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
108-297 1.61e-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: 86.36  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY--PQCLCLSPTYELAL 181
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRngPGVLVLTPTRELAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 182 QtgkVIEQMGKF-YPELKlAYAVRGNKlERGQKISEQ-----IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaT 255
Cdd:cd17958    79 Q---IEAECSKYsYKGLK-SVCVYGGG-NRNEQIEDLskgvdIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-D 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1394533528 256 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17958   152 MGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
115-301 1.71e-19

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: 86.87  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 115 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPA------NKYPQCLCLSPTYELALQTGKVIE 188
Cdd:cd17949     9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdrSDGTLALVLVPTRELALQIYEVLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 189 QMGKFYPELKLAYAVRGNKlergqKISEQ--------IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQD 260
Cdd:cd17949    87 KLLKPFHWIVPGYLIGGEK-----RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533528 261 QSIRIQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 301
Cdd:cd17949   161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
108-300 1.03e-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: 84.31  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYPQC-------LCLSPTYEL 179
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLIMFaLEQEKKLPFIkgegpygLIVCPSREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 180 ALQTGKVIEQMGKF-----YPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADV 251
Cdd:cd17951    79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533528 252 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 300
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 ...
109-281 9.26e-18

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 81.25  E-value: 9.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 109 LQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCLSPTYELALQTG 184
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 185 KVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQS 262
Cdd:cd17942    80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEEEM 158
                         170
                  ....*....|....*....
gi 1394533528 263 IRIQRMLPRNCQMLLFSAT 281
Cdd:cd17942   159 RQIIKLLPKRRQTMLFSAT 177
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
108-297 1.97e-17

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 80.49  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPANKyPQCLCLSPTYELAL 181
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHInaqpplERGDG-PIVLVLAPTRELAQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 182 QtgkVIEQMGKFYPELKL----AY--AVRGNK---LERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVM 252
Cdd:cd17966    78 Q---IQQEANKFGGSSRLrntcVYggAPKGPQirdLRRGV----EICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRM 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533528 253 IaTQGHQDQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 297
Cdd:cd17966   150 L-DMGFEPQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
83-296 1.88e-14

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: 72.73  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  83 EVLQRDPNSPlYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV- 161
Cdd:cd18049    11 EITVRGHNCP-KPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHIn 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 162 -EPANKY---PQCLCLSPTYELALQTGKVIEQMGK--------FYPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDW 229
Cdd:cd18049    88 hQPFLERgdgPICLVLAPTRELAQQVQQVAAEYGRacrlkstcIYGGAPKGPQIR--DLERGV----EICIATPGRLIDF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 230 --CSKLKFidpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 296
Cdd:cd18049   162 leAGKTNL---RRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
83-296 3.06e-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: 72.74  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  83 EVLQRDPNSPlYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV- 161
Cdd:cd18050    49 EITIRGVGCP-KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHIn 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 162 -EP---ANKYPQCLCLSPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWC 230
Cdd:cd18050   126 hQPyleRGDGPICLVLAPTRELAQQVQQVADDYGK-SSRLKSTCIYGGapkgpqiRDLERGV----EICIATPGRLIDFL 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 231 SKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 296
Cdd:cd18050   201 EAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
137-292 8.97e-14

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 69.88  E-value: 8.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 137 QNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfypelKLAYAVRGNKLER 210
Cdd:cd17944    28 KDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 211 GQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSAT 281
Cdd:cd17944   103 QQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSAT 181
                         170
                  ....*....|.
gi 1394533528 282 FEDSVWKFAQK 292
Cdd:cd17944   182 CPDWVYNVAKK 192
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
146-482 1.09e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 146 GTGKT--AAFVLAMLSQVEPAnkypqcLCLSPTYELALQTGKVIEQMgkfypeLKLAYAVRGNKlergqKISEQIVIGTP 223
Cdd:COG1061   110 GTGKTvlALALAAELLRGKRV------LVLVPRRELLEQWAEELRRF------LGDPLAGGGKK-----DSDAPITVATY 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 224 GTVldwcSKLKFID--PKKIKVFVLDEAdvmiatqgHQDQSIRIQRMLPR--NCQMLLFSAT--FEDSVWKF-------- 289
Cdd:COG1061   173 QSL----ARRAHLDelGDRFGLVIIDEA--------HHAGAPSYRRILEAfpAAYRLGLTATpfRSDGREILlflfdgiv 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 290 ---------AQKVVPDPNVI----KLKREEETLDTIKQ--YYVLCSSRDEKFQALCNLYGAIT-IAQAMIFCHTRKTASW 353
Cdd:COG1061   241 yeyslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 354 LAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdGNPDneTYLHRIG 433
Cdd:COG1061   321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT---GSPR--EFIQRLG 394
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533528 434 R---TGRFGKRGLAVNMVDSKHSM--NILNRIQEHFNKKIERLDTDDLDEIEKI 482
Cdd:COG1061   395 RglrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
138-281 1.41e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 67.81  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 138 NLIAQSQSGTGKTAAFVLAMLSQVEPanKYPQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKI-- 214
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlg 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533528 215 SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 281
Cdd:cd00046    79 DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
288-440 2.67e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.99  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 288 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 361
Cdd:COG1111   309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 362 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 433
Cdd:COG1111   377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450

                  ....*..
gi 1394533528 434 RTGRFGK 440
Cdd:COG1111   451 RTGRKRE 457
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
343-439 5.29e-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: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 343 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 420
Cdd:cd18793    32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107
                          90
                  ....*....|....*....
gi 1394533528 421 GNPDNEtyLHRIGRTGRFG 439
Cdd:cd18793   108 WNPAVE--EQAIDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
343-439 1.08e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.09  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 343 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 420
Cdd:COG0553   554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630
                          90
                  ....*....|....*....
gi 1394533528 421 gNPDNEtyLHRIGRTGRFG 439
Cdd:COG0553   631 -NPAVE--EQAIDRAHRIG 646
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
108-295 2.92e-10

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: 60.46  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKY--PQCLCLSPTYELA 180
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLlryklLAEGPFnaPRGLVITPSRELA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 181 LQTGKVIEQMGKFYPeLKlAYAVRGNKLERGQKISEQ----IVIGTPGTVldwcSKL---KFIDPKKIKVFVLDEADVMI 253
Cdd:cd17948    79 EQIGSVAQSLTEGLG-LK-VKVITGGRTKRQIRNPHFeevdILVATPGAL----SKLltsRIYSLEQLRHLVLDEADTLL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1394533528 254 -------------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 295
Cdd:cd17948   153 ddsfneklshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
322-416 3.34e-10

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 57.99  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 322 RDEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 382
Cdd:cd18802     5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1394533528 383 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 416
Cdd:cd18802    85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
343-440 9.45e-10

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 56.45  E-value: 9.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 343 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 422
Cdd:cd18794    35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108
                          90
                  ....*....|....*...
gi 1394533528 423 PDNETYLHRIGRTGRFGK 440
Cdd:cd18794   109 KSMESYYQESGRAGRDGL 126
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
108-281 2.82e-09

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: 57.26  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 108 LLQGVYAMGFNRPSKIQENALPLMLAE-------PPQNLIAQSQSGTGKTAAFVL----AMLSQVEPAnkyPQCLCLSPT 176
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVPR---LRALIVVPT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 177 YELALQTGKVIEQMGKFYPeLKLAyAVRGNK-----------LERGQKISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVF 244
Cdd:cd17956    78 KELVQQVYKVFESLCKGTG-LKVV-SLSGQKsfkkeqklllvDTSGRYLSRvDILVATPGRLVDHLNSTPGFTLKHLRFL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 245 VLDEAD-------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 281
Cdd:cd17956   156 VIDEADrllnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
343-445 3.43e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 343 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 420
Cdd:COG0514   235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308
                          90       100
                  ....*....|....*....|....*
gi 1394533528 421 GNPdnETYLHRIGRTGRFGKRGLAV 445
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 ...
341-437 5.03e-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: 51.97  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 341 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 410
Cdd:cd18801    33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
                          90       100
                  ....*....|....*....|....*..
gi 1394533528 411 INFdlpvdkDGNPDNETYLHRIGRTGR 437
Cdd:cd18801   113 ICY------DASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
339-445 2.20e-07

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 53.30  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 339 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 412
Cdd:COG1205   289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1394533528 413 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 445
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 ...
328-445 5.06e-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: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 328 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 400
Cdd:cd18797    29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533528 401 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 445
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) ...
347-467 9.97e-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: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 347 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 426
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533528 427 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 467
Cdd:cd18790   114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
PRK13766 PRK13766
Hef nuclease; Provisional
288-437 1.55e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.64  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 288 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 356
Cdd:PRK13766  321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 357 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 428
Cdd:PRK13766  384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                  ....*....
gi 1394533528 429 LHRIGRTGR 437
Cdd:PRK13766  458 IQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
390-442 2.06e-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: 45.39  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1394533528 390 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 442
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
137-249 5.22e-06

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: 47.26  E-value: 5.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 137 QNLIAQSQSGTGKT--AAFVL-AMLSQV-EPANKYPQCLCLSPTYELALQTGKVIEQ-----MGKFYPELKLAYAVRGNK 207
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIkEMGELNrKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlkVGEYSGEMGVDKWTKERW 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1394533528 208 LERGQKIseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 249
Cdd:cd18034    97 KEELEKY--DVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
342-439 1.11e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 342 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 421
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                          90
                  ....*....|....*...
gi 1394533528 422 npdnETYLHRIGRTGRFG 439
Cdd:PRK11057  318 ----ESYYQETGRAGRDG 331
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
354-481 1.24e-05

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


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 45.76  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 354 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 428
Cdd:cd18798    43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533528 429 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 481
Cdd:cd18798   110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
119-281 1.27e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 45.87  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 119 RPSKIQENALPL----MLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEpANKypQCLCLSPTYELALQTGKVIEqmgKFY 194
Cdd:cd17918    15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAYK-NGK--QVAILVPTEILAHQHYEEAR---KFL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 195 PELKLAYAVRGNKlergQKISEQI--VIGTpgtvldwcSKLKFIDPKKikvfvlDEADVMIATQGHQ---DQSIRIQRMl 269
Cdd:cd17918    89 PFINVELVTGGTK----AQILSGIslLVGT--------HALLHLDVKF------KNLDLVIVDEQHRfgvAQREALYNL- 149
                         170
                  ....*....|..
gi 1394533528 270 pRNCQMLLFSAT 281
Cdd:cd17918   150 -GATHFLEATAT 160
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
365-455 2.03e-05

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 44.57  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 365 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 443
Cdd:cd18792    63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136
                          90
                  ....*....|..
gi 1394533528 444 AVNMVDSKHSMN 455
Cdd:cd18792   137 CYLLYPDPKKLT 148
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
340-449 2.23e-05

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 44.47  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 340 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 419
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1394533528 420 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 449
Cdd:cd18795   121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
349-411 3.57e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 3.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533528 349 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 411
Cdd:PRK10917  490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
365-461 4.89e-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: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 365 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 443
Cdd:cd18811    64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137
                          90
                  ....*....|....*...
gi 1394533528 444 AVNMVDSKHSMNILNRIQ 461
Cdd:cd18811   138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
339-411 1.23e-04

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


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 44.48  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533528 339 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 411
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 ...
343-437 2.49e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 41.48  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 343 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 416
Cdd:cd18796    43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119
                          90       100
                  ....*....|....*....|..
gi 1394533528 417 vdkdGNPDNET-YLHRIGRTGR 437
Cdd:cd18796   120 ----GSPKSVArLLQRLGRSGH 137
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
342-445 4.77e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528  342 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 421
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                           90       100
                   ....*....|....*....|....
gi 1394533528  422 npdnetYLHRIGRTGRFGKRGLAV 445
Cdd:PLN03137   764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
365-455 1.03e-03

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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 365 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 443
Cdd:cd18810    54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127
                          90
                  ....*....|..
gi 1394533528 444 AVNMVDSKHSMN 455
Cdd:cd18810   128 AYFLYPDQKKLT 139
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
243-441 1.72e-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: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 243 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpnviklkREEETLDTI---KQYYVL 318
Cdd:cd09639   126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 319 CSSRD-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 390
Cdd:cd09639   197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1394533528 391 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 441
Cdd:cd09639   277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
349-404 2.29e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.42  E-value: 2.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533528 349 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 404
Cdd:COG1200   488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
338-417 9.94e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 36.00  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533528 338 IAQAMIFCHTRKTASWLAAELSKEG-HQVALLSGEMMVEQRAAVIER--FREGKEKVLVTTNVCARGIDVEQVSVVInFD 414
Cdd:cd18799     6 EIKTLIFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDEALILlfFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84

                  ...
gi 1394533528 415 LPV 417
Cdd:cd18799    85 RPT 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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