NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27545267|ref|NP_775365|]
View 

ATP-dependent RNA helicase DDX19B [Danio rerio]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209184)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 83-311 7.15e-143

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


The actual alignment was detected with superfamily member cd18048:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 229  Bit Score: 409.03  E-value: 7.15e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  83 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEPPQNLIAQSQSRTGKTAAFVLAMLS 162
Cdd:cd18048   1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 163 HVDTENKWPECLCVCPTYELALQTGKVIEQMGKHYPEVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKLKFIDPK 242
Cdd:cd18048  81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27545267 243 KIKVFVLDEADVMIATQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEET 311
Cdd:cd18048 161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 315-450 8.48e-53

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: 174.23  E-value: 8.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 315 IKQYYVICNSKEEKFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKV 394
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267 395 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINM 450
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITF 130
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 83-311 7.15e-143

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 409.03  E-value: 7.15e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  83 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEPPQNLIAQSQSRTGKTAAFVLAMLS 162
Cdd:cd18048   1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 163 HVDTENKWPECLCVCPTYELALQTGKVIEQMGKHYPEVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKLKFIDPK 242
Cdd:cd18048  81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27545267 243 KIKVFVLDEADVMIATQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEET 311
Cdd:cd18048 161 NISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
101-484 1.88e-118

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 354.07  E-value: 1.88e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE-NKWPECLCVCPT 179
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 180 YELALQTGKVIEQMGKHYP-EVQLVY---AIRG--NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEAD 253
Cdd:COG0513  81 RELALQVAEELRKLAKYLGlRVATVYggvSIGRqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEAD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 254 VMIAtQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQYYVICNsKEEKFQALC 333
Cdd:COG0513 156 RMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVD-KRDKLELLR 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 334 NIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVV 413
Cdd:COG0513 234 RLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27545267 414 INFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINMADSKfSMNTLNRIQDHFNKKIEKLDTDDLDEIEK 484
Cdd:COG0513 314 INYDLPEDP------EDYVHRIGRTGRAGAEGTAISLVTPD-ERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 99-477 2.77e-91

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 283.64  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   99 VKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCP 178
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  179 TYELALQTGKVIEQMGKhYPEVQLVYAIRG-------NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDE 251
Cdd:PTZ00424 105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  252 ADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQYYVICNSKEEKFQA 331
Cdd:PTZ00424 179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  332 LCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVS 411
Cdd:PTZ00424 258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267  412 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINMADSKfSMNTLNRIQDHFNKKIEKLDTD 477
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 ...
 315-450 8.48e-53

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: 174.23  E-value: 8.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 315 IKQYYVICNSKEEKFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKV 394
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267 395 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINM 450
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITF 130
DEXDc smart00487
DEAD-like helicases superfamily;
115-318 2.02e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 127.99  E-value: 2.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    115 VYAMGFNRPSKIQETALPMMLAEPpQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPeCLCVCPTYELALQTGKVIEQMG 194
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    195 KHYPEVQLVYAIRGNKLERGAKLQE---QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSVRIQRM 271
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 27545267    272 LPKTCQMLLFSATFEETVWNFAKRIVPDPniIKLKREEETLDTIKQY 318
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 124-289 1.67e-33

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: 124.28  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   124 SKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYELALQTGKVIEQMGKHYpEVQLV 203
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   204 YAIRGN--KLERGAKLQEQIVIGTPGTVLDWCQKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLF 281
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 27545267   282 SATFEETV 289
Cdd:pfam00270 155 SATLPRNL 162
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 327-442 1.00e-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: 117.70  E-value: 1.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   327 EKFQALCNIYGAITIAQAMIFCHTRKTA--GWLageLSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARG 404
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27545267   405 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 442
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
356-442 2.52e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.90  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    356 WLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 435
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 27545267    436 GRTGRFG 442
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
293-443 6.59e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.38  E-value: 6.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 293 AKRIVPDPNIIKLKREEETLDtikqyyvICNSKEEK-FQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALL 371
Cdd:COG1111 311 SKRLVSDPRFRKAMRLAEEAD-------IEHPKLSKlREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRF 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 372 SGE--------MQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIGRTGRFGK 443
Cdd:COG1111 384 VGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
 293-440 2.52e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.26  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  293 AKRIVPDPNIIKLKREEETLDtikqyyvICNSKEEKfqaLCNIYGAITIAQ----AMIFCHTRKTAGWLAGELSREGHQV 368
Cdd:PRK13766 323 SKRLVEDPRFRKAVRKAKELD-------IEHPKLEK---LREIVKEQLGKNpdsrIIVFTQYRDTAEKIVDLLEKEGIKA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  369 ALLSGE--------M-QVEQRAAvIERFRDGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETYLHRIGRTG 439
Cdd:PRK13766 393 VRFVGQaskdgdkgMsQKEQIEI-LDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRSIQRKGRTG 465


                 .
gi 27545267  440 R 440
Cdd:PRK13766 466 R 466
 
Name Accession Description Interval E-value
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 83-311 7.15e-143

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 409.03  E-value: 7.15e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  83 NQVEVLQRDPSSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEPPQNLIAQSQSRTGKTAAFVLAMLS 162
Cdd:cd18048   1 HRVEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 163 HVDTENKWPECLCVCPTYELALQTGKVIEQMGKHYPEVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKLKFIDPK 242
Cdd:cd18048  81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVT 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27545267 243 KIKVFVLDEADVMIATQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEET 311
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 ...
 100-304 2.50e-129

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 373.67  E-value: 2.50e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 100 KSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEPPQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPT 179
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 180 YELALQTGKVIEQMGKHYPEVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADVMIATQ 259
Cdd:cd18047  81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQ 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27545267 260 GHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd18047 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 107-304 9.91e-123

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: 356.50  E-value: 9.91e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 107 LKPQLLQGVYAMGFNRPSKIQETALPMMLAEPPQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYELALQT 186
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 187 GKVIEQMGKhYPEVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIATQGHQDQSV 266
Cdd:cd17963  81 GEVVEKMGK-FTGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSI 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27545267 267 RIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd17963 159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
101-484 1.88e-118

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 354.07  E-value: 1.88e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE-NKWPECLCVCPT 179
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 180 YELALQTGKVIEQMGKHYP-EVQLVY---AIRG--NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEAD 253
Cdd:COG0513  81 RELALQVAEELRKLAKYLGlRVATVYggvSIGRqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEAD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 254 VMIAtQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQYYVICNsKEEKFQALC 333
Cdd:COG0513 156 RMLD-MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVD-KRDKLELLR 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 334 NIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVV 413
Cdd:COG0513 234 RLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27545267 414 INFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINMADSKfSMNTLNRIQDHFNKKIEKLDTDDLDEIEK 484
Cdd:COG0513 314 INYDLPEDP------EDYVHRIGRTGRAGAEGTAISLVTPD-ERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
 99-477 2.77e-91

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 283.64  E-value: 2.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   99 VKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCP 178
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  179 TYELALQTGKVIEQMGKhYPEVQLVYAIRG-------NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDE 251
Cdd:PTZ00424 105 TRELAQQIQKVVLALGD-YLKVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  252 ADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQYYVICNSKEEKFQA 331
Cdd:PTZ00424 179 ADEML-SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  332 LCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVS 411
Cdd:PTZ00424 258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267  412 VVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINMADSKfSMNTLNRIQDHFNKKIEKLDTD 477
Cdd:PTZ00424 338 LVINYDLPASP------ENYIHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 102-448 1.01e-68

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 225.98  E-value: 1.01e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSH-VDTENKW---PECLCVC 177
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQHlLDFPRRKsgpPRILILT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  178 PTYELALQTGKVIEQMGKHypeVQLVYAI------RGNKLERGAKLQEqIVIGTPGTVLDWCQKLKFiDPKKIKVFVLDE 251
Cdd:PRK11192  81 PTRELAMQVADQARELAKH---THLDIATitggvaYMNHAEVFSENQD-IVVATPGRLLQYIKEENF-DCRAVETLILDE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  252 ADVMIATQGHQDqsvrIQRMLPKTC---QMLLFSATFE-ETVWNFAKRIVPDPNIIKL---KREEETldtIKQYYVICNS 324
Cdd:PRK11192 156 ADRMLDMGFAQD----IETIAAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---IHQWYYRADD 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  325 KEEKFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARG 404
Cdd:PRK11192 229 LEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 27545267  405 IDVEQVSVVINFDLPVDKDgnpdneTYLHRIGRTGRFGKRGLAI 448
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSAD------TYLHRIGRTGRAGRKGTAI 346
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 98-480 3.26e-68

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 225.45  E-value: 3.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   98 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVC 177
Cdd:PRK11776   2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  178 PTYELALQTGKVIEQMGKHYPEVQLVYAIRG-------NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLD 250
Cdd:PRK11776  80 PTRELADQVAKEIRRLARFIPNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  251 EADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKrEEETLDTIKQYYVICnSKEEKFQ 330
Cdd:PRK11776 155 EADRML-DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEV-SPDERLP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  331 ALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQV 410
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  411 SVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAINMADSKfSMNTLNRIQDHFNKKIEKLDTDDLD 480
Cdd:PRK11776 312 EAVINYELA------RDPEVHVHRIGRTGRAGSKGLALSLVAPE-EMQRANAIEDYLGRKLNWEPLPSLS 374
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 101-448 5.33e-61

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 210.47  E-value: 5.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTY 180
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  181 ELALQTGKVIEQMGKHYPEVQLVYAIRGNKLE---RGAKLQEQIVIGTPGTVLDWCqKLKFIDPKKIKVFVLDEADVMIa 257
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  258 TQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQ-YYVICNSKeeKFQALCNIY 336
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  337 GAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINF 416
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320

                        330       340       350
                 ....*....|....*....|....*....|..
gi 27545267  417 DLPVdkdgnpDNETYLHRIGRTGRFGKRGLAI 448
Cdd:PRK11634 321 DIPM------DSESYVHRIGRTGRAGRAGRAL 346
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 102-472 9.50e-58

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 198.21  E-value: 9.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHV----DTENKW---PECL 174
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLlqtpPPKERYmgePRAL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  175 CVCPTYELALQTGKVIEQMGKhYPEVQLVYAIRGNKLERGAKLQEQ----IVIGTPGTVLDWCQKlKFIDPKKIKVFVLD 250
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLD 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  251 EADVMIaTQGHQDQSVRIQRMLPKTC--QMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQY-YVIcnSKEE 327
Cdd:PRK01297 245 EADRML-DMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHvYAV--AGSD 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  328 KFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDV 407
Cdd:PRK01297 322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27545267  408 EQVSVVINFDLPVDkdgnPDNetYLHRIGRTGRFGKRGLAINMA--DSKFSmntLNRIQDHFNKKIE 472
Cdd:PRK01297 402 DGISHVINFTLPED----PDD--YVHRIGRTGRAGASGVSISFAgeDDAFQ---LPEIEELLGRKIS 459
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 100-479 2.31e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 185.17  E-value: 2.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  100 KSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLA----MLSHVDTENK---WPE 172
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRkvnQPR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  173 CLCVCPTYELALQTGKVIEQMGKHYP-EVQLVYAIRG-----NKLERGAklqeQIVIGTPGTVLDWCqKLKFIDPKKIKV 246
Cdd:PRK04837  86 ALIMAPTRELAVQIHADAEPLAQATGlKLGLAYGGDGydkqlKVLESGV----DILIGTTGRLIDYA-KQNHINLGAIQV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  247 FVLDEADVMIATQGHQDQSVRIQRMlPKTCQML--LFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQ--YYvic 322
Cdd:PRK04837 161 VVLDEADRMFDLGFIKDIRWLFRRM-PPANQRLnmLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY--- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  323 NSKEEKFQALcniygaITIAQ------AMIFCHTR----KTAGWLAGElsreGHQVALLSGEMQVEQRAAVIERFRDGKE 392
Cdd:PRK04837 237 PSNEEKMRLL------QTLIEeewpdrAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDL 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  393 KVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAINMADSKFSMNtLNRIQDHFNKKI- 471
Cdd:PRK04837 307 DILVATDVAARGLHIPAVTHVFNYDLP------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSIp 379


                 ....*....
gi 27545267  472 -EKLDTDDL 479
Cdd:PRK04837 380 vSKYDSDAL 388
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 95-471 4.35e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 187.85  E-value: 4.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   95 PLYSVkSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLaePPQNLIAQSQSRTGKTAAFVLAMLSH-------VDTE 167
Cdd:PRK04537   5 PLTDL-TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVAL--PGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  168 NKWPECLCVCPTYELALQTGKVIEQMGKHYP-EVQLVYAirGNKLERGAKLQEQ---IVIGTPGTVLDWCQKLKFIDPKK 243
Cdd:PRK04537  82 PEDPRALILAPTRELAIQIHKDAVKFGADLGlRFALVYG--GVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVSLHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  244 IKVFVLDEADVMIATQGHQDQSVRIQRMlPKTC--QMLLFSATFEETVWNFAKRIVPDPNiiKLKREEETLDTIK-QYYV 320
Cdd:PRK04537 160 CEICVLDEADRMFDLGFIKDIRFLLRRM-PERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARvRQRI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  321 ICNSKEEKFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNV 400
Cdd:PRK04537 237 YFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27545267  401 CARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINMADSKFSMnTLNRIQDHFNKKI 471
Cdd:PRK04537 317 AARGLHIDGVKYVYNYDLPFDA------EDYVHRIGRTARLGEEGDAISFACERYAM-SLPDIEAYIEQKI 380
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 315-450 8.48e-53

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: 174.23  E-value: 8.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 315 IKQYYVICNSKEEKFQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKV 394
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267 395 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAINM 450
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITF 130
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 101-450 9.92e-49

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 173.84  E-value: 9.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPE------CL 174
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  175 CVCPTYELALQTGKVIEQMGKHYPEVQLVY--AIRGN----KLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFV 248
Cdd:PRK10590  80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVfgGVSINpqmmKLRGGV----DVLVATPGRLLDLEHQ-NAVKLDQVEILV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  249 LDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKLKREEETLDTIKQYyVICNSKEEK 328
Cdd:PRK10590 155 LDEADRML-DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  329 FQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVE 408
Cdd:PRK10590 233 RELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 27545267  409 QVSVVINFDLP-VDKDgnpdnetYLHRIGRTGRFGKRGLAINM 450
Cdd:PRK10590 313 ELPHVVNYELPnVPED-------YVHRIGRTGRAAATGEALSL 348
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 111-304 1.82e-48

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: 165.31  E-value: 1.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKW----PECLCVCPTYELALQT 186
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 187 GKVIEQMGKHYP-EVQLVYAirGNKLERGAKLQE---QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIaTQGHQ 262
Cdd:cd00268  79 AEVARKLGKGTGlKVAAIYG--GAPIKKQIEALKkgpDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML-DMGFE 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27545267 263 DQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd00268 155 EDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 102-300 1.36e-45

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: 157.84  E-value: 1.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYE 181
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 182 LALQTGKVIEQMGKHyPEVQLVYAIRGNKLERGA-KLQE--QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIaT 258
Cdd:cd17940  79 LALQTSQVCKELGKH-MGVKVMVTTGGTSLRDDImRLYQtvHVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADKLL-S 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27545267 259 QGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 102-300 7.88e-44

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: 153.37  E-value: 7.88e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQLLQGVYAMGFNRPSKIQETA-LPMMLAeppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTY 180
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 181 ELALQTGKVIEQMGKhYPEVQLVYAIRG-------NKLERGAklqeQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEAD 253
Cdd:cd18046  78 ELAQQIQKVVMALGD-YMGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEAD 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27545267 254 VMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd18046 152 EML-SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 104-303 1.04e-42

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: 150.17  E-value: 1.04e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 104 ELRLKPQLLQGVYAMGFNRPSKIQETA-LPMMLAEppqNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYEL 182
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTREL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 183 ALQTGKVIEQMGKhYPEVQLVYAIRGNKL-ERGAKLQE--QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIaTQ 259
Cdd:cd17939  78 AQQIQKVVKALGD-YMGVKVHACIGGTSVrEDRRKLQYgpHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SR 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27545267 260 GHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17939 155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 102-303 5.41e-39

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 140.30  E-value: 5.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYE 181
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKG--RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 182 LALQTGKVIEQMGkHYPEVQLVYAIRGNKLERG-AKLQ--EQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIaT 258
Cdd:cd18045  79 LAVQIQKVLLALG-DYMNVQCHACIGGTSVGDDiRKLDygQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEML-N 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27545267 259 QGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
PTZ00110 PTZ00110
helicase; Provisional
 99-487 2.42e-37

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 144.15  E-value: 2.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   99 VKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE-----NKWPEC 173
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHINAQpllryGDGPIV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  174 LCVCPTYELALQTGKVIEQMGKHY-----------PEVQLVYAIRgnkleRGAklqeQIVIGTPGTVLDWCQKlKFIDPK 242
Cdd:PTZ00110 207 LVLAPTRELAEQIREQCNKFGASSkirntvayggvPKRGQIYALR-----RGV----EILIACPGRLIDFLES-NVTNLR 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  243 KIKVFVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFA----KRIVPDPNI--IKLKreeeTLDTIK 316
Cdd:PTZ00110 277 RVTYLVLDEADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLArdlcKEEPVHVNVgsLDLT----ACHNIK 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  317 QYYVICNSKEEKFQaLCNIYGAITI--AQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKV 394
Cdd:PTZ00110 352 QEVFVVEEHEKRGK-LKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  395 LVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDNETYLHRIGRTGRFGKRGLAINM--ADSKFSMNTLNRIQDHFNKKIE 472
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFP------NQIEDYVHRIGRTGRAGAKGASYTFltPDKYRLARDLVKVLREAKQPVP 504

                        410
                 ....*....|....*
gi 27545267  473 KldtddldEIEKIAN 487
Cdd:PTZ00110 505 P-------ELEKLSN 512
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 75-448 5.23e-37

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 142.62  E-value: 5.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   75 RSNLVNTTNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTA 154
Cdd:PLN00206  99 QAELLRRKLEIHVKGEAVPPP---ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  155 AFVLAMLSHVDT-------ENKWPECLCVCPTYELALQTGKVIEQMGKHYP-EVQLVyaIRGNKLERGAKLQEQ---IVI 223
Cdd:PLN00206 174 SFLVPIISRCCTirsghpsEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPfKTALV--VGGDAMPQQLYRIQQgveLIV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  224 GTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSVRIQRMLPkTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:PLN00206 252 GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML-ERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILI 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  304 KLKREEETLDTIKQYYVICNSKEEKfQALCNIYGAITIAQ--AMIFCHTRKTAGWLAGELSR-EGHQVALLSGEMQVEQR 380
Cdd:PLN00206 329 SIGNPNRPNKAVKQLAIWVETKQKK-QKLFDILKSKQHFKppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKER 407

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27545267  381 AAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgNPDNEtYLHRIGRTGRFGKRGLAI 448
Cdd:PLN00206 408 REVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP-----NTIKE-YIHQIGRASRMGEKGTAI 469
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 111-304 2.25e-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: 130.08  E-value: 2.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYELALQTGKVI 190
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 191 EQMGKHYPEVQLVYAIRGNKLERG-AKLQE-QIVIGTPGTVldwCQ--KLKFIDPKKIKVFVLDEAD-VMIATqgHQDQS 265
Cdd:cd17943  79 KKIGKKLEGLKCEVFIGGTPVKEDkKKLKGcHIAVGTPGRI---KQliELGALNVSHVRLFVLDEADkLMEGS--FQKDV 153

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27545267 266 VRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEXDc smart00487
DEAD-like helicases superfamily;
115-318 2.02e-34

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 127.99  E-value: 2.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    115 VYAMGFNRPSKIQETALPMMLAEPpQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPeCLCVCPTYELALQTGKVIEQMG 194
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    195 KHYPEVQLVYAIRGNKLERGAKLQE---QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSVRIQRM 271
Cdd:smart00487  79 PSLGLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 27545267    272 LPKTCQMLLFSATFEETVWNFAKRIVPDPniIKLKREEETLDTIKQY 318
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 124-289 1.67e-33

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: 124.28  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   124 SKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYELALQTGKVIEQMGKHYpEVQLV 203
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   204 YAIRGN--KLERGAKLQEQIVIGTPGTVLDWCQKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLF 281
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154


                  ....*...
gi 27545267   282 SATFEETV 289
Cdd:pfam00270 155 SATLPRNL 162
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 101-304 2.01e-32

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: 122.80  E-value: 2.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAepPQNLIAQSQSRTGKTAAFVLAMLSHVDTE--NKWPECLCVCP 178
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 179 TYELALQTGKVIEQMGKhYPEVQLVYAIRGNKLERG-AKLQEQ--IVIGTPGTVLDWCQKLKFiDPKKIKVFVLDEADVM 255
Cdd:cd17959  80 TRELALQTLKVTKELGK-FTDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27545267 256 IAtQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd17959 158 FE-MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 101-300 3.34e-32

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 122.07  E-value: 3.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPM-MLAEppqNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPT 179
Cdd:cd17950   3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQaILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 180 YELALQTGKVIEQMGKHYPEV--QLVY---AIRGNKlERGAKLQEQIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADV 254
Cdd:cd17950  80 RELAFQISNEYERFSKYMPNVktAVFFggvPIKKDI-EVLKNKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDK 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27545267 255 MIATQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17950 158 MLEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 327-442 1.00e-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: 117.70  E-value: 1.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   327 EKFQALCNIYGAITIAQAMIFCHTRKTA--GWLageLSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARG 404
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27545267   405 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 442
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 111-294 6.84e-30

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: 115.43  E-value: 6.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLS---HVDTENKWPECLCVCPTYELALQTG 187
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILErllYRPKKKAATRVLVLVPTRELAMQCF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 188 KVIEQMGKhYPEVQLVYAIRGNKL---ERGAKLQEQIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADVMIaTQGHQDQ 264
Cdd:cd17947  79 SVLQQLAQ-FTDITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADE 156

                       170       180       190
                ....*....|....*....|....*....|
gi 27545267 265 SVRIQRMLPKTCQMLLFSATFEETVWNFAK 294
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAK 186
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 107-305 3.42e-29

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: 113.83  E-value: 3.42e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 107 LKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHV------DTENKWPECLCVCPTY 180
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 181 ELALQTGKVIEQMGKHY-PEVQLVyAIRGNKLERGAK--LQEQ--IVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADVM 255
Cdd:cd17961  79 ELAQQVSKVLEQLTAYCrKDVRVV-NLSASSSDSVQRalLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLV 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27545267 256 IaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNIIKL 305
Cdd:cd17961 158 L-SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 85-293 7.99e-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: 108.90  E-value: 7.99e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  85 VEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHV 164
Cdd:cd18052  31 VEVTGRNPPPA---ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGM 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 165 DTEN---------KWPECLCVCPTYELALQTGKVIEQMGKH--------YPEVQLVYAIRgnKLERGAklqeQIVIGTPG 227
Cdd:cd18052 106 MKEGltassfsevQEPQALIVAPTRELANQIFLEARKFSYGtcirpvvvYGGVSVGHQIR--QIEKGC----HILVATPG 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27545267 228 TVLDWCQKLKfIDPKKIKVFVLDEADVMIATQGHQDqsvrIQR------MLPKTC-QMLLFSATFEETVWNFA 293
Cdd:cd18052 180 RLLDFIGRGK-ISLSKLKYLILDEADRMLDMGFGPE----IRKlvsepgMPSKEDrQTLMFSATFPEEIQRLA 247
HELICc smart00490
helicase superfamily c-terminal domain;
356-442 2.52e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.90  E-value: 2.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267    356 WLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 435
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75


                   ....*..
gi 27545267    436 GRTGRFG 442
Cdd:smart00490  76 GRAGRAG 82
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 102-300 5.79e-26

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 104.71  E-value: 5.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVdtenkwpECLCVCPTYE 181
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 182 LALQTGKVIEQMGKHY--PEVQLVYAIRGNKLERGAKLQEQ---IVIGTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMI 256
Cdd:cd17938  72 LAEQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 27545267 257 aTQGHQDQSVRIQRMLPKTC------QMLLFSATFEET-VWNFAKRIVPDP 300
Cdd:cd17938 151 -SQGNLETINRIYNRIPKITsdgkrlQVIVCSATLHSFeVKKLADKIMHFP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 101-284 2.69e-25

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: 102.78  E-value: 2.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTY 180
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 181 ELALQTGKVIEQMGKhypevqlVYAIRGNKLERGAKLQEQ---------IVIGTPGTVLDWCQKLKFIDPKKIKVFVLDE 251
Cdd:cd17954  79 ELAQQISEQFEALGS-------SIGLKSAVLVGGMDMMAQaialakkphVIVATPGRLVDHLENTKGFSLKSLKFLVMDE 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27545267 252 ADVMIatqgHQDQSVRIQRML---PKTCQMLLFSAT 284
Cdd:cd17954 152 ADRLL----NMDFEPEIDKILkviPRERTTYLFSAT 183
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 101-295 3.41e-25

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 103.34  E-value: 3.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 101 SFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHV----------DTENKW 170
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 171 PECLCVCPTYELALQTGKVIEQMGKHYP-EVQLVY---AIRG--NKLERGAKlqeqIVIGTPGTVLDWCQKLKfIDPKKI 244
Cdd:cd17967  79 PSALILAPTRELAIQIYEEARKFSYRSGvRSVVVYggaDVVHqqLQLLRGCD----ILVATPGRLVDFIERGR-ISLSSI 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27545267 245 KVFVLDEADVMIaTQGHQDQSVRI---QRMLPKTC-QMLLFSATFEETVWNFAKR 295
Cdd:cd17967 154 KFLVLDEADRML-DMGFEPQIRKIvehPDMPPKGErQTLMFSATFPREIQRLAAD 207
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 111-303 5.38e-25

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 101.86  E-value: 5.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPECLCVCPTYELALQTGKVI 190
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 191 EQMGKHYPEVQLVYAIRGNKLE-RGAKLQE--QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSVR 267
Cdd:cd17962  79 KELMKGLPPMKTALLVGGLPLPpQLYRLQQgvKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVLD 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27545267 268 IQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 102-300 5.88e-24

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: 99.22  E-value: 5.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLshvdteNKWPE------CLC 175
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPIL------QRLSEdpygifALV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 176 VCPTYELALQtgkVIEQM---GKHyPEVQLVYAIRGNKLERGAKLQEQ---IVIGTPGTVLDW---CQKLKFiDPKKIKV 246
Cdd:cd17955  73 LTPTRELAYQ---IAEQFralGAP-LGLRCCVIVGGMDMVKQALELSKrphIVVATPGRLADHlrsSDDTTK-VLSRVKF 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27545267 247 FVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17955 148 LVLDEADRLL-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 107-303 7.22e-24

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: 99.19  E-value: 7.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 107 LKPQLLQGVYAMGFNRPSKIQETALPMMLaEPPQNLIAQSQSRTGKTAAFVLAMLSHV-----DTENKWPECLCVCPTYE 181
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 182 LALQTGKVIEQMGKHYPEVQLVYAIRGNK----LERGAKLQEQIVIGTPGTVLDWCQKLKFIDP-KKIKVFVLDEADVMI 256
Cdd:cd17964  80 LALQIAAEAKKLLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGRLIDHLENPGVAKAfTDLDYLVLDEADRLL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27545267 257 aTQGHQDQSVRIQRMLPKTC----QMLLFSATFEETVWNFAKRIV-PDPNII 303
Cdd:cd17964 160 -DMGFRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 112-303 2.73e-23

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: 97.36  E-value: 2.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 112 LQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTEnKWPE-----CLCVCPTYELALQT 186
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLYRE-RWTPedglgALIISPTRELAMQI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 187 GKVIEQMGKHYP-EVQLVYAIRGNKLERGAKLQEQIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADvMIATQGHQDQS 265
Cdd:cd17941  79 FEVLRKVGKYHSfSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKETL 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27545267 266 VRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 111-300 2.96e-22

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 94.40  E-value: 2.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE-----NKWPECLCVCPTYELALQ 185
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHIMDQrelekGEGPIAVIVAPTRELAQQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 186 TGKVIEQMGKHYP-EVQLVYAiRGNKLERGAKLQE--QIVIGTPGTVLDWCqKLKFIDPKKIKVFVLDEADVMIaTQGHQ 262
Cdd:cd17952  79 IYLEAKKFGKAYNlRVVAVYG-GGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFE 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27545267 263 DQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17952 156 YQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 111-303 1.75e-21

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: 92.40  E-value: 1.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSH-VDTENKWPEC-------LCVCPTYEL 182
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLIMFaLEQEKKLPFIkgegpygLIVCPSREL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 183 ALQTGKVIEQMGKH-----YPEVQLVYAIRGNKLERGAKLQEQ---IVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEADV 254
Cdd:cd17951  79 ARQTHEVIEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADR 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27545267 255 MIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17951 158 MI-DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 111-284 5.88e-21

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: 90.71  E-value: 5.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHV---DTENKWPE--CLCVCPTYELALQ 185
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 186 TGKVIEQMGKHY-PEVQLVYAIRGNKLERG-AKLQE---QIVIGTPGTVLDWCQKLKF-IDPKKIKVFVLDEADVMIaTQ 259
Cdd:cd17960  79 IYEVLQSFLEHHlPKLKCQLLIGGTNVEEDvKKFKRngpNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLL-DL 157

                       170       180
                ....*....|....*....|....*
gi 27545267 260 GHQDQSVRIQRMLPKTCQMLLFSAT 284
Cdd:cd17960 158 GFEADLNRILSKLPKQRRTGLFSAT 182
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 111-303 1.07e-19

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 87.76  E-value: 1.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAepPQNLIAQSQSRTGKTAAFVLAMLSHVD--------TENKWPECLCVCPTYEL 182
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTREL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 183 ALQTGKVIEQMGKHYPeVQLVYAIRGNKLERGA-KLQE--QIVIGTPGTVLDwCQKLKFIDPKKIKVFVLDEADVMIaTQ 259
Cdd:cd17945  79 AQQIEEETQKFAKPLG-IRVVSIVGGHSIEEQAfSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DM 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27545267 260 GHQDQSVRIQRMLPKTC--------------------QMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17945 156 GFEPQVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 111-300 1.87e-18

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: 83.41  E-value: 1.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEPpqNLIAQSQSRTGKTAAFVLAMLSHV--DTENKWPECLCVCPTYELALQTGK 188
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 189 VIEQMGKHYP-EVQLVYAIRGNKLERGAKLQEQ--IVIGTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMIATqGHQDQS 265
Cdd:cd17957  79 ELLKLSKGTGlRIVLLSKSLEAKAKDGPKSITKydILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFREQT 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27545267 266 VRIQRMLPKTC-QMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17957 157 DEILAACTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 112-294 2.04e-18

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 83.18  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 112 LQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKWPE----CLCVCPTYELALQT- 186
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 187 GKVIEQMGKHYPEVQLVyaIRG-NKLERGAKLQE--QIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADvMIATQGHQD 263
Cdd:cd17942  80 GVAKELLKYHSQTFGIV--IGGaNRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEE 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 27545267 264 QSVRIQRMLPKTCQMLLFSATFEETVWNFAK 294
Cdd:cd17942 157 EMRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 111-303 2.04e-18

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: 83.28  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE------NKWPECLCVCPTYELAL 184
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqRNGPGVLVLTPTRELAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 185 QtgkvIEQMGKHYP----EVQLVYAiRGNKLERGAKLQE--QIVIGTPGTVLDwCQKLKFIDPKKIKVFVLDEADVMIaT 258
Cdd:cd17958  79 Q----IEAECSKYSykglKSVCVYG-GGNRNEQIEDLSKgvDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-D 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27545267 259 QGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDPNII 303
Cdd:cd17958 152 MGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 99-300 2.44e-18

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: 83.58  E-value: 2.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  99 VKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVD-----TENKWPEC 173
Cdd:cd17953  11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIKdqrpvKPGEGPIG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 174 LCVCPTYELALQTGKVIEQMGKHYP-EVQLVYAIRGNK-----LERGAklqeQIVIGTPGTVLDW--CQKLKFIDPKKIK 245
Cdd:cd17953  89 LIMAPTRELALQIYVECKKFSKALGlRVVCVYGGSGISeqiaeLKRGA----EIVVCTPGRMIDIltANNGRVTNLRRVT 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27545267 246 VFVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17953 165 YVVLDEADRMF-DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 118-304 1.07e-17

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: 81.48  E-value: 1.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 118 MGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDT-ENKW-----PECLCVCPTYELALQTGKVIE 191
Cdd:cd17949   9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSlEPRVdrsdgTLALVLVPTRELALQIYEVLE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 192 QMGKHYPEVQLVYAIRGNK-------LERGAklqeQIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADVMIaTQGHQDQ 264
Cdd:cd17949  87 KLLKPFHWIVPGYLIGGEKrksekarLRKGV----NILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEKD 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27545267 265 SVRIQRML-------------PKTCQMLLFSATFEETVWNFAKRIVPDPNIIK 304
Cdd:cd17949 162 ITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 111-285 1.48e-17

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: 81.90  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEPpQNLIAQSQSRTGKTAAFVLAMLSH---------VDTENKWPECLCVCPTYE 181
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPILERllsqkssngVGGKQKPLRALILTPTRE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 182 LALQTGKVIEQMGKhYPEVQLVYAIRG---NKLERGAKLQEQIVIGTPGTVLDWCQK----LKFIdpKKIKVFVLDEADV 254
Cdd:cd17946  80 LAVQVKDHLKAIAK-YTNIKIASIVGGlavQKQERLLKKRPEIVVATPGRLWELIQEgnehLANL--KSLRFLVLDEADR 156

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27545267 255 MIaTQGHQDQSVRIQRMLPKTC-------QMLLFSATF 285
Cdd:cd17946 157 ML-EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 111-300 3.98e-17

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


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 79.72  E-value: 3.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTENKW-----PECLCVCPTYELALQ 185
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHINAQPPLergdgPIVLVLAPTRELAQQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 186 TGKVIEQMGKH-YPEVQLVY--AIRGNK---LERGAklqeQIVIGTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMIaTQ 259
Cdd:cd17966  79 IQQEANKFGGSsRLRNTCVYggAPKGPQirdLRRGV----EICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML-DM 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27545267 260 GHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPDP 300
Cdd:cd17966 153 GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 98-285 2.41e-16

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: 78.54  E-value: 2.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  98 SVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE---------- 167
Cdd:cd18051  19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpses 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 168 ------NKWPECLCVCPTYELALQtgkVIEQMGKH-Y-----PEVqlVYA---IRGN--KLERGAKLqeqiVIGTPGTVL 230
Cdd:cd18051  97 gyygrrKQYPLALVLAPTRELASQ---IYDEARKFaYrsrvrPCV--VYGgadIGQQmrDLERGCHL----LVATPGRLV 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27545267 231 DWCQKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSVRI--QRMLPKTC--QMLLFSATF 285
Cdd:cd18051 168 DMLERGK-IGLDYCKYLVLDEADRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 82-299 5.51e-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: 71.19  E-value: 5.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  82 TNQVEVLQRDPSSPlysVKSFEELRLKPQLLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAML 161
Cdd:cd18049   9 SKEITVRGHNCPKP---VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 162 SHVDTE-----NKWPECLCVCPTYELALQTGKVIEQMGKHYP-EVQLVY--AIRGNK---LERGAklqeQIVIGTPGTVL 230
Cdd:cd18049  84 VHINHQpflerGDGPICLVLAPTRELAQQVQQVAAEYGRACRlKSTCIYggAPKGPQirdLERGV----EICIATPGRLI 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27545267 231 DWCQKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSVRIQRMLPKTCQMLLFSATFEETVWNFAKRIVPD 299
Cdd:cd18049 160 DFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
293-443 6.59e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.38  E-value: 6.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 293 AKRIVPDPNIIKLKREEETLDtikqyyvICNSKEEK-FQALCNIYGAITIAQAMIFCHTRKTAGWLAGELSREGHQVALL 371
Cdd:COG1111 311 SKRLVSDPRFRKAMRLAEEAD-------IEHPKLSKlREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRF 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 372 SGE--------MQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIGRTGRFGK 443
Cdd:COG1111 384 VGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKGRTGRKRE 457
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 120-299 7.79e-14

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 71.58  E-value: 7.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 120 FNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAMLSHVDTE-----NKWPECLCVCPTYELALQTGKVIEQMG 194
Cdd:cd18050  82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHINHQpylerGDGPICLVLAPTRELAQQVQQVADDYG 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 195 KHYP-EVQLVY--AIRGNK---LERGAklqeQIVIGTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSVRI 268
Cdd:cd18050 160 KSSRlKSTCIYggAPKGPQirdLERGV----EICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRKI 233

                       170       180       190
                ....*....|....*....|....*....|.
gi 27545267 269 QRMLPKTCQMLLFSATFEETVWNFAKRIVPD 299
Cdd:cd18050 234 VDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
150-485 1.41e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 72.75  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 150 TGKT--AAFVLAMLSHVDTenkwpeCLCVCPTYELAlqtgkviEQMGKHYPEVQLVYAIRGNKLERGAklqeQIVIGTPG 227
Cdd:COG1061 111 TGKTvlALALAAELLRGKR------VLVLVPRRELL-------EQWAEELRRFLGDPLAGGGKKDSDA----PITVATYQ 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 228 TVLDWCQKLKFIDpkKIKVFVLDEAdvmiatqgHQ---DQSVRIQRMLPKTCqMLLFSAT-------------FEETVWN 291
Cdd:COG1061 174 SLARRAHLDELGD--RFGLVIIDEA--------HHagaPSYRRILEAFPAAY-RLGLTATpfrsdgreillflFDGIVYE 242

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 292 F------AKRIVPDPNII----KLKREEETLDTIKQ--YYVICNSKEEKFQALCNIYGAIT-IAQAMIFCHTRKTAGWLA 358
Cdd:COG1061 243 YslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEALA 322

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 359 GELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdGNPDneTYLHRIGR- 437
Cdd:COG1061 323 ELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT---GSPR--EFIQRLGRg 396

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 27545267 438 --TGRFGKRGLAINMADSKFSM--NTLNRIQDHFNKKIEKLDTDDLDEIEKI 485
Cdd:COG1061 397 lrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 346-442 1.05e-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: 65.19  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 346 IFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 423
Cdd:cd18793  32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107

                        90
                ....*....|....*....
gi 27545267 424 GNPDNEtyLHRIGRTGRFG 442
Cdd:cd18793 108 WNPAVE--EQAIDRAHRIG 124
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 140-295 1.41e-11

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: 63.71  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 140 QNLIAQSQSRTGKTAAFVLAMLSHVDTEN------KWPECLCVCPTYELALQTGKVIEQMGKHY---------PEVQLVY 204
Cdd:cd17944  28 KDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLsvacfyggtPYQQQIF 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 205 AIRGNKlergaklqeQIVIGTPGTVLDWCQKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSVRIQRMLPKTCQMLL 280
Cdd:cd17944 108 AIRNGI---------DILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLL 177

                       170
                ....*....|....*
gi 27545267 281 FSATFEETVWNFAKR 295
Cdd:cd17944 178 FSATCPDWVYNVAKK 192
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 141-284 4.84e-11

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: 60.88  E-value: 4.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 141 NLIAQSQSRTGKTAAFVLAMLSHVDTenKWPECLCVCPTYELALQTGKVIEQMGKHYPEVQLVYAIRgNKLERGAK--LQ 218
Cdd:cd00046   3 NVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGS-SAEEREKNklGD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27545267 219 EQIVIGTPGTVLDWCQKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSVRIQRMLPKTCQMLLFSAT 284
Cdd:cd00046  80 ADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 346-442 4.82e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.78  E-value: 4.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 346 IFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 423
Cdd:COG0553 554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630

                        90
                ....*....|....*....
gi 27545267 424 gNPDNEtyLHRIGRTGRFG 442
Cdd:COG0553 631 -NPAVE--EQAIDRAHRIG 646
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 325-419 5.20e-10

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 57.60  E-value: 5.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 325 KEEKFQALCNI----YGAITIAQAMIFCHTRKTA----GWLAGELSRE---------GHQVALLSGEMQVEQRA--AVIE 385
Cdd:cd18802   5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAvvlsRLLKEHPSTLafircgfliGRGNSSQRKRSLMTQRKqkETLD 84

                        90       100       110
                ....*....|....*....|....*....|....
gi 27545267 386 RFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLP 419
Cdd:cd18802  85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 111-284 1.69e-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: 58.03  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLaePPQNLIAQSQSR---------TGKTAAFVL----AMLSHVDTENKwpeCLCVC 177
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLL--PSSKSTPPYRPGdlcvsaptgSGKTLAYVLpivqALSKRVVPRLR---ALIVV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 178 PTYELALQTGKVIEQMGKH--------------YPEVQLVYAIRGNKLERGAklqeQIVIGTPGTVLDWCQKLKFIDPKK 243
Cdd:cd17956  76 PTKELVQQVYKVFESLCKGtglkvvslsgqksfKKEQKLLLVDTSGRYLSRV----DILVATPGRLVDHLNSTPGFTLKH 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 244 IKVFVLDEAD-------------VMIATQGHQDQSVR------IQRMLPKTCQMLLFSAT 284
Cdd:cd17956 152 LRFLVIDEADrllnqsfqdwletVMKALGRPTAPDLGsfgdanLLERSVRPLQKLLFSAT 211
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 346-443 2.81e-09

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 55.29  E-value: 2.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 346 IFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 425
Cdd:cd18794  35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108

                        90
                ....*....|....*...
gi 27545267 426 PDNETYLHRIGRTGRFGK 443
Cdd:cd18794 109 KSMESYYQESGRAGRDGL 126
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 111-289 8.24e-09

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 55.84  E-value: 8.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 111 LLQGVYAMGFNRPSKIQETALPMMLAEppQNLIAQSQSRTGKTAAFVLAML------SHVDT--ENKwPECLCVCPTYEL 182
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIqrllryKLLAEgpFNA-PRGLVITPSREL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 183 ALQTGKVIEQMGKHYP-EVQLVYAIRGNKLERGAKLQE-QIVIGTPGTVLdwcqKL---KFIDPKKIKVFVLDEADVMI- 256
Cdd:cd17948  78 AEQIGSVAQSLTEGLGlKVKVITGGRTKRQIRNPHFEEvDILVATPGALS----KLltsRIYSLEQLRHLVLDEADTLLd 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27545267 257 ------------ATQGHQDQSVRIQRMLPKTcQMLLFSATFEETV 289
Cdd:cd17948 154 dsfneklshflrRFPLASRRSENTDGLDPGT-QLVLVSATMPSGV 197
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
346-448 1.21e-08

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.07  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 346 IFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 423
Cdd:COG0514 235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308

                        90       100
                ....*....|....*....|....*
gi 27545267 424 GNPdnETYLHRIGRTGRFGKRGLAI 448
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 ...
 344-440 1.69e-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: 53.13  E-value: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 344 AMIFCHTRKTAGWLAGELSREGHQV-----------ALLSGEMQVEQRAaVIERFRDGKEKVLVTTNVCARGIDVEQVSV 412
Cdd:cd18801  33 VIIFSEFRDSAEEIVNFLSKIRPGIratrfigqasgKSSKGMSQKEQKE-VIEQFRKGGYNVLVATSIGEEGLDIGEVDL 111

                        90       100
                ....*....|....*....|....*...
gi 27545267 413 VINFdlpvdkDGNPDNETYLHRIGRTGR 440
Cdd:cd18801 112 IICY------DASPSPIRMIQRMGRTGR 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 393-445 1.77e-06

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.77  E-value: 1.77e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 27545267 393 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 445
Cdd:cd18785  24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 342-448 1.88e-06

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: 50.60  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 342 AQAMIFCHTRKTAGWLAGELSRE------GHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVIN 415
Cdd:COG1205 289 LRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368

                        90       100       110
                ....*....|....*....|....*....|....
gi 27545267 416 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAI 448
Cdd:COG1205 369 -------AGYPGTRAsFWQQAGRAGRRGQDSLVV 395
PRK13766 PRK13766
Hef nuclease; Provisional
 293-440 2.52e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.26  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  293 AKRIVPDPNIIKLKREEETLDtikqyyvICNSKEEKfqaLCNIYGAITIAQ----AMIFCHTRKTAGWLAGELSREGHQV 368
Cdd:PRK13766 323 SKRLVEDPRFRKAVRKAKELD-------IEHPKLEK---LREIVKEQLGKNpdsrIIVFTQYRDTAEKIVDLLEKEGIKA 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  369 ALLSGE--------M-QVEQRAAvIERFRDGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETYLHRIGRTG 439
Cdd:PRK13766 393 VRFVGQaskdgdkgMsQKEQIEI-LDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRSIQRKGRTG 465


                 .
gi 27545267  440 R 440
Cdd:PRK13766 466 R 466
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
 350-470 6.94e-06

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 46.47  E-value: 6.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 350 TRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 429
Cdd:cd18790  36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27545267 430 TYL-HRIGRTGRfGKRGLAINMADS-----KFSMNTLNR---IQDHFNKK 470
Cdd:cd18790 114 TSLiQTIGRAAR-NVNGKVILYADKitdsmQKAIEETERrreIQMEYNEE 162
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 343-452 1.05e-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: 45.62  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 343 QAMIFCHTRK----TAGWLAGelsreghqVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDL 418
Cdd:cd18795  45 PVLVFCSSRKecekTAKDLAG--------IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQ 116

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 27545267 419 PVDKDGN---PDNEtYLHRIGRTGR--FGKRGLAINMAD 452
Cdd:cd18795 117 RYDGKGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 337-448 1.15e-05

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 45.33  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 337 GAITIAqamiFCHTRKTAGWLAGELSREGHQVALLSGEMQV-------EQRAAVIERFRDGKEKVLVTTNVCARGIDVEQ 409
Cdd:cd18797  35 GVKTIV----FCRSRKLAELLLRYLKARLVEEGPLASKVASyragylaEDRREIEAELFNGELLGVVATNALELGIDIGG 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 27545267 410 VSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAI 448
Cdd:cd18797 111 LDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 140-252 2.07e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 45.34  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 140 QNLIAQSQSRTGKT--AAFVLAMLSHVDTENKWPECLCV--CPTYELALQTGKVIEQmgkHYP-EVQLVYAIRGNKLERG 214
Cdd:cd18034  17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVflVPTVPLVAQQAEAIRS---HTDlKVGEYSGEMGVDKWTK 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 27545267 215 AKLQE-----QIVIGTPGTVLDWCQKlKFIDPKKIKVFVLDEA 252
Cdd:cd18034  94 ERWKEelekyDVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 368-459 6.50e-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: 43.41  E-value: 6.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 368 VALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 446
Cdd:cd18792  63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136

                        90
                ....*....|...
gi 27545267 447 AINMADSKFSMNT 459
Cdd:cd18792 137 CYLLYPDPKKLTE 149
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 345-442 6.63e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 45.47  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  345 MIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 424
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317

                         90
                 ....*....|....*...
gi 27545267  425 npdnETYLHRIGRTGRFG 442
Cdd:PRK11057 318 ----ESYYQETGRAGRDG 331
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 357-464 8.33e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 45.14  E-value: 8.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267  357 LAGELSRE--GHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSV-VI----NFDLpvdkdgnpdne 429
Cdd:PRK10917 495 TYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVIenaeRFGL----------- 563

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 27545267  430 TYLH--RiGRTGRFGKRGLAINMADSKFSMNTLNRIQ 464
Cdd:PRK10917 564 AQLHqlR-GRVGRGAAQSYCVLLYKDPLSETARERLK 599
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 368-464 9.48e-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: 42.72  E-value: 9.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 368 VALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 446
Cdd:cd18811  64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137

                        90
                ....*....|....*...
gi 27545267 447 AINMADSKFSMNTLNRIQ 464
Cdd:cd18811 138 CLLVYKDPLTETAKQRLR 155
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 102-284 2.10e-04

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 42.75  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 102 FEELRLKPQ---------LLQGVYAMGFNRPSKIQETALPMML-------------AEPPQN--LIAqSQSRTGKTAAFV 157
Cdd:cd17965   1 FDQLKLLPSvreaiikeiLKGSNKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsnEEPKLEvfLLA-AETGSGKTLAYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 158 LAMLSHV-DTENKWPE----------------CLCVCPTYELALQTGKVIEQMgKHYpevqLVYAIRGNKLERGAKLQE- 219
Cdd:cd17965  80 APLLDYLkRQEQEPFEeaeeeyesakdtgrprSVILVPTHELVEQVYSVLKKL-SHT----VKLGIKTFSSGFGPSYQRl 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27545267 220 --------QIVIGTPGTVldwcQKLKFIDPK---KIKVFVLDEADVMIATQGHQDQSVRIQRMlPKTCQMLLFSAT 284
Cdd:cd17965 155 qlafkgriDILVTTPGKL----ASLAKSRPKilsRVTHLVVDEADTLFDRSFLQDTTSIIKRA-PKLKHLILCSAT 225
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
 342-414 2.18e-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: 43.71  E-value: 2.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27545267 342 AQAMIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVI 414
Cdd:COG4098 320 RQLLIFVPTIELLEQLVALLQKLFPEERIAGVHAEDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAV 392
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 345-444 1.15e-03

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 41.81  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267   345 MIFCHTRKTAGWLAGELSREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 424
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763

                          90       100
                  ....*....|....*....|
gi 27545267   425 npdnetYLHRIGRTGRFGKR 444
Cdd:PLN03137  764 ------YHQECGRAGRDGQR 777
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 346-440 1.99e-03

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: 38.78  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 346 IFCHTRKTAGWLAGEL------SREGHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFdlp 419
Cdd:cd18796  43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119

                        90       100
                ....*....|....*....|..
gi 27545267 420 vdkdGNPDNET-YLHRIGRTGR 440
Cdd:cd18796 120 ----GSPKSVArLLQRLGRSGH 137
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
360-464 2.73e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.42  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 360 ELSRE--GHQVALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSV-VI----NFDLpvdkdgnpdneTYL 432
Cdd:COG1200 496 ELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVIenaeRFGL-----------SQL 564

                        90       100       110
                ....*....|....*....|....*....|....
gi 27545267 433 H--RiGRTGRFGKRGLAINMADSKFSMNTLNRIQ 464
Cdd:COG1200 565 HqlR-GRVGRGSAQSYCLLLYDAPLSETARERLE 597
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 368-447 4.53e-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: 37.71  E-value: 4.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545267 368 VALLSGEMQVEQRAAVIERFRDGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 446
Cdd:cd18810  54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127


                .
gi 27545267 447 A 447
Cdd:cd18810 128 A 128
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH