NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|380503833|ref|NP_001244102|]
View 

ATP-dependent RNA helicase DDX19B isoform 3 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209184)

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

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 ...
1-187 1.13e-123

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 cd18047:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 205  Bit Score: 354.80  E-value: 1.13e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd18047   19 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 160
Cdd:cd18047   99 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 178
                        170       180
                 ....*....|....*....|....*..
gi 380503833 161 MLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd18047  179 MLLFSATFEDSVWKFAQKVVPDPNVIK 205
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
198-334 1.39e-52

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.77  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 198 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 277
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380503833 278 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 334
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
1-187 1.13e-123

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: 354.80  E-value: 1.13e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd18047   19 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 160
Cdd:cd18047   99 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 178
                        170       180
                 ....*....|....*....|....*..
gi 380503833 161 MLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd18047  179 MLLFSATFEDSVWKFAQKVVPDPNVIK 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-367 2.66e-117

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 346.36  E-value: 2.66e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANKYPQCLCLSPTYELALQTGKVIEQMGKF 79
Cdd:COG0513   20 LGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTRELALQVAEELRKLAKY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  80 YPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQ 152
Cdd:COG0513   98 LG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEADRML-DMGFIEDIERIL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 153 RMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCH 232
Cdd:COG0513  171 KLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCN 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 233 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnE 312
Cdd:COG0513  250 TKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP------E 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 380503833 313 TYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 367
Cdd:COG0513  324 DYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
2-360 2.00e-90

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 277.09  E-value: 2.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfYP 81
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  82 ELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRM 154
Cdd:PTZ00424 124 KVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKK 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 155 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTR 234
Cdd:PTZ00424 198 LPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTR 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 235 KTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETY 314
Cdd:PTZ00424 278 RKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ENY 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 380503833 315 LHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 360
Cdd:PTZ00424 352 IHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
198-334 1.39e-52

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.77  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 198 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 277
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380503833 278 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 334
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
7-172 3.54e-39

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 136.99  E-value: 3.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833    7 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 86
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   87 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 164
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 380503833  165 SATFEDSV 172
Cdd:pfam00270 155 SATLPRNL 162
DEXDc smart00487
DEAD-like helicases superfamily;
1-201 2.62e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 130.69  E-value: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833     1 MGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833    81 PELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPR 157
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 380503833   158 NCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 201
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
210-325 3.34e-32

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.93  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  210 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 287
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380503833  288 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 325
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
239-325 4.09e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.29  E-value: 4.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   239 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 318
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 380503833   319 GRTGRFG 325
Cdd:smart00490  76 GRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
174-326 1.08e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 69.37  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 174 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 247
Cdd:COG1111  309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 248 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 319
Cdd:COG1111  377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450

                 ....*..
gi 380503833 320 RTGRFGK 326
Cdd:COG1111  451 RTGRKRE 457
PRK13766 PRK13766
Hef nuclease; Provisional
174-323 8.61e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 174 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 242
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 243 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 314
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                 ....*....
gi 380503833 315 LHRIGRTGR 323
Cdd:PRK13766 458 IQRKGRTGR 466
 
Name Accession Description Interval E-value
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
1-187 1.13e-123

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: 354.80  E-value: 1.13e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd18047   19 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 160
Cdd:cd18047   99 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 178
                        170       180
                 ....*....|....*....|....*..
gi 380503833 161 MLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd18047  179 MLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
1-194 1.59e-123

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: 355.48  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd18048   36 MGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 160
Cdd:cd18048  116 VGIQVIYAIRGNRPGKGTDIEAQIVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVRVKRSMPKECQ 195
                        170       180       190
                 ....*....|....*....|....*....|....
gi 380503833 161 MLLFSATFEDSVWKFAQKVVPDPNVIKLKREEET 194
Cdd:cd18048  196 MLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
1-187 2.50e-120

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: 345.71  E-value: 2.50e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFy 80
Cdd:cd17963   12 MGFNKPSKIQETALPLILSDPPENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEVVEKMGKF- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQ 160
Cdd:cd17963   91 TGVKVALAVPGNDVPRGKKITAQIVIGTPGTVLDWLKK-RQLDLKKIKILVLDEADVMLDTQGHGDQSIRIKRMLPRNCQ 169
                        170       180
                 ....*....|....*....|....*..
gi 380503833 161 MLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd17963  170 ILLFSATFPDSVRKFAEKIAPNANTIK 196
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-367 2.66e-117

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 346.36  E-value: 2.66e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP-ANKYPQCLCLSPTYELALQTGKVIEQMGKF 79
Cdd:COG0513   20 LGYTTPTPIQAQAIPLILAG--RDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTRELALQVAEELRKLAKY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  80 YPeLKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQ 152
Cdd:COG0513   98 LG-LRVATVYGGvsigrqiRALKRGV----DIVVATPGRLLDLIER-GALDLSGVETLVLDEADRML-DMGFIEDIERIL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 153 RMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAITIAQAMIFCH 232
Cdd:COG0513  171 KLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPERAIVFCN 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 233 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnE 312
Cdd:COG0513  250 TKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP------E 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 380503833 313 TYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLDEIEK 367
Cdd:COG0513  324 DYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIGQKIEEEELPGFEPVEE 377
PTZ00424 PTZ00424
helicase 45; Provisional
2-360 2.00e-90

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 277.09  E-value: 2.00e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfYP 81
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGD-YL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  82 ELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRM 154
Cdd:PTZ00424 124 KVRCHACVGGtvvrddiNKLKAGV----HMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEML-SRGFKGQIYDVFKK 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 155 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTR 234
Cdd:PTZ00424 198 LPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTR 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 235 KTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETY 314
Cdd:PTZ00424 278 RKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP------ENY 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 380503833 315 LHRIGRTGRFGKRGLAVNMVDSKhSMNILNRIQEHFNKKIERLDTD 360
Cdd:PTZ00424 352 IHRIGRSGRFGRKGVAINFVTPD-DIEQLKEIERHYNTQIEEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-363 3.33e-69

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 224.29  E-value: 3.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:PRK11776  22 LGYTEMTPIQAQSLPAILAG--KDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQR 153
Cdd:PRK11776 100 PNIKVLTLCGGvpmgpqiDSLEHGA----HIIVGTPGRILDHLRK-GTLDLDALNTLVLDEADRML-DMGFQDAIDAIIR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 154 MLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKrEEETLDTIKQYYVLCSsRDEKFQALCNLYGAITIAQAMIFCHT 233
Cdd:PRK11776 174 QAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVS-PDERLPALQRLLLHHQPESCVVFCNT 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 234 RKTASWLAAELSKEGHQVALLSGEMmvEQ--RAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgnPDN 311
Cdd:PRK11776 252 KKECQEVADALNAQGFSALALHGDL--EQrdRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELA------RDP 323
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 380503833 312 ETYLHRIGRTGRFGKRGLAVNMVdSKHSMNILNRIQEHFNKKIERLDTDDLD 363
Cdd:PRK11776 324 EVHVHRIGRTGRAGSKGLALSLV-APEEMQRANAIEDYLGRKLNWEPLPSLS 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
1-362 1.62e-67

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 219.04  E-value: 1.62e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANK--YPQCLCLSPTYELALQtgkVIEQM 76
Cdd:PRK11192  19 KGYTRPTAIQAEAIPPALDG--RDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKsgPPRILILTPTRELAMQ---VADQA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKFYPELKL---------AYAVRGNKLERGQkiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMIATQGHQD- 146
Cdd:PRK11192  94 RELAKHTHLdiatitggvAYMNHAEVFSENQ----DIVVATPGRLLQYIKEENF-DCRAVETLILDEADRMLDMGFAQDi 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 147 QSIRIQrmlPRNC-QMLLFSATFE-DSVWKFAQKVVPDPNVIKL---KREEETldtIKQYYVLCSSRDEKFQALCNLYGA 221
Cdd:PRK11192 169 ETIAAE---TRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAepsRRERKK---IHQWYYRADDLEHKTALLCHLLKQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 222 ITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDL 301
Cdd:PRK11192 243 PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380503833 302 PVDKDgnpdneTYLHRIGRTGRFGKRGLAVNMVDSkHSMNILNRIQEHFNKKIERLDTDDL 362
Cdd:PRK11192 323 PRSAD------TYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKIERYIEEPLKARVIDEL 376
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
1-337 9.85e-58

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 198.15  E-value: 9.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:PRK11634  24 LGYEKPSPIQAECIPHLLNG--RDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPR 157
Cdd:PRK11634 102 RGVNVVALYGGQRYDvqlRALRQGPQIVVGTPGRLLDHL-KRGTLDLSKLSGLVLDEADEML-RMGFIEDVETIMAQIPE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 158 NCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ-YYVLCSSRdeKFQALCNLYGAITIAQAMIFCHTRKT 236
Cdd:PRK11634 180 GHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsYWTVWGMR--KNEALVRFLEAEDFDAAIIFVRTKNA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 237 ASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVdkdgnpDNETYLH 316
Cdd:PRK11634 258 TLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM------DSESYVH 331
                        330       340
                 ....*....|....*....|.
gi 380503833 317 RIGRTGRFGKRGLAVNMVDSK 337
Cdd:PRK11634 332 RIGRTGRAGRAGRALLFVENR 352
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
1-355 3.37e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 193.21  E-value: 3.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----PANKY---PQCLCLSPTYELALQTGKVI 73
Cdd:PRK01297 105 LGFPYCTPIQAQVLGYTLAG--HDAIGRAQTGTGKTAAFLISIINQLLqtppPKERYmgePRALIIAPTRELVVQIAKDA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  74 EQMGKfYPELKLAYAVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 149
Cdd:PRK01297 183 AALTK-YTGLNVMTFVGGMDFDKQLKQLEArfcdILVATPGRLLDFNQR-GEVHLDMVEVMVLDEADRML-DMGFIPQVR 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 150 RIQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDeKFQALCNLYGAITIAQA 227
Cdd:PRK01297 260 QIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLLYNLVTQNPWERV 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 228 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDkdg 307
Cdd:PRK01297 339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPED--- 415
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 380503833 308 nPDNetYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKIE 355
Cdd:PRK01297 416 -PDD--YVHRIGRTGRAGASGVSISFAGEDDAFQ-LPEIEELLGRKIS 459
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
2-354 5.80e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 184.38  E-value: 5.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQenALPLMLAEPPQNLIAQSQSGTGKTAAFVLA----MLSQVEPANKYPQ---CLCLSPTYELALQTGKvie 74
Cdd:PRK04537  28 GFTRCTPIQ--ALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnrLLSRPALADRKPEdprALILAPTRELAIQIHK--- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKFYPELKLAYAV--RGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDqsI 149
Cdd:PRK04537 103 DAVKFGADLGLRFALvyGGVDYDKQRELLQQgvdVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKD--I 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 150 R-IQRMLPRNC--QMLLFSATFEDSVWKFAQKVVPDPNviKLKREEETLDTIK-QYYVLCSSRDEKFQALCNLYGAITIA 225
Cdd:PRK04537 181 RfLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPE--KLVVETETITAARvRQRIYFPADEEKQTLLLGLLSRSEGA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 226 QAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 305
Cdd:PRK04537 259 RTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDA 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 380503833 306 dgnpdnETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 354
Cdd:PRK04537 339 ------EDYVHRIGRTARLGEEGDAISFACERYAMS-LPDIEAYIEQKI 380
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
198-334 1.39e-52

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 170.77  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 198 IKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKV 277
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 380503833 278 LVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRGLAVNMV 334
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDA------EDYVHRIGRTGRAGRKGTAITFV 131
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
1-354 2.03e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 179.40  E-value: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY---PQCLCLSPTYELALQTGKVI 73
Cdd:PRK04837  26 KGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKvnqPRALIMAPTRELAVQIHADA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  74 EQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATQGHQDqsIR 150
Cdd:PRK04837 104 EPLAQ-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDY-AKQNHINLGAIQVVVLDEADRMFDLGFIKD--IR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 151 --IQRMLPRNCQM-LLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQ--YYvlcSSRDEKFQALCNLYGAITIA 225
Cdd:PRK04837 180 wlFRRMPPANQRLnMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PSNEEKMRLLQTLIEEEWPD 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 226 QAMIFCHTR----KTASWLAAElskeGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDL 301
Cdd:PRK04837 257 RAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDL 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 380503833 302 PvdkdgnPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNiLNRIQEHFNKKI 354
Cdd:PRK04837 333 P------DDCEDYVHRIGRTGRAGASGHSISLACEEYALN-LPAIETYIGHSI 378
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
1-187 4.82e-52

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 171.47  E-value: 4.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEP----ANKYPQCLCLSPTYELALQTGKVIEQM 76
Cdd:cd00268    8 LGFEKPTPIQAQAIPLILSG--RDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAEVARKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKfYPELKlAYAVRGnklerGQKISEQ---------IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQ 147
Cdd:cd00268   86 GK-GTGLK-VAAIYG-----GAPIKKQiealkkgpdIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRML-DMGFEED 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 380503833 148 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd00268  157 VEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
2-334 9.91e-49

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 170.37  E-value: 9.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML-----SQVEPANKYP-QCLCLSPTYELALQTGKVIEQ 75
Cdd:PRK10590  20 GYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLqhlitRQPHAKGRRPvRALILTPTRELAAQIGENVRD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  76 MGKFYPELKLAyaVRGnklerGQKISEQ---------IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQD 146
Cdd:PRK10590  98 YSKYLNIRSLV--VFG-----GVSINPQmmklrggvdVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRML-DMGFIH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 147 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYyVLCSSRDEKFQALCNLYGAITIAQ 226
Cdd:PRK10590 169 DIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRKRELLSQMIGKGNWQQ 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 227 AMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP-VDK 305
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPnVPE 327
                        330       340
                 ....*....|....*....|....*....
gi 380503833 306 DgnpdnetYLHRIGRTGRFGKRGLAVNMV 334
Cdd:PRK10590 328 D-------YVHRIGRTGRAAATGEALSLV 349
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
2-186 5.01e-43

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: 148.24  E-value: 5.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENA-LPLMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGkFY 80
Cdd:cd17939   16 GFEKPSAIQQRAiVPIIKGR---DVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALG-DY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPR 157
Cdd:cd17939   92 MGVKVHACIGGTSVRedrRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEML-SRGFKDQIYDIFQFLPP 169
                        170       180
                 ....*....|....*....|....*....
gi 380503833 158 NCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd17939  170 ETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
1-186 1.02e-39

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: 139.74  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfY 80
Cdd:cd17940   17 KGFEKPSPIQEESIPIALSG--RDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKELGK-H 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPR 157
Cdd:cd17940   94 MGVKVMVTTGGTSLrDDIMRLYQtvHVLVGTPGRILDLAKK-GVADLSHCKTLVLDEADKLL-SQDFQPIIEKILNFLPK 171
                        170       180
                 ....*....|....*....|....*....
gi 380503833 158 NCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd17940  172 ERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PTZ00110 PTZ00110
helicase; Provisional
2-330 1.73e-39

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 147.23  E-value: 1.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQtgkVIEQM 76
Cdd:PTZ00110 149 GFTEPTPIQVQGWPIALSG--RDMIGIAETGSGKTLAFLLPAIVHInaQPLLRYgdgPIVLVLAPTRELAEQ---IREQC 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKFYPELKLAYAVR-GNKLERGQKIS----EQIVIGTPGTVLDW----CSKLKfidpkKIKVFVLDEADVMIaTQGHQDQ 147
Cdd:PTZ00110 224 NKFGASSKIRNTVAyGGVPKRGQIYAlrrgVEILIACPGRLIDFlesnVTNLR-----RVTYLVLDEADRML-DMGFEPQ 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 148 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP----NV--IKLKreeeTLDTIKQYYVLCSSRdEKFQALCNLYGA 221
Cdd:PTZ00110 298 IRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpvhvNVgsLDLT----ACHNIKQEVFVVEEH-EKRGKLKMLLQR 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 222 ITI--AQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINF 299
Cdd:PTZ00110 373 IMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINF 452
                        330       340       350
                 ....*....|....*....|....*....|.
gi 380503833 300 DLPvdkdgnPDNETYLHRIGRTGRFGKRGLA 330
Cdd:PTZ00110 453 DFP------NQIEDYVHRIGRTGRAGAKGAS 477
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
2-183 3.30e-39

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: 138.35  E-value: 3.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGkFY 80
Cdd:cd18046   18 GFEKPSAIQQRAiMPCIKG---YDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALG-DY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQR 153
Cdd:cd18046   94 MGIKCHACIGGtsvrddaQKLQAGP----HIVVGTPGRVFDMINR-RYLRTDYIKMFVLDEADEML-SRGFKDQIYDIFQ 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 380503833 154 MLPRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd18046  168 KLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
7-172 3.54e-39

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 136.99  E-value: 3.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833    7 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYpELKLA 86
Cdd:pfam00270   1 TPIQAEAIPAILEG--RDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   87 YAVRGN--KLERGQKISEQIVIGTPGTVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLF 164
Cdd:pfam00270  78 SLLGGDsrKEQLEKLKGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLL-DMGFGPDLEEILRRLPKKRQILLL 154

                  ....*...
gi 380503833  165 SATFEDSV 172
Cdd:pfam00270 155 SATLPRNL 162
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
2-335 4.45e-38

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 143.00  E-value: 4.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS-------QVEPANKYPQCLCLSPTYELALQTGKVIE 74
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSG--RSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLAMVLTPTRELCVQVEDQAK 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKFYPeLKLAYAVRGN----KLERGQKISEQIViGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIR 150
Cdd:PLN00206 218 VLGKGLP-FKTALVVGGDampqQLYRIQQGVELIV-GTPGRLIDLLSKHD-IELDNVSVLVLDEVDCML-ERGFRDQVMQ 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 151 IQRMLPRNcQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQalcnLYGAITIAQ---- 226
Cdd:PLN00206 294 IFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----LFDILKSKQhfkp 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 227 -AMIFCHTRKTASWLAAELSK-EGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvd 304
Cdd:PLN00206 369 pAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP-- 446
                        330       340       350
                 ....*....|....*....|....*....|.
gi 380503833 305 kdgNPDNEtYLHRIGRTGRFGKRGLAVNMVD 335
Cdd:PLN00206 447 ---NTIKE-YIHQIGRASRMGEKGTAIVFVN 473
DEXDc smart00487
DEAD-like helicases superfamily;
1-201 2.62e-36

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 130.69  E-value: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833     1 MGFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAMLSQVEPaNKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGL-RDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833    81 PELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRMLPR 157
Cdd:smart00487  82 GLKVVGLYGGDSKREQLRKLESgktDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 380503833   158 NCQMLLFSATFEDSVWKFAQKVVPDPNVIklKREEETLDTIKQY 201
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFI--DVGFTPLEPIEQF 201
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
2-186 1.02e-34

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: 126.43  E-value: 1.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd18045   18 GFEKPSAIQQRAIkPIIKG---RDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 pELKLAYAVRGN-------KLERGQkiseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQR 153
Cdd:cd18045   95 -NVQCHACIGGTsvgddirKLDYGQ----HIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEML-NKGFKEQIYDVYR 167
                        170       180       190
                 ....*....|....*....|....*....|...
gi 380503833 154 MLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd18045  168 YLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
1-187 1.60e-34

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 125.84  E-value: 1.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd17943    8 AGFQRPSPIQLAAIPLGLAG--HDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKLERG-QKISE-QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEAD-VMIATqgHQDQSIRIQRMLPR 157
Cdd:cd17943   86 EGLKCEVFIGGTPVKEDkKKLKGcHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADkLMEGS--FQKDVNWIFSSLPK 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 380503833 158 NCQMLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd17943  163 NKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
1-187 6.75e-33

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: 122.03  E-value: 6.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLS--QVEPANKYPQCLCLSPTYELALQTGKVIEQMGK 78
Cdd:cd17959   19 KGYKVPTPIQRKTIPLILD--GRDVVAMARTGSGKTAAFLIPMIEklKAHSPTVGARALILSPTRELALQTLKVTKELGK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  79 FyPELKLAYAVRGNKLERG-QKISEQ--IVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMIAtQGHQDQSIRIQRML 155
Cdd:cd17959   97 F-TDLRTALLVGGDSLEEQfEALASNpdIIIATPGRLLHLLVEMNL-KLSSVEYVVFDEADRLFE-MGFAEQLHEILSRL 173
                        170       180       190
                 ....*....|....*....|....*....|..
gi 380503833 156 PRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd17959  174 PENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
210-325 3.34e-32

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.93  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  210 EKFQALCNLYGAITIAQAMIFCHTRKTA--SWLaaeLSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARG 287
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 380503833  288 IDVEQVSVVINFDLPvdkdGNPdnETYLHRIGRTGRFG 325
Cdd:pfam00271  78 LDLPDVDLVINYDLP----WNP--ASYIQRIGRAGRAG 109
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
1-188 4.64e-32

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: 119.61  E-value: 4.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTYELALQTGKVIE 74
Cdd:cd17961   12 LGWEKPTLIQSKAIPLALEG--KDILARARTGSGKTAAYALPIIqkilkaKAESGEEQGTRALILVPTRELAQQVSKVLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKFY-PELKLAyAVRGNKLERGQK--ISEQ--IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 149
Cdd:cd17961   90 QLTAYCrKDVRVV-NLSASSSDSVQRalLAEKpdIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVL-SYGYEEDLK 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 380503833 150 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKL 188
Cdd:cd17961  168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
1-176 9.22e-31

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: 115.82  E-value: 9.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQCLCLSPTYELALQTGKVIEQMG 77
Cdd:cd17947    8 LGFTKPTPIQAAAIPLALLG--KDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  78 KFYPeLKLAYAVRGNKL---ERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRM 154
Cdd:cd17947   86 QFTD-ITFALAVGGLSLkaqEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRML-EEGFADELKEILRL 163
                        170       180
                 ....*....|....*....|..
gi 380503833 155 LPRNCQMLLFSATFEDSVWKFA 176
Cdd:cd17947  164 CPRTRQTMLFSATMTDEVKDLA 185
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
2-183 1.31e-30

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: 115.91  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALP-LMLAEppqNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd17950   21 GFEHPSEVQHECIPqAILGM---DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYM 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAY-----AVRGNKlERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRML 155
Cdd:cd17950   98 PNVKTAVffggvPIKKDI-EVLKNKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKMLEQLDMRRDVQEIFRAT 175
                        170       180
                 ....*....|....*....|....*...
gi 380503833 156 PRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17950  176 PHDKQVMMFSATLSKEIRPVCKKFMQDP 203
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
1-183 2.26e-28

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: 109.71  E-value: 2.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFy 80
Cdd:cd17954   18 LGWKKPTKIQEEAIPVALQG--RDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELAQQISEQFEALGSS- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRG-----NKLERGQKisEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIatqgHQDQSIRIQRML 155
Cdd:cd17954   95 IGLKSAVLVGGmdmmaQAIALAKK--PHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLL----NMDFEPEIDKIL 168
                        170       180       190
                 ....*....|....*....|....*....|.
gi 380503833 156 ---PRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17954  169 kviPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
2-183 2.50e-28

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 109.18  E-value: 2.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYP 81
Cdd:cd17962    9 GYEVPTPIQMQMIPVGLLG--RDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  82 ELKLAYAVRGN----KLERGQKiSEQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPR 157
Cdd:cd17962   87 PMKTALLVGGLplppQLYRLQQ-GVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTML-KMGFQQQVLDILENISH 163
                        170       180
                 ....*....|....*....|....*.
gi 380503833 158 NCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17962  164 DHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
1-186 3.56e-27

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: 106.90  E-value: 3.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLaEPPQNLIAQSQSGTGKTAAFVL----AMLSQVEPANKYP-QCLCLSPTYELALQTGKVIEQ 75
Cdd:cd17964   12 MGFETMTPVQQKTLKPIL-STGDDVLARAKTGTGKTLAFLLpaiqSLLNTKPAGRRSGvSALIISPTRELALQIAAEAKK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  76 MGKFYPELKLAYAVRGNK----LERGQKISEQIVIGTPG---TVLDWCSKLKFIdpKKIKVFVLDEADVMIaTQGHQDQS 148
Cdd:cd17964   91 LLQGLRKLRVQSAVGGTSrraeLNRLRRGRPDILVATPGrliDHLENPGVAKAF--TDLDYLVLDEADRLL-DMGFRPDL 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 380503833 149 IRIQRMLPRNC----QMLLFSATFEDSVWKFAQKVV-PDPNVI 186
Cdd:cd17964  168 EQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLkKDYKFI 210
HELICc smart00490
helicase superfamily c-terminal domain;
239-325 4.09e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.29  E-value: 4.09e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   239 WLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRI 318
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP------ASYIQRI 75

                   ....*..
gi 380503833   319 GRTGRFG 325
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 ...
1-183 9.74e-27

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: 105.48  E-value: 9.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVepankypQCLCLSPTYELALQTGKVIEQMGKFY 80
Cdd:cd17938   17 LDWLLPTDIQAEAIPLILGG--GDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYNCIENFKKYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 --PELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRML 155
Cdd:cd17938   88 dnPKLRVALLIGGVKAREQLKRLESgvdIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLL-SQGNLETINRIYNRI 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380503833 156 P------RNCQMLLFSATFE-DSVWKFAQKVVPDP 183
Cdd:cd17938  166 PkitsdgKRLQVIVCSATLHsFEVKKLADKIMHFP 200
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
1-183 1.01e-25

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: 102.69  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYpqCLCLSPTYELALQtgkVIEQM-- 76
Cdd:cd17955   17 LGIKEPTPIQKLCIPEILAG--RDVIGGAKTGSGKTAAFALPILQRlsEDPYGIF--ALVLTPTRELAYQ---IAEQFra 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 -GKFyPELKLAYAVRG-NKLERGQKISEQ--IVIGTPGTVLDW---CSKLKFiDPKKIKVFVLDEADVMIaTQGHQDQSI 149
Cdd:cd17955   90 lGAP-LGLRCCVIVGGmDMVKQALELSKRphIVVATPGRLADHlrsSDDTTK-VLSRVKFLVLDEADRLL-TGSFEDDLA 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 380503833 150 RIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17955  167 TILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
1-172 1.83e-24

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: 99.19  E-value: 1.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYPQ--CLCLSPTYELALQTGKVIEQ 75
Cdd:cd17960    8 LGFTSMTPVQAATIPLFLSN--KDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIYEVLQS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  76 MGKFY-PELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLD-WCSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSI 149
Cdd:cd17960   86 FLEHHlPKLKCQLLIGGTNVEEDVKKfkrnGPNILVGTPGRLEElLSRKADKVKVKSLEVLVLDEADRLLDL-GFEADLN 164
                        170       180
                 ....*....|....*....|...
gi 380503833 150 RIQRMLPRNCQMLLFSATFEDSV 172
Cdd:cd17960  165 RILSKLPKQRRTGLFSATQTDAV 187
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
1-177 5.46e-24

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: 98.33  E-value: 5.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANK--------YPQCLCLSPTYELALQTg 70
Cdd:cd17967   18 AGYTKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPIISKLleDGPPSvgrgrrkaYPSALILAPTRELAIQI- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  71 kvieqmgkfYPE-LKLAY-------AVRGNKLERGQKISEQ----IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVM 138
Cdd:cd17967   95 ---------YEEaRKFSYrsgvrsvVVYGGADVVHQQLQLLrgcdILVATPGRLVDFIERGR-ISLSSIKFLVLDEADRM 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380503833 139 IaTQGHQDQsirIQRML-------PRNCQMLLFSATFEDSVWKFAQ 177
Cdd:cd17967  165 L-DMGFEPQ---IRKIVehpdmppKGERQTLMFSATFPREIQRLAA 206
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
2-178 9.77e-22

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: 93.11  E-value: 9.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ-----VEPAN----KYPQCLCLSPTYELALQTGKv 72
Cdd:cd18052   62 GYEKPTPVQKYAIPIILAG--RDLMACAQTGSGKTAAFLLPVLTGmmkegLTASSfsevQEPQALIVAPTRELANQIFL- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  73 ieQMGKF-----------YPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIAT 141
Cdd:cd18052  139 --EARKFsygtcirpvvvYGGVSVGHQIR--QIEKGC----HILVATPGRLLDFIGRGK-ISLSKLKYLILDEADRMLDM 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 380503833 142 QGHQDqsirIQRML-----PR--NCQMLLFSATFEDSVWKFAQK 178
Cdd:cd18052  210 GFGPE----IRKLVsepgmPSkeDRQTLMFSATFPEEIQRLAAE 249
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
2-186 1.71e-21

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


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 90.81  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEpANKYPQ-----CLCLSPTYELALQTGKVIEQM 76
Cdd:cd17941    9 GFIKMTEIQRDSIPHALQG--RDILGAAKTGSGKTLAFLVPLLEKLY-RERWTPedglgALIISPTRELAMQIFEVLRKV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKfYPELKLAYAVRGNKLERGQ-KISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRM 154
Cdd:cd17941   86 GK-YHSFSAGLIIGGKDVKEEKeRINRmNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEAD-RILDMGFKETLDAIVEN 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 380503833 155 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd17941  164 LPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
1-183 5.73e-21

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 90.13  E-value: 5.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQtgkVIEQ 75
Cdd:cd17953   30 LGYEKPTPIQAQALPAIMSG--RDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIGLIMAPTRELALQ---IYVE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  76 MGKFYPELKL-AYAVRGnklerGQKISEQ---------IVIGTPGTVLDW--CSKLKFIDPKKIKVFVLDEADVMIaTQG 143
Cdd:cd17953  105 CKKFSKALGLrVVCVYG-----GSGISEQiaelkrgaeIVVCTPGRMIDIltANNGRVTNLRRVTYVVLDEADRMF-DMG 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 380503833 144 HQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17953  179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
2-183 9.88e-21

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 88.80  E-value: 9.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEPpqNLIAQSQSGTGKTAAFVLAMLSQVEP--ANKYPQCLCLSPTYELALQTGKVIEQMGKF 79
Cdd:cd17957    9 GYREPTPIQMQAIPILLHGR--DLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYRELLKLSKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  80 YPE-----LKLAYAVRGNKLERGQKISeqIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRM 154
Cdd:cd17957   87 TGLrivllSKSLEAKAKDGPKSITKYD--ILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEP-GFREQTDEILAA 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 380503833 155 LPRNC-QMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17957  163 CTNPNlQRSLFSATIPSEVEELARSVMKDP 192
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
1-178 1.25e-20

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: 89.30  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAML---SQVEPANKY-----PQCLCLSPTYELALQTGKV 72
Cdd:cd17945    8 LGYKEPTPIQRQAIPIGLQ--NRDIIGIAETGSGKTAAFLIPLLvyiSRLPPLDEEtkddgPYALILAPTRELAQQIEEE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  73 IEQMGKFYPeLKLAYAVRGNKLE-RGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSI 149
Cdd:cd17945   86 TQKFAKPLG-IRVVSIVGGHSIEeQAFSLRNgcEILIATPGRLLD-CLERRLLVLNQCTYVVLDEADRMI-DMGFEPQVT 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 380503833 150 RIQRMLP--------------------RNCQMLLFSATFEDSVWKFAQK 178
Cdd:cd17945  163 KILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKG 211
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
2-186 1.62e-20

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: 88.24  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQTGKVIEQM 76
Cdd:cd17952    9 EYEQPTPIQAQALPVALSG--RDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQIYLEAKKF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRIQRM 154
Cdd:cd17952   87 GKAYNLRVVAVYGGGSKWEQAKALQEgaEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMF-DMGFEYQVRSIVGH 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 380503833 155 LPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd17952  165 VRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
1-187 4.58e-20

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 87.26  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPA------NKYPQCLCLSPTYELALQTGKVIE 74
Cdd:cd17949    9 MGIEKPTAIQKLAIPVLLQG--RDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdrSDGTLALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKFYPELKLAYAVRGNKlergqKISEQ--------IVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQGHQD 146
Cdd:cd17949   87 KLLKPFHWIVPGYLIGGEK-----RKSEKarlrkgvnILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLL-DMGFEK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 380503833 147 QSIRIQRML-------------PRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 187
Cdd:cd17949  161 DITKILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
1-183 9.62e-20

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


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 85.98  E-value: 9.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQVEPANKY--PQCLCLSPTYELALQtgkVIE 74
Cdd:cd17958    8 QGFEKPSPIQSQAWPIILQG--IDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRngPGVLVLTPTRELALQ---IEA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKF-YPELKlAYAVRGNKlERGQKISEQ-----IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIaTQGHQDQS 148
Cdd:cd17958   83 ECSKYsYKGLK-SVCVYGGG-NRNEQIEDLskgvdIIIATPGRLND-LQMNNVINLKSITYLVLDEADRML-DMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380503833 149 IRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
3-168 1.16e-19

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 87.02  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   3 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPA----------NKYPQCLCLSPTYELA 66
Cdd:cd18051   41 YTKPTPVQKHAIPIIKSK--RDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLpsesgyygrrKQYPLALVLAPTRELA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  67 LQtgkVIEQMGKFypelklAY--AVRGNKLERGQKISEQI---------VIGTPGTVLDWCSKLKfIDPKKIKVFVLDEA 135
Cdd:cd18051  119 SQ---IYDEARKF------AYrsRVRPCVVYGGADIGQQMrdlergchlLVATPGRLVDMLERGK-IGLDYCKYLVLDEA 188
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 380503833 136 DVMIaTQGHQDQSIRI--QRMLPRNC--QMLLFSATF 168
Cdd:cd18051  189 DRML-DMGFEPQIRRIveQDTMPPTGerQTLMFSATF 224
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
2-168 2.89e-19

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 85.75  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   2 GFNRPSKIQENALPLMLAEPpQNLIAQSQSGTGKTAAFVLAM----LSQVE-----PANKYPQCLCLSPTYELALQTGKV 72
Cdd:cd17946    9 GFSEPTPIQALALPAAIRDG-KDVIGAAETGSGKTLAFGIPIlerlLSQKSsngvgGKQKPLRALILTPTRELAVQVKDH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  73 IEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDW----CSKLKFIdpKKIKVFVLDEADVMIaTQGHQ 145
Cdd:cd17946   88 LKAIAK-YTNIKIASIVGGLAVQKQERLLKKrpeIVVATPGRLWELiqegNEHLANL--KSLRFLVLDEADRML-EKGHF 163
                        170       180       190
                 ....*....|....*....|....*....|
gi 380503833 146 DQSIRIQRMLPRNC-------QMLLFSATF 168
Cdd:cd17946  164 AELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
1-167 5.57e-18

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


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 81.25  E-value: 5.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCLSPTYELALQTGKVIEQM 76
Cdd:cd17942    8 MGFTKMTEIQAKSIPPLLEG--RDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGVAKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  77 GKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIATQGHQDQSIRIQRM 154
Cdd:cd17942   86 LKYHSQTFGIVIGGANRKAEAEKLGKgvNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEAD-RILEIGFEEEMRQIIKL 164
                        170
                 ....*....|...
gi 380503833 155 LPRNCQMLLFSAT 167
Cdd:cd17942  165 LPKRRQTMLFSAT 177
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
1-186 1.29e-17

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 80.46  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYPQC-------LCLSPTYELALQTGKV 72
Cdd:cd17951    8 KGIKKPTPIQMQGLPTILSG--RDMIGIAFTGSGKTLVFTLPLIMFaLEQEKKLPFIkgegpygLIVCPSRELARQTHEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  73 IEQMGKF-----YPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIaTQGH 144
Cdd:cd17951   86 IEYYCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKgvhIVVATPGRLMDMLNK-KKINLDICRYLCLDEADRMI-DMGF 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 380503833 145 QDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 186
Cdd:cd17951  164 EEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
1-183 1.62e-16

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: 77.02  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPANKyPQCLCLSPTYELALQtgkVIE 74
Cdd:cd17966    8 QGFTEPTAIQAQGWPMALSG--RDMVGIAQTGSGKTLAFLLPAIVHInaqpplERGDG-PIVLVLAPTRELAQQ---IQQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  75 QMGKFYPELKL----AY--AVRGNK---LERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQ 145
Cdd:cd17966   82 EANKFGGSSRLrntcVYggAPKGPQirdLRRGV----EICIATPGRLIDFLDQGK-TNLRRVTYLVLDEADRML-DMGFE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 380503833 146 DQ------SIRIQRmlprncQMLLFSATFEDSVWKFAQKVVPDP 183
Cdd:cd17966  156 PQirkivdQIRPDR------QTLMWSATWPKEVRRLAEDFLKDY 193
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
32-368 2.33e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 74.29  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  32 GTGKT--AAFVLAMLSQVEPAnkypqcLCLSPTYELALQTGKVIEQMgkfypeLKLAYAVRGNKlergqKISEQIVIGTP 109
Cdd:COG1061  110 GTGKTvlALALAAELLRGKRV------LVLVPRRELLEQWAEELRRF------LGDPLAGGGKK-----DSDAPITVATY 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 110 GTVldwcSKLKFID--PKKIKVFVLDEAdvmiatqgHQDQSIRIQRMLPR--NCQMLLFSAT--FEDSVWKF-------- 175
Cdd:COG1061  173 QSL----ARRAHLDelGDRFGLVIIDEA--------HHAGAPSYRRILEAfpAAYRLGLTATpfRSDGREILlflfdgiv 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 176 ---------AQKVVPDPNVI----KLKREEETLDTIKQ--YYVLCSSRDEKFQALCNLYGAIT-IAQAMIFCHTRKTASW 239
Cdd:COG1061  241 yeyslkeaiEDGYLAPPEYYgirvDLTDERAEYDALSErlREALAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 240 LAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdGNPDneTYLHRIG 319
Cdd:COG1061  321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PT---GSPR--EFIQRLG 394
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 380503833 320 R---TGRFGKRGLAVNMVDSKHSM--NILNRIQEHFNKKIERLDTDDLDEIEKI 368
Cdd:COG1061  395 RglrPAPGKEDALVYDFVGNDVPVleELAKDLRDLAGYRVEFLDEEESEELALL 448
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
3-182 2.56e-14

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


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 72.35  E-value: 2.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   3 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EP---ANKYPQCLCLSPTYELALQTGKVIEQMG 77
Cdd:cd18050   82 FKEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHInhQPyleRGDGPICLVLAPTRELAQQVQQVADDYG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  78 KfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMIaTQGHQDQSIR 150
Cdd:cd18050  160 K-SSRLKSTCIYGGapkgpqiRDLERGV----EICIATPGRLIDFLEAGK-TNLRRCTYLVLDEADRML-DMGFEPQIRK 232
                        170       180       190
                 ....*....|....*....|....*....|..
gi 380503833 151 IQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 182
Cdd:cd18050  233 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
23-178 5.00e-14

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 70.26  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  23 QNLIAQSQSGTGKTAAFVLAML------SQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKfypelKLAYAVRGNKLER 96
Cdd:cd17944   28 KDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  97 GQKISE-----QIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI----ATQGHQDQSIRIQRMLPRNCQMLLFSAT 167
Cdd:cd17944  103 QQQIFAirngiDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLdmgfAEQVEEILSVSYKKDSEDNPQTLLFSAT 181
                        170
                 ....*....|.
gi 380503833 168 FEDSVWKFAQK 178
Cdd:cd17944  182 CPDWVYNVAKK 192
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
24-167 7.36e-14

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 68.20  E-value: 7.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  24 NLIAQSQSGTGKTAAFVLAMLSQVEPanKYPQCLCLSPTYELALQTGKVIeqMGKFYPELKLAYAVRG-NKLERGQKI-- 100
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERL--RELFGPGIRVAVLVGGsSAEEREKNKlg 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380503833 101 SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM-IATQGHQDQSIRIQRMLPRNCQMLLFSAT 167
Cdd:cd00046   79 DADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALlIDSRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
3-182 4.12e-13

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


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 68.11  E-value: 4.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   3 FNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKY---PQCLCLSPTYELALQTGKVIEQMG 77
Cdd:cd18049   44 FTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHInhQPFLERgdgPICLVLAPTRELAQQVQQVAAEYG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  78 K--------FYPELKLAYAVRgnKLERGQkiseQIVIGTPGTVLDW--CSKLKFidpKKIKVFVLDEADVMIaTQGHQDQ 147
Cdd:cd18049  122 RacrlkstcIYGGAPKGPQIR--DLERGV----EICIATPGRLIDFleAGKTNL---RRCTYLVLDEADRML-DMGFEPQ 191
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380503833 148 SIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 182
Cdd:cd18049  192 IRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
174-326 1.08e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 69.37  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 174 KFAQKVVPDPNVIKLKREEETLDtikqyyvlcssrDE--KFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKE 247
Cdd:COG1111  309 KASKRLVSDPRFRKAMRLAEEAD------------IEhpKLSKLREIlkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEP 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 248 GHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlPVdkdgnPDNETYLHRIG 319
Cdd:COG1111  377 GIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PV-----PSEIRSIQRKG 450

                 ....*..
gi 380503833 320 RTGRFGK 326
Cdd:COG1111  451 RTGRKRE 457
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
229-325 3.34e-12

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 63.26  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 229 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPvdkd 306
Cdd:cd18793   32 IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPW---- 107
                         90
                 ....*....|....*....
gi 380503833 307 GNPDNEtyLHRIGRTGRFG 325
Cdd:cd18793  108 WNPAVE--EQAIDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
229-325 3.35e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.48  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 229 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEK--VLVTTNVCARGIDVEQVSVVINFDLPVdkd 306
Cdd:COG0553  554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWW--- 630
                         90
                 ....*....|....*....
gi 380503833 307 gNPDNEtyLHRIGRTGRFG 325
Cdd:COG0553  631 -NPAVE--EQAIDRAHRIG 646
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
1-181 2.23e-10

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 60.07  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKY--PQCLCLSPTYELALQTGKVI 73
Cdd:cd17948    8 QGITKPTTVQKQGIPSILRG--RNTLCAAETGSGKTLTYLLPIIQRLlryklLAEGPFnaPRGLVITPSRELAEQIGSVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  74 EQMGKFYPeLKlAYAVRGNKLERGQKISEQ----IVIGTPGTVldwcSKL---KFIDPKKIKVFVLDEADVMI------- 139
Cdd:cd17948   86 QSLTEGLG-LK-VKVITGGRTKRQIRNPHFeevdILVATPGAL----SKLltsRIYSLEQLRHLVLDEADTLLddsfnek 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 380503833 140 ------ATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVP 181
Cdd:cd17948  160 lshflrRFPLASRRSENTDG-LDPGTQLVLVSATMPSGVGEVLSKVID 206
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
208-302 2.78e-10

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 57.99  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 208 RDEKFQALCNL----YGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMV-------------EQRA--AVIE 268
Cdd:cd18802    5 VIPKLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGFLIgrgnssqrkrslmTQRKqkETLD 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 380503833 269 RFREGKEKVLVTTNVCARGIDVEQVSVVINFDLP 302
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLP 118
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
229-326 9.37e-10

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 56.06  E-value: 9.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 229 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPvdkdgn 308
Cdd:cd18794   35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLP------ 108
                         90
                 ....*....|....*...
gi 380503833 309 PDNETYLHRIGRTGRFGK 326
Cdd:cd18794  109 KSMESYYQESGRAGRDGL 126
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
1-167 1.39e-09

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 57.64  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   1 MGFNRPSKIQENALPLMLAE-------PPQNLIAQSQSGTGKTAAFVL----AMLSQVEPAnkyPQCLCLSPTYELALQT 69
Cdd:cd17956    8 NGITSAFPVQAAVIPWLLPSskstppyRPGDLCVSAPTGSGKTLAYVLpivqALSKRVVPR---LRALIVVPTKELVQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  70 GKVIEQMGKFYPeLKLAyAVRGNK-----------LERGQKISE-QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEAD- 136
Cdd:cd17956   85 YKVFESLCKGTG-LKVV-SLSGQKsfkkeqklllvDTSGRYLSRvDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEADr 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 380503833 137 ------------VMIATQGHQDQ------SIRIQRMLPRNCQMLLFSAT 167
Cdd:cd17956  163 llnqsfqdwletVMKALGRPTAPdlgsfgDANLLERSVRPLQKLLFSAT 211
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
229-331 1.64e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.00  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 229 IFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNvcA--RGIDVEQVSVVINFDLPvdkd 306
Cdd:COG0514  235 VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AfgMGIDKPDVRFVIHYDLP---- 308
                         90       100
                 ....*....|....*....|....*
gi 380503833 307 GNPdnETYLHRIGRTGRFGKRGLAV 331
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 ...
227-323 5.04e-08

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 51.59  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 227 AMIFCHTRKTASWLAAELSKEGHQV--ALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVV 296
Cdd:cd18801   33 VIIFSEFRDSAEEIVNFLSKIRPGIraTRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
                         90       100
                 ....*....|....*....|....*..
gi 380503833 297 INFdlpvdkDGNPDNETYLHRIGRTGR 323
Cdd:cd18801  113 ICY------DASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
225-331 1.28e-07

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 53.30  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 225 AQAMIFCHTRK----TASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVIN 298
Cdd:COG1205  289 LRTLVFTRSRRgaelLARYARRALREPdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVL 368
                         90       100       110
                 ....*....|....*....|....*....|....
gi 380503833 299 fdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 331
Cdd:COG1205  369 -------AGYPGTRAsFWQQAGRAGRRGQDSLVV 395
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
214-331 3.62e-07

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 49.18  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 214 ALCNLYGAITIAqamiFCHTRKTA----SWLAAELSKEGHQVALLS---GEMMVEQRAAVIERFREGKEKVLVTTNVCAR 286
Cdd:cd18797   29 ADLVRAGVKTIV----FCRSRKLAelllRYLKARLVEEGPLASKVAsyrAGYLAEDRREIEAELFNGELLGVVATNALEL 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 380503833 287 GIDVEQVSVVINfdlpvdkDGNPDNET-YLHRIGRTGRFGKRGLAV 331
Cdd:cd18797  105 GIDIGGLDAVVL-------AGYPGSLAsLWQQAGRAGRRGKDSLVI 143
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
233-353 6.75e-07

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 48.78  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 233 TRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDNE 312
Cdd:cd18790   36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGFLRSE 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 380503833 313 TYL-HRIGRTGRfGKRGLAV----NMVDS-KHSMNILNR---IQEHFNKK 353
Cdd:cd18790  114 TSLiQTIGRAAR-NVNGKVIlyadKITDSmQKAIEETERrreIQMEYNEE 162
PRK13766 PRK13766
Hef nuclease; Provisional
174-323 8.61e-07

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 51.03  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 174 KFAQKVVPDPNVIKLKRE-----------EETLDTIKQyyVLCSSRDEKfqalcnlygaitiaqAMIFCHTRKTASWLAA 242
Cdd:PRK13766 321 KASKRLVEDPRFRKAVRKakeldiehpklEKLREIVKE--QLGKNPDSR---------------IIVFTQYRDTAEKIVD 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 243 ELSKEGHQVALLSGE--------MMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVInFDLPVdkdgnPDNETY 314
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPV-----PSEIRS 457

                 ....*....
gi 380503833 315 LHRIGRTGR 323
Cdd:PRK13766 458 IQRKGRTGR 466
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
276-328 1.75e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.39  E-value: 1.75e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 380503833 276 KVLVTTNVCARGIDVEQVSVVINFDLPVDKdgnpdnETYLHRIGRTGRFGKRG 328
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSA------ASYIQRVGRAGRGGKDE 70
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
23-135 5.29e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.49  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  23 QNLIAQSQSGTGKT--AAFVL-AMLSQV-EPANKYPQCLCLSPTYELALQTGKVIEQ-----MGKFYPELKLAYAVRGNK 93
Cdd:cd18034   17 RNTIVVLPTGSGKTliAVMLIkEMGELNrKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlkVGEYSGEMGVDKWTKERW 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 380503833  94 LERGQKIseQIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEA 135
Cdd:cd18034   97 KEELEKY--DVLVMTAQILLDALRH-GFLSLSDINLLIFDEC 135
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
5-167 5.84e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 46.26  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833   5 RPSKIQENALPL----MLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEpANKypQCLCLSPTYELALQTGKVIEqmgKFY 80
Cdd:cd17918   15 SLTKDQAQAIKDiekdLHSPEPMDRLLSGDVGSGKTLVALGAALLAYK-NGK--QVAILVPTEILAHQHYEEAR---KFL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  81 PELKLAYAVRGNKlergQKISEQI--VIGTpgtvldwcSKLKFIDPKKikvfvlDEADVMIATQGHQ---DQSIRIQRMl 155
Cdd:cd17918   89 PFINVELVTGGTK----AQILSGIslLVGT--------HALLHLDVKF------KNLDLVIVDEQHRfgvAQREALYNL- 149
                        170
                 ....*....|..
gi 380503833 156 pRNCQMLLFSAT 167
Cdd:cd17918  150 -GATHFLEATAT 160
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
228-325 6.36e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 48.17  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 228 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKdg 307
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI-- 317
                         90
                 ....*....|....*...
gi 380503833 308 npdnETYLHRIGRTGRFG 325
Cdd:PRK11057 318 ----ESYYQETGRAGRDG 331
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
240-367 8.26e-06

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


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 45.76  E-value: 8.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 240 LAAELSKEGHQVALLSgemmvEQRAAVIERFREGKEKVLVTT----NVCARGIDV-EQVSVVINFDLPVdkdgnpdnETY 314
Cdd:cd18798   43 LKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYAIFYGVPV--------TTY 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380503833 315 LHRIGRTGRF--GK--RGLAVNMVDSKHSMNILNRIQEHF--NKKIERLDTDDLDEIEK 367
Cdd:cd18798  110 IQASGRTSRLyaGGltKGLSVVLVDDPELFEALKKRLKLIldEFIFKELEEVDLEELLS 168
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
251-341 1.51e-05

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 44.57  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 251 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 329
Cdd:cd18792   63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--ADRFGLSQ----LHQLrGRVGRGKHQSY 136
                         90
                 ....*....|..
gi 380503833 330 AVNMVDSKHSMN 341
Cdd:cd18792  137 CYLLYPDPKKLT 148
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
226-335 1.60e-05

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 44.47  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 226 QAMIFCHTRKTASWLAAELSKeghqVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDK 305
Cdd:cd18795   45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG 120
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 380503833 306 DGN---PDNEtYLHRIGRTGR--FGKRGLAVNMVD 335
Cdd:cd18795  121 KGYrelSPLE-YLQMIGRAGRpgFDTRGEAIIMTK 154
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
235-297 2.07e-05

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 46.30  E-value: 2.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380503833 235 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSV-VI 297
Cdd:PRK10917 490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
251-347 4.02e-05

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.49  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 251 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGnpdnETYLHRI-GRTGRFGKRGL 329
Cdd:cd18811   64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--AERFG----LSQLHQLrGRVGRGDHQSY 137
                         90
                 ....*....|....*...
gi 380503833 330 AVNMVDSKHSMNILNRIQ 347
Cdd:cd18811  138 CLLVYKDPLTETAKQRLR 155
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
225-297 8.38e-05

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


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 44.48  E-value: 8.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380503833 225 AQAMIFCHTRKTASWLAAELSKEGHQVALLSgemmV----EQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVI 297
Cdd:COG4098  320 RQLLIFVPTIELLEQLVALLQKLFPEERIAG----VhaedPERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAV 392
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
229-323 1.79e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 41.48  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 229 IFCHTRKTASWLAAEL------SKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFdlp 302
Cdd:cd18796   43 VFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI--- 119
                         90       100
                 ....*....|....*....|..
gi 380503833 303 vdkdGNPDNET-YLHRIGRTGR 323
Cdd:cd18796  120 ----GSPKSVArLLQRLGRSGH 137
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
228-331 2.85e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833  228 MIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDG 307
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                          90       100
                  ....*....|....*....|....
gi 380503833  308 npdnetYLHRIGRTGRFGKRGLAV 331
Cdd:PLN03137  764 ------YHQECGRAGRDGQRSSCV 781
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
251-341 6.69e-04

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 39.63  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 251 VALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDlpVDKDGNPDnetyLHRI-GRTGRFGKRGL 329
Cdd:cd18810   54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIER--ADKFGLAQ----LYQLrGRVGRSKERAY 127
                         90
                 ....*....|..
gi 380503833 330 AVNMVDSKHSMN 341
Cdd:cd18810  128 AYFLYPDQKKLT 139
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
129-327 1.32e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.49  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 129 VFVLDEADVMIA-TQGHQDQSIRIQRmlPRNCQMLLFSATFEDSVWKFAQKVVPDpnviklkREEETLDTI---KQYYVL 204
Cdd:cd09639  126 LLIFDEVHFYDEyTLALILAVLEVLK--DNDVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKpneRAPFIK 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 205 CSSRD-EKFQALCNLYGAIT-IAQAMIFCHTRKTASWLAAELSKEGHQ--VALLSGEMM----VEQRAAVIERFREGKEK 276
Cdd:cd09639  197 IESDKvGEISSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTekdrAKKEAELLLEFKKSEKF 276
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 380503833 277 VLVTTNVCargidveQVSVVINFDLPVDKDGNPDneTYLHRIGRTGRFGKR 327
Cdd:cd09639  277 VIVATQVI-------EASLDISVDVMITELAPID--SLIQRLGRLHRYGEK 318
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
235-290 1.35e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.80  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 380503833 235 KTASWLAAELSKE--GHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDV 290
Cdd:COG1200  488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDV 545
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
224-303 8.84e-03

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 35.61  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380503833 224 IAQAMIFCHTRKTASWLAAELSKEG-HQVALLSGEMMVEQRAAVIER--FREGKEKVLVTTNVCARGIDVEQVSVVInFD 300
Cdd:cd18799    6 EIKTLIFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDEALILlfFGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84

                 ...
gi 380503833 301 LPV 303
Cdd:cd18799   85 RPT 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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