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Conserved domains on  [gi|6320119|ref|NP_010199|]
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ATP-dependent RNA helicase SUB2 [Saccharomyces cerevisiae S288C]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028696)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
61-270 1.02e-153

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: 434.08  E-value: 1.02e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNAR 140
Cdd:cd17950   1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  141 ELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:cd17950  81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNK--CPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6320119  221 LEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFV 270
Cdd:cd17950 159 LEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
281-410 5.28e-51

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


:

Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 5.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  281 LQQYYIKLEEREKNRKL-AQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRI 359
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320119  360 CVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFV 410
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
61-270 1.02e-153

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: 434.08  E-value: 1.02e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNAR 140
Cdd:cd17950   1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  141 ELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:cd17950  81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNK--CPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6320119  221 LEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFV 270
Cdd:cd17950 159 LEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
61-440 6.51e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 376.41  E-value: 6.51e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDP-VPGEVAVVVICNA 139
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  140 RELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDK 219
Cdd:COG0513  81 RELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRG---VDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  220 VLeelDM--RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKlTLHGLQQYYIKLEEREKNRKL 297
Cdd:COG0513 157 ML---DMgfIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENA-TAETIEQRYYLVDKRDKLELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  298 AQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINL 377
Cdd:COG0513 233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320119  378 AINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEdEEVLAKIQERFDVKIAEFPEEGIDP 440
Cdd:COG0513 313 VINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE-RRLLRAIEKLIGQKIEEEELPGFEP 374
PTZ00424 PTZ00424
helicase 45; Provisional
64-436 1.60e-81

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 257.06  E-value: 1.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEE 223
Cdd:PTZ00424 110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKA---GVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   224 lDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEaKLTLHGLQQYYIKLEERE-KNRKLAQLLD 302
Cdd:PTZ00424 186 -GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKD-ELTLEGIRQFYVAVEKEEwKFDTLCDLYE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   303 DLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYD 382
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6320119   383 LTNEADQYLHRVGRAGRFGTKGLAISFVSSkEDEEVLAKIQERFDVKIAEFPEE 436
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTP-DDIEQLKEIERHYNTQIEEMPME 396
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
281-410 5.28e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 5.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  281 LQQYYIKLEEREKNRKL-AQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRI 359
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320119  360 CVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFV 410
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
77-284 2.22e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 143.40  E-value: 2.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119      77 IIDCGFEHPSEVQQHTIPQSIHGT-DVLCQAKSGLGKTAVFVLSTLQQLDPVPGeVAVVVICNARELAYQIRNEYLRFSK 155
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG-GRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     156 YMPdVKTAVFYGGTPISKDAELLKNKDTapHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEElDMRRDVQEIFR 235
Cdd:smart00487  80 SLG-LKVVGLYGGDSKREQLRKLESGKT--DILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG-GFGDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 6320119     236 ATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIfvdDEAKLTLHGLQQY 284
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI---DVGFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
86-255 8.86e-40

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: 140.46  E-value: 8.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     86 SEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMpDVKTAVF 165
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    166 YGGTPISKDAELLKNkdtaPHIVVATPGRLKALVREKyIDLSHVKNFVIDECDKVLEElDMRRDVQEIFRATPRDKQVMM 245
Cdd:pfam00270  80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDM-GFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|
gi 6320119    246 FSATLSQEIR 255
Cdd:pfam00270 154 LSATLPRNLE 163
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
292-401 1.93e-31

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.16  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    292 EKNRKLAQLLDDLEFNQVIIFVKSTTRAnELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGID 371
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 6320119    372 IERINLAINYDLTNEADQYLHRVGRAGRFG 401
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
321-401 7.41e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 7.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     321 ELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRF 400
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 6320119     401 G 401
Cdd:smart00490  82 G 82
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
286-426 8.95e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.46  E-value: 8.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  286 IKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDV 365
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIA 289
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320119  366 FGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSkEDEEvlakIQERF 426
Cdd:COG0514 290 FGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGP-EDVA----IQRFF 345
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
292-409 3.23e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 46.24  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   292 EKNRKLAQL---LDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGR 368
Cdd:PRK11057 219 EKFKPLDQLmryVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320119   369 GIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISF 409
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
 
Name Accession Description Interval E-value
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
61-270 1.02e-153

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: 434.08  E-value: 1.02e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNAR 140
Cdd:cd17950   1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  141 ELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:cd17950  81 ELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNK--CPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6320119  221 LEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFV 270
Cdd:cd17950 159 LEQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
61-440 6.51e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 376.41  E-value: 6.51e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDP-VPGEVAVVVICNA 139
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  140 RELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDK 219
Cdd:COG0513  81 RELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRG---VDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  220 VLeelDM--RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKlTLHGLQQYYIKLEEREKNRKL 297
Cdd:COG0513 157 ML---DMgfIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENA-TAETIEQRYYLVDKRDKLELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  298 AQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINL 377
Cdd:COG0513 233 RRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320119  378 AINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEdEEVLAKIQERFDVKIAEFPEEGIDP 440
Cdd:COG0513 313 VINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDE-RRLLRAIEKLIGQKIEEEELPGFEP 374
PTZ00424 PTZ00424
helicase 45; Provisional
64-436 1.60e-81

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 257.06  E-value: 1.60e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEE 223
Cdd:PTZ00424 110 QQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKA---GVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   224 lDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEaKLTLHGLQQYYIKLEERE-KNRKLAQLLD 302
Cdd:PTZ00424 186 -GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKD-ELTLEGIRQFYVAVEKEEwKFDTLCDLYE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   303 DLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYD 382
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6320119   383 LTNEADQYLHRVGRAGRFGTKGLAISFVSSkEDEEVLAKIQERFDVKIAEFPEE 436
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTP-DDIEQLKEIERHYNTQIEEMPME 396
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
61-431 3.19e-74

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 239.70  E-value: 3.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNAR 140
Cdd:PRK11776   3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   141 ELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:PRK11776  83 ELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEH---GAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   221 LeelDM--RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTlhGLQQYYIKLEEREKNRKLA 298
Cdd:PRK11776 160 L---DMgfQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP--AIEQRFYEVSPDERLPALQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   299 QLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEER---IARykaFKDFEKRICVSTDVFGRGIDIERI 375
Cdd:PRK11776 235 RLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRdqvLVR---FANRSCSVLVATDVAARGLDIKAL 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320119   376 NLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVlAKIQERFDVKIA 431
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRA-NAIEDYLGRKLN 366
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
62-426 2.19e-71

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 231.76  E-value: 2.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    62 TGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVP----GEVAVVVIC 137
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPrrksGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   138 NARELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELL-KNKDtaphIVVATPGRLKALVREKYIDLSHVKNFVIDE 216
Cdd:PRK11192  81 PTRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFsENQD----IVVATPGRLLQYIKEENFDCRAVETLILDE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   217 CDKVLeelDM--RRDVQEIFRATPRDKQVMMFSATLSQE-IRPICRRFLQNPLEIFVD----DEAKLTlhglQQYYIKLE 289
Cdd:PRK11192 156 ADRML---DMgfAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEpsrrERKKIH----QWYYRADD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   290 EREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRG 369
Cdd:PRK11192 229 LEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320119   370 IDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSkEDEEVLAKIqERF 426
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEA-HDHLLLGKI-ERY 363
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
73-268 2.39e-69

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: 218.47  E-value: 2.39e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDP----VPGEVAVVVICNARELAYQIRN 148
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  149 EYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLeELDMRR 228
Cdd:cd00268  81 VARKLGKGT-GLKVAAIYGGAPIKKQIEALKKG---PDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML-DMGFEE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6320119  229 DVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd00268 156 DVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
61-432 1.34e-67

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 227.04  E-value: 1.34e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    61 STGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNAR 140
Cdd:PRK11634   5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   141 ELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQ---GPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   221 LEeLDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKlTLHGLQQYYIKLEEREKNRKLAQL 300
Cdd:PRK11634 162 LR-MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVT-TRPDISQSYWTVWGMRKNEALVRF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   301 LDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAIN 380
Cdd:PRK11634 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6320119   381 YDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEdEEVLAKIQERFDVKIAE 432
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRE-RRLLRNIERTMKLTIPE 370
PTZ00110 PTZ00110
helicase; Provisional
57-412 1.97e-61

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 208.47  E-value: 1.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    57 VGIHSTGFKDFLLKpelsrAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVP------GE 130
Cdd:PTZ00110 130 VSFEYTSFPDYILK-----SLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllrygdGP 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   131 VaVVVICNARELAYQIRNEYLRFSKyMPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVK 210
Cdd:PTZ00110 205 I-VLVLAPTRELAEQIREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRR---GVEILIACPGRLIDFLESNVTNLRRVT 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   211 NFVIDECDKVLE---ELDMRRDVQEIfraTPrDKQVMMFSATLSQEIRPICRRFL-QNPLEIFVDDEAKLTLHGLQQYYI 286
Cdd:PTZ00110 280 YLVLDEADRMLDmgfEPQIRKIVSQI---RP-DRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTACHNIKQEVF 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   287 KLEEREKNRKLAQLLDDL--EFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTD 364
Cdd:PTZ00110 356 VVEEHEKRGKLKMLLQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATD 435
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 6320119   365 VFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSS 412
Cdd:PTZ00110 436 VASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
62-430 1.05e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 202.45  E-value: 1.05e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    62 TGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVP-----GEVAVV 134
Cdd:PRK01297  87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqTPPPkerymGEPRAL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   135 VICNARELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKDTapHIVVATPGRLKALVREKYIDLSHVKNFVI 214
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMDFDKQLKQLEARFC--DILVATPGRLLDFNQRGEVHLDMVEVMVL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   215 DECDKVLEeLDMRRDVQEIFRATPR--DKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKlTLHGLQQYYIKLEERE 292
Cdd:PRK01297 244 DEADRMLD-MGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENV-ASDTVEQHVYAVAGSD 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   293 KNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDI 372
Cdd:PRK01297 322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6320119   373 ERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFvSSKEDEEVLAKIQERFDVKI 430
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF-AGEDDAFQLPEIEELLGRKI 458
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
64-440 5.88e-58

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 197.34  E-value: 5.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLD--PVPGE----VAVVVIC 137
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItrQPHAKgrrpVRALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   138 NARELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDEC 217
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRG---GVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   218 DKVLeelDMR--RDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVddeAKLTLHGLQ--QYYIKLEEREK 293
Cdd:PRK10590 159 DRML---DMGfiHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV---ARRNTASEQvtQHVHFVDKKRK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   294 NRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIE 373
Cdd:PRK10590 233 RELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320119   374 RINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEdEEVLAKIQERFDVKIAEFPEEGIDP 440
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDE-HKLLRDIEKLLKKEIPRIAIPGYEP 378
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
66-269 5.74e-53

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: 176.36  E-value: 5.74e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   66 DFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQ 145
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  146 IRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKnkdTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEElD 225
Cdd:cd17939  81 IQKVVKALGDYM-GVKVHACIGGTSVREDRRKLQ---YGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR-G 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6320119  226 MRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIF 269
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
64-268 4.30e-52

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: 174.02  E-value: 4.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEE 223
Cdd:cd17940  81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQT---VHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  224 lDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17940 157 -DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
281-410 5.28e-51

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


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 168.45  E-value: 5.28e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  281 LQQYYIKLEEREKNRKL-AQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRI 359
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320119  360 CVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFV 410
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
75-265 1.21e-47

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: 162.05  E-value: 1.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   75 RAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFS 154
Cdd:cd17943   3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  155 KYMPDVKTAVFYGGTPISKDAELLKNkdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEElDMRRDVQEIF 234
Cdd:cd17943  83 KKLEGLKCEVFIGGTPVKEDKKKLKG----CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEG-SFQKDVNWIF 157
                       170       180       190
                ....*....|....*....|....*....|.
gi 6320119  235 RATPRDKQVMMFSATLSQEIRPICRRFLQNP 265
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKP 188
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
64-269 4.81e-47

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: 160.85  E-value: 4.81e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVR---EKYIDLSHVKNFVIDECDKV 220
Cdd:cd17955  81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKR---PHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6320119  221 LEElDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIF 269
Cdd:cd17955 157 LTG-SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
64-268 9.56e-47

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: 159.92  E-value: 9.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKnkdTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEE 223
Cdd:cd18046  81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQ---AGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  224 lDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd18046 157 -GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
64-410 4.58e-46

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 166.89  E-value: 4.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTL--------QQLDPVPGEVAVVv 135
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQRNPLAMV- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   136 ICNARELAYQIRNEYLRFSKYMPdVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVID 215
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQ---GVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   216 ECDKVLEElDMRRDVQEIFRATPRdKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTlHGLQQYYIKLEEREKNR 295
Cdd:PLN00206 278 EVDCMLER-GFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPN-KAVKQLAIWVETKQKKQ 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   296 KLAQLLDDLEFNQ--VIIFVKSTTRANELTKLLN-ASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDI 372
Cdd:PLN00206 355 KLFDILKSKQHFKppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 6320119   373 ERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFV 410
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
64-409 8.60e-46

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 167.05  E-value: 8.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL-------DPVPGEVAVVVI 136
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   137 CNARELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVRE-KYIDLSHVKNFVID 215
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQ---GVDVIIATPGRLIDYVKQhKVVSLHACEICVLD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   216 ECDKVLEeLDMRRDVQEIFRATPR--DKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEErEK 293
Cdd:PRK04537 167 EADRMFD-LGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADE-EK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   294 NRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIE 373
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 6320119   374 RINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISF 409
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
69-259 1.15e-43

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: 152.35  E-value: 1.15e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   69 LKPELSRAIIDCGFEHPSEVQQHTIPQSI-HGTDVLCQAKSGLGKTAVFVLSTLQQL-----DPVPGEVAVVVICNAREL 142
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  143 AYQIRNEYLRFSKYMPDVKTAVFYGGTpiSKDAELLKNKDTAPHIVVATPGRLKALVREKY--IDLSHVKNFVIDECDKV 220
Cdd:cd17964  81 ALQIAAEAKKLLQGLRKLRVQSAVGGT--SRRAELNRLRRGRPDILVATPGRLIDHLENPGvaKAFTDLDYLVLDEADRL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  221 leeLDM--RRDVQEIFRATP----RDKQVMMFSATLSQEIRPICR 259
Cdd:cd17964 159 ---LDMgfRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIAR 200
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
64-409 9.22e-43

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 155.90  E-value: 9.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVPGEVAV-----VVI 136
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVnqpraLIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   137 CNARELAYQIRNEYLRFSKyMPDVKTAVFYGGTPISKDAELLknkDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDE 216
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVL---ESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   217 CDKVLEeLDMRRDVQEIFRATPRDKQ--VMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKlTLHGLQQYYIKLEEREKN 294
Cdd:PRK04837 166 ADRMFD-LGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQK-TGHRIKEELFYPSNEEKM 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   295 RKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIER 374
Cdd:PRK04837 244 RLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPA 323
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 6320119   375 INLAINYDLTNEADQYLHRVGRAGRFGTKGLAISF 409
Cdd:PRK04837 324 VTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
73-269 3.66e-41

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: 145.09  E-value: 3.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVA---VVVICNARELAYQIRNE 149
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSKYMpDVKTAVFYGGTPISKDAELLKnkdTAPHIVVATPGRLKALVRE-KYIDLSHVKNFVIDECDKVLEElDMRR 228
Cdd:cd17947  81 LQQLAQFT-DITFALAVGGLSLKAQEAALR---ARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEE-GFAD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320119  229 DVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIF 269
Cdd:cd17947 156 ELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
64-268 6.78e-41

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


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 144.53  E-value: 6.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKYMpDVKTAVFYGGTPISKDaelLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLeE 223
Cdd:cd18045  81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDD---IRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML-N 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  224 LDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEXDc smart00487
DEAD-like helicases superfamily;
77-284 2.22e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 143.40  E-value: 2.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119      77 IIDCGFEHPSEVQQHTIPQSIHGT-DVLCQAKSGLGKTAVFVLSTLQQLDPVPGeVAVVVICNARELAYQIRNEYLRFSK 155
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG-GRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     156 YMPdVKTAVFYGGTPISKDAELLKNKDTapHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEElDMRRDVQEIFR 235
Cdd:smart00487  80 SLG-LKVVGLYGGDSKREQLRKLESGKT--DILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG-GFGDQLEKLLK 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 6320119     236 ATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIfvdDEAKLTLHGLQQY 284
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI---DVGFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
86-255 8.86e-40

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: 140.46  E-value: 8.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     86 SEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMpDVKTAVF 165
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    166 YGGTPISKDAELLKNkdtaPHIVVATPGRLKALVREKyIDLSHVKNFVIDECDKVLEElDMRRDVQEIFRATPRDKQVMM 245
Cdd:pfam00270  80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDM-GFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|
gi 6320119    246 FSATLSQEIR 255
Cdd:pfam00270 154 LSATLPRNLE 163
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
64-265 1.12e-39

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: 141.30  E-value: 1.12e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQldpvpgeVAVVVICNARELA 143
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKYM--PDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVL 221
Cdd:cd17938  74 EQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLES---GVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6320119  222 EElDMRRDVQEIFRATP----RDK--QVMMFSATL-SQEIRPICRRFLQNP 265
Cdd:cd17938 151 SQ-GNLETINRIYNRIPkitsDGKrlQVIVCSATLhSFEVKKLADKIMHFP 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
69-268 1.72e-39

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: 140.79  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   69 LKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTD--VLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQI 146
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  147 RNEYLRFSKYmPDVKTAVfyggtpISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDM 226
Cdd:cd17963  81 GEVVEKMGKF-TGVKVAL------AVPGNDVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGH 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  227 RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
64-268 2.40e-39

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: 140.53  E-value: 2.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELA 143
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  144 YQIRNEYLRFSKyMPDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLK-ALVREKYIDLSHVKNFVIDECDKVLe 222
Cdd:cd17954  82 QQISEQFEALGS-SIGLKSAVLVGGMDMMAQAIALAKK---PHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLL- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6320119  223 ELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
73-270 4.08e-39

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: 139.65  E-value: 4.08e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVPGEVAVVVICNARELAYQIRNEY 150
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  151 LRFSKYMPdVKTAVFYGGT-PISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLeELDMRRD 229
Cdd:cd17957  81 LKLSKGTG-LRIVLLSKSLeAKAKDGPKSITK---YDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF-EPGFREQ 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  230 VQEIFRA-TPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFV 270
Cdd:cd17957 156 TDEILAAcTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
64-270 1.42e-38

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: 139.16  E-value: 1.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVPGEVA--------V 133
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGRgrrkaypsA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  134 VVICNARELAYQIRNEYLRFSKYMPdVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFV 213
Cdd:cd17967  82 LILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLR---GCDILVATPGRLVDFIERGRISLSSIKFLV 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  214 IDECDKVLE---ELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNplEIFV 270
Cdd:cd17967 158 LDEADRMLDmgfEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKN--YIFL 215
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
69-265 2.92e-37

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: 135.02  E-value: 2.92e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   69 LKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL------DPVPGEVAVVVICNAREL 142
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  143 AYQIRNEYLRFSKYM-PDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYI-DLSHVKNFVIDECDKV 220
Cdd:cd17961  81 AQQVSKVLEQLTAYCrKDVRVVNLSASSSDSVQRALLAEK---PDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLV 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6320119  221 L----EEldmrrDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNP 265
Cdd:cd17961 158 LsygyEE-----DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
63-265 2.31e-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: 124.72  E-value: 2.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   63 GFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL---DPVPGeVAVVVICNA 139
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkahSPTVG-ARALILSPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  140 RELAYQIRNEYLRFSKYMpDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDK 219
Cdd:cd17959  81 RELALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASN---PDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6320119  220 vLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNP 265
Cdd:cd17959 157 -LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
75-268 1.09e-32

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: 122.68  E-value: 1.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   75 RAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL-----DPVPGEVAVVVICNARELAYQIRNE 149
Cdd:cd17960   3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIYEV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSKYMPD-VKTAVFYGGTPISKDAELLKNKdtAPHIVVATPGRLKALVREKY--IDLSHVKNFVIDECDKVLeELDM 226
Cdd:cd17960  83 LQSFLEHHLPkLKCQLLIGGTNVEEDVKKFKRN--GPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLL-DLGF 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  227 RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
73-268 6.16e-32

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: 120.60  E-value: 6.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTL------QQLDPVPGEVAVVViCNARELAYQI 146
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdqRELEKGEGPIAVIV-APTRELAQQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  147 RNEYLRFSKYMpDVKTAVFYGGtpISKdAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLeELDM 226
Cdd:cd17952  80 YLEAKKFGKAY-NLRVVAVYGG--GSK-WEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF-DMGF 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  227 RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17952 155 EYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
75-270 1.85e-31

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: 119.32  E-value: 1.85e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   75 RAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL-----DPVPGeVAVVVICNARELAYQIRNE 149
Cdd:cd17941   3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwTPEDG-LGALIISPTRELAMQIFEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSKYMpDVKTAVFYGGtpisKDAELLKNKDTAPHIVVATPGR-LKALVREKYIDLSHVKNFVIDECDKVLeELDMRR 228
Cdd:cd17941  82 LRKVGKYH-SFSAGLIIGG----KDVKEEKERINRMNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRIL-DMGFKE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  229 DVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFV 270
Cdd:cd17941 156 TLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
292-401 1.93e-31

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 116.16  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119    292 EKNRKLAQLLDDLEFNQVIIFVKSTTRAnELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGID 371
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 6320119    372 IERINLAINYDLTNEADQYLHRVGRAGRFG 401
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
80-270 9.48e-31

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: 119.30  E-value: 9.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   80 CGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVPG-------EVAVVVICNARELAYQIRNEY 150
Cdd:cd18052  61 AGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkEGLTAssfsevqEPQALIVAPTRELANQIFLEA 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  151 LRFSkYMPDVKTAVFYGGTPISKDA-ELLKnkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLE---ELDM 226
Cdd:cd18052 141 RKFS-YGTCIRPVVVYGGVSVGHQIrQIEK----GCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDmgfGPEI 215
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6320119  227 RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLqNPLEIFV 270
Cdd:cd18052 216 RKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL-KEDYLFL 258
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
73-268 1.18e-30

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: 116.88  E-value: 1.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLR 152
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  153 FSKYMPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEeLDMRRDVQE 232
Cdd:cd17962  81 LMKGLPPMKTALLVGGLPLPPQLYRLQQ---GVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK-MGFQQQVLD 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320119  233 IFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
76-268 3.43e-30

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: 116.71  E-value: 3.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   76 AIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQ----QLDPVPGEVAVVVICN-ARELAYQIRNEY 150
Cdd:cd17953  26 LIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRhikdQRPVKPGEGPIGLIMApTRELALQIYVEC 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  151 LRFSKYMpDVKTAVFYGGTPISKD-AELLKNKDtaphIVVATPGRLKALVRE---KYIDLSHVKNFVIDECDKVLeELDM 226
Cdd:cd17953 106 KKFSKAL-GLRVVCVYGGSGISEQiAELKRGAE----IVVCTPGRMIDILTAnngRVTNLRRVTYVVLDEADRMF-DMGF 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  227 RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17953 180 EPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
73-268 3.75e-30

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: 116.27  E-value: 3.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFV---LSTLQQLDPVPGEVA-----VVVICNARELAY 144
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLiplLVYISRLPPLDEETKddgpyALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  145 QIRNEYLRFSKYmPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVleeL 224
Cdd:cd17945  81 QIEEETQKFAKP-LGIRVVSIVGGHSIEEQAFSLRN---GCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRM---I 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320119  225 DM--RRDVQEIFRATP--------------------RDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17945 154 DMgfEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
60-264 6.64e-29

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: 113.60  E-value: 6.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   60 HSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL-DPVPGEVAV----- 133
Cdd:cd18051  19 HIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyEQGPGESLPsesgy 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  134 ----------VVICNARELAYQIRNEYLRFSkYMPDVKTAVFYGGTPISKDaelLKNKDTAPHIVVATPGRLKALVREKY 203
Cdd:cd18051  99 ygrrkqyplaLVLAPTRELASQIYDEARKFA-YRSRVRPCVVYGGADIGQQ---MRDLERGCHLLVATPGRLVDMLERGK 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320119  204 IDLSHVKNFVIDECDKVLE---ELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQN 264
Cdd:cd18051 175 IGLDYCKYLVLDEADRMLDmgfEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
77-268 4.45e-27

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: 107.46  E-value: 4.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   77 IIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTL------QQLDPVPGEVaVVVICNARELAYQIRNEY 150
Cdd:cd17966   5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERGDGPI-VLVLAPTRELAQQIQQEA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  151 LRFSKyMPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLE---ELDMR 227
Cdd:cd17966  84 NKFGG-SSRLRNTCVYGGAPKGPQIRDLRR---GVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDmgfEPQIR 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320119  228 RDVQEIfRAtprDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17966 160 KIVDQI-RP---DRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
76-269 5.64e-25

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: 101.39  E-value: 5.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   76 AIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLD--PVPGEV----AVVVICNARELAYQIRNE 149
Cdd:cd17958   4 EIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREQrngpGVLVLTPTRELALQIEAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSkyMPDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVleeLDMRRD 229
Cdd:cd17958  84 CSKYS--YKGLKSVCVYGGGNRNEQIEDLSKG---VDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM---LDMGFE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320119  230 VQ--EIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIF 269
Cdd:cd17958 156 PQirKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
75-271 5.27e-24

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: 98.97  E-value: 5.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   75 RAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQ-----QLDPVPGeVAVVVICNARELAYQIRNE 149
Cdd:cd17942   3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPRNG-TGVIIISPTRELALQIYGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSKYmpDVKT-AVFYGGTPISKDAELLKNkdtAPHIVVATPGRLkalvrekyidLSHVKN-----------FVIDEC 217
Cdd:cd17942  82 AKELLKY--HSQTfGIVIGGANRKAEAEKLGK---GVNILVATPGRL----------LDHLQNtkgflyknlqcLIIDEA 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320119  218 DKVLE---ELDMRrdvqEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPlEIFVD 271
Cdd:cd17942 147 DRILEigfEEEMR----QIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
HELICc smart00490
helicase superfamily c-terminal domain;
321-401 7.41e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 7.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119     321 ELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRF 400
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 6320119     401 G 401
Cdd:smart00490  82 G 82
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
64-265 1.78e-23

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: 97.48  E-value: 1.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHG--TDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARE 141
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  142 LAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELlknKDtapHIVVATPGR-LKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:cd18047  83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKI---SE---QIVIGTPGTvLDWCSKLKFIDPKKIKVFVLDEADVM 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  221 LEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNP 265
Cdd:cd18047 157 IATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
73-278 1.88e-23

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: 98.47  E-value: 1.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   73 LSRAIIDCGFEHPSEVQQHTIPQSIH-GTDVLCQAKSGLGKTAVF----VLSTLQQLDPVPGEVAV-----VVICNAREL 142
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFgipiLERLLSQKSSNGVGGKQkplraLILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  143 AYQIRNEYLRFSKYmPDVKTAVFYGGTPISKDAELLKNKdtaPHIVVATPGRLKALVRE--KYID-LSHVKNFVIDECDK 219
Cdd:cd17946  81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKR---PEIVVATPGRLWELIQEgnEHLAnLKSLRFLVLDEADR 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320119  220 VLEELDMrRDVQEIFRATPRD-------KQVMMFSATLSqEIRPICRRFLQNPLEIFVDDEAKLTL 278
Cdd:cd17946 157 MLEKGHF-AELEKILELLNKDragkkrkRQTFVFSATLT-LDHQLPLKLNSKKKKKKKEKKQKLEL 220
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
81-268 1.90e-23

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: 97.41  E-value: 1.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   81 GFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQ-------LDPVPGEVAV-VVICNARELAYQIRNEYLR 152
Cdd:cd17951   9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFaleqekkLPFIKGEGPYgLIVCPSRELARQTHEVIEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  153 FSKY-----MPDVKTAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVleeLDM- 226
Cdd:cd17951  89 YCKAlqeggYPQLRCLLCIGGMSVKEQLEVIRK---GVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM---IDMg 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6320119  227 -RRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17951 163 fEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
64-265 4.22e-20

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: 88.92  E-value: 4.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   64 FKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHG--TDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARE 141
Cdd:cd18048  20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  142 LAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKnkdtapHIVVATPGR-LKALVREKYIDLSHVKNFVIDECDKV 220
Cdd:cd18048 100 LALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA------QIVIGTPGTvLDWCFKLRLIDVTNISVFVLDEADVM 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320119  221 LEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNP 265
Cdd:cd18048 174 INVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
88-267 4.98e-20

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: 87.98  E-value: 4.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   88 VQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVA------VVVICNARELAYQIRNEYLRFSKYMpdvK 161
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKL---S 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  162 TAVFYGGTPISKDAELLKNkdtAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLeELDMRRDVQEI----FRAT 237
Cdd:cd17944  93 VACFYGGTPYQQQIFAIRN---GIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML-DMGFAEQVEEIlsvsYKKD 168
                       170       180       190
                ....*....|....*....|....*....|.
gi 6320119  238 PRDK-QVMMFSATLSQEIRPICRRFLQNPLE 267
Cdd:cd17944 169 SEDNpQTLLFSATCPDWVYNVAKKYMKSQYE 199
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
81-268 1.70e-19

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 86.49  E-value: 1.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   81 GFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVA------VVVICNARELAYQIRNEYLRFS 154
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  155 KYMPDVKTAVFYGGTpiSKDAE---LLK--NkdtaphIVVATPGR-LKALVREKYIDLSHVKNFVIDECDKVLEE----- 223
Cdd:cd17949  90 KPFHWIVPGYLIGGE--KRKSEkarLRKgvN------ILIATPGRlLDHLKNTQSFDVSNLRWLVLDEADRLLDMgfekd 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6320119  224 -------LDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd17949 162 itkilelLDDKRSKAGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
58-268 8.68e-19

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: 85.83  E-value: 8.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   58 GIHSTGFKDFLLKpelsrAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVP----GEVAV 133
Cdd:cd18050  63 AFHQANFPQYVMD-----VLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylerGDGPI 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  134 -VVICNARELAYQIRNEYLRFSKyMPDVKTAVFYGGTPiskDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNF 212
Cdd:cd18050 138 cLVLAPTRELAQQVQQVADDYGK-SSRLKSTCIYGGAP---KGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYL 213
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320119  213 VIDECDKVLE---ELDMRRDVQEIfraTPrDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd18050 214 VLDEADRMLDmgfEPQIRKIVDQI---RP-DRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
98-439 1.53e-18

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 88.16  E-value: 1.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   98 HGTDVLCQAKSGLGKT--AVFVLSTLQQLDPVpgevavVVICNARELAYQIRNEYLRFskympdVKTAVFYGGtpiskda 175
Cdd:COG1061  99 GGGRGLVVAPTGTGKTvlALALAAELLRGKRV------LVLVPRRELLEQWAEELRRF------LGDPLAGGG------- 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  176 ellkNKDTAPHIVVATPGRLKALVREKYIDlshvKNF---VIDEC--------DKVLEELDMRrdvqeiFR----ATP-- 238
Cdd:COG1061 160 ----KKDSDAPITVATYQSLARRAHLDELG----DRFglvIIDEAhhagapsyRRILEAFPAA------YRlgltATPfr 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  239 ---RDKQVMMF-----SATLSQEIRpicRRFLQNP--LEIFVDDEAKLTLH-----GLQQYYIKLEEReKNRKLAQLLDD 303
Cdd:COG1061 226 sdgREILLFLFdgivyEYSLKEAIE---DGYLAPPeyYGIRVDLTDERAEYdalseRLREALAADAER-KDKILRELLRE 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  304 L-EFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYD 382
Cdd:COG1061 302 HpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320119  383 LTNEADQYLHRVGRA---GRFGTKGLAISFVSSKED--EEVLAKIQERFDVKIAEFPEEGID 439
Cdd:COG1061 382 PTGSPREFIQRLGRGlrpAPGKEDALVYDFVGNDVPvlEELAKDLRDLAGYRVEFLDEEESE 443
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
82-268 5.96e-18

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: 82.75  E-value: 5.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   82 FEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVP----GEVAV-VVICNARELAYQIRN---EYLRF 153
Cdd:cd18049  44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflerGDGPIcLVLAPTRELAQQVQQvaaEYGRA 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  154 SKympdVKTAVFYGGTPiskDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLE---ELDMRRDV 230
Cdd:cd18049 124 CR----LKSTCIYGGAP---KGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDmgfEPQIRKIV 196
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320119  231 QEIfraTPrDKQVMMFSATLSQEIRPICRRFLQNPLEI 268
Cdd:cd18049 197 DQI---RP-DRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
81-250 2.49e-17

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: 80.87  E-value: 2.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   81 GFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQL--DPVPGEVA-----VVVICNARELAYQIRNEYLRF 153
Cdd:cd17948   9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaprGLVITPSRELAEQIGSVAQSL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  154 SKYMPdVKTAVFYGGtpisKDAELLKN-KDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEE--LDMrrdV 230
Cdd:cd17948  89 TEGLG-LKVKVITGG----RTKRQIRNpHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDsfNEK---L 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 6320119  231 QEIFRATP-------------RDKQVMMFSATL 250
Cdd:cd17948 161 SHFLRRFPlasrrsentdgldPGTQLVLVSATM 193
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
81-252 1.57e-16

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: 78.44  E-value: 1.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   81 GFEHPSEVQQHTIP---------QSIHGTDVLCQAKSGLGKTAVFVLSTLQQLD--PVPGEVAVVVIcNARELAYQIRNE 149
Cdd:cd17956   9 GITSAFPVQAAVIPwllpsskstPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSkrVVPRLRALIVV-PTKELVQQVYKV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  150 YLRFSKYMpDVKTAVFYGGTPISKDAELLKNK-----DTAPHIVVATPGRLKA-LVREKYIDLSHVKNFVIDE------- 216
Cdd:cd17956  88 FESLCKGT-GLKVVSLSGQKSFKKEQKLLLVDtsgryLSRVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDEadrllnq 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6320119  217 -----CDKVLEELDMRRDV---QEIFRAT----PRDKQVMMFSATLSQ 252
Cdd:cd17956 167 sfqdwLETVMKALGRPTAPdlgSFGDANLlersVRPLQKLLFSATLTR 214
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
99-249 2.54e-13

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 67.04  E-value: 2.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   99 GTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVavVVICNARELAYQIRNEYLRFSKymPDVKTAVFYGGtpiSKDAELL 178
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFG--PGIRVAVLVGG---SSAEERE 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320119  179 KNKDTAPHIVVATPGRL-KALVREKYIDLSHVKNFVIDECDKVL-EELDMRRDVQEIFRATPRDKQVMMFSAT 249
Cdd:cd00046  74 KNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLiDSRGALILDLAVRKAGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
286-426 8.95e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 57.46  E-value: 8.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  286 IKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDV 365
Cdd:COG0514 210 VPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIA 289
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320119  366 FGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSkEDEEvlakIQERF 426
Cdd:COG0514 290 FGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGP-EDVA----IQRFF 345
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
293-403 4.52e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 55.51  E-value: 4.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  293 KNRKLAQLLDD-LEFN---QVIIFVKSTTRANELTKLLNASNFPAITVHG--------HMKQEERIARYKAFKDFEKRIC 360
Cdd:COG1111 336 KLSKLREILKEqLGTNpdsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVL 415
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6320119  361 VSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTK 403
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREG 458
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
287-399 9.11e-08

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 51.20  E-value: 9.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  287 KLEEREKNR-KLAQLLDDlefNQVIIFVKSTTRANELTKLLNaSNFPAITVH---GH--------MKQEERIARYKAFKD 354
Cdd:cd18801  13 KLEEIVKEHfKKKQEGSD---TRVIIFSEFRDSAEEIVNFLS-KIRPGIRATrfiGQasgksskgMSQKEQKEVIEQFRK 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6320119  355 FEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGR 399
Cdd:cd18801  89 GGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
293-403 1.29e-07

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: 50.55  E-value: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  293 KNRKLAQLLDDLEFNQ--VIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRIC--VSTDVFGR 368
Cdd:cd18793  12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflLSTKAGGV 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6320119  369 GIDIERINLAINYDL----TNEaDQylhRVGRAGRFGTK 403
Cdd:cd18793  92 GLNLTAANRVILYDPwwnpAVE-EQ---AIDRAHRIGQK 126
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
140-399 1.88e-07

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: 52.95  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  140 RELAYqirneylRFSKYMPDVKTAVFYGGTPiskdaellkNKDTAPHIVVATPGRLkalVR-EKYIDLshvknFVIDE-- 216
Cdd:COG4098 171 LELAP-------RLQQAFPGVDIAALYGGSE---------EKYRYAQLVIATTHQL---LRfYQAFDL-----LIIDEvd 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  217 -----CDKVLE---ELDMRRDVQEIF-RATPRDKQVmmfsATLSQEIRPIC---RRFLQNPLeifvdDEAKL-TLHGLQQ 283
Cdd:COG4098 227 afpysGDPMLQyavKRARKPDGKLIYlTATPSKALQ----RQVKRGKLKVVklpARYHGHPL-----PVPKFkWLGNWKK 297
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  284 yyiKLEEREKNRKLAQLLDDL--EFNQVIIFVKSTTRANELTKLLnASNFPAITVHG-HMKQEERIARYKAFKDFEKRIC 360
Cdd:COG4098 298 ---RLRRGKLPRKLLKWLKKRlkEGRQLLIFVPTIELLEQLVALL-QKLFPEERIAGvHAEDPERKEKVQAFRDGEIPIL 373
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 6320119  361 VSTDVFGRGIDIERINLAINYdltneADqylHRV----------GRAGR 399
Cdd:COG4098 374 VTTTILERGVTFPNVDVAVLG-----AD---HPVfteaalvqiaGRVGR 414
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
286-401 6.32e-07

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: 48.36  E-value: 6.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  286 IKLEEREKNRKLAQLLDDLEFNQ------VIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRI 359
Cdd:cd18794   4 LFYSVRPKDKKDEKLDLLKRIKVehlggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQV 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6320119  360 CVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFG 401
Cdd:cd18794  84 IVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
240-403 1.48e-06

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: 50.12  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  240 DKQVMMFSATLSQEIRpicrRFLQNpLEIFVDDEAkLTLHGLQQYYIKLEEREKNRKLAQLLDDLEF----NQVIIFVKS 315
Cdd:cd09639 154 DVPILLMSATLPKFLK----EYAEK-IGYVEENEP-LDLKPNERAPFIKIESDKVGEISSLERLLEFikkgGSVAIIVNT 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  316 TTRANELTKLLNASN--FPAITVHGHMKQEERIARYK----AFKDFEKRICVSTDVFGRGIDIErINLAINyDLTnEADQ 389
Cdd:cd09639 228 VDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKEAelllEFKKSEKFVIVATQVIEASLDIS-VDVMIT-ELA-PIDS 304
                       170
                ....*....|....
gi 6320119  390 YLHRVGRAGRFGTK 403
Cdd:cd09639 305 LIQRLGRLHRYGEK 318
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
99-216 1.61e-06

DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 47.96  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   99 GTDVLCQAKSGLGKTAVFVLSTLQQL-DPVPGEVAVVVICNARELayqIRNEYLRFSKY----MPDVKTAVFYGGTPISK 173
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKAL---INDQERRLEEPldeiDLEIPVAVRHGDTSQSE 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6320119  174 DAELLKNkdtAPHIVVATPGRLKA-LVREKYI-DLSHVKNFVIDE 216
Cdd:cd17922  78 KAKQLKN---PPGILITTPESLELlLVNKKLReLFAGLRYVVVDE 119
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
359-410 2.41e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.00  E-value: 2.41e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 6320119  359 ICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTK-GLAISFV 410
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
99-322 4.44e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 48.74  E-value: 4.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   99 GTDVLCQAKSGLGKTAV---FVLSTLQQldpvPGEVavVVICNARELAYQIRNEYLR-FSKYmpDVKTAVFYGgtPISKD 174
Cdd:COG1204  38 GKNLVVSAPTASGKTLIaelAILKALLN----GGKA--LYIVPLRALASEKYREFKRdFEEL--GIKVGVSTG--DYDSD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  175 AELLKNKDtaphIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVleeLDMRR-----DVQEIFRATPRDKQVMMFSAT 249
Cdd:COG1204 108 DEWLGRYD----ILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLI---DDESRgptleVLLARLRRLNPEAQIVALSAT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  250 LS--QEI-------------RPIcrrflqnPLEIFVDDEAKLtlhglqqYYIKLEEREKNRKLAQLLDDLEFN-QVIIFV 313
Cdd:COG1204 181 IGnaEEIaewldaelvksdwRPV-------PLNEGVLYDGVL-------RFDDGSRRSKDPTLALALDLLEEGgQVLVFV 246

                ....*....
gi 6320119  314 KSTTRANEL 322
Cdd:COG1204 247 SSRRDAESL 255
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
282-403 1.11e-05

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 45.32  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  282 QQYYIKLEEREKNRKLAQLLDDLE-FNQVIIFVKSTTRANELTKLLNAsnfPAITvhGHMKQEERIARYKAFKDFEKRIC 360
Cdd:cd18789  24 KRRLLAAMNPNKLRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLK---PFIT--GETPQSEREEILQNFREGEYNTL 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6320119  361 VSTDVFGRGIDIERINLAI----NYDLTNEADQYLHRVGRAGRFGTK 403
Cdd:cd18789  99 VVSKVGDEGIDLPEANVAIqisgHGGSRRQEAQRLGRILRPKKGGGK 145
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
292-409 3.23e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 46.24  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   292 EKNRKLAQL---LDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGR 368
Cdd:PRK11057 219 EKFKPLDQLmryVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320119   369 GIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISF 409
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
218-401 5.13e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 45.60  E-value: 5.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  218 DKVLEELDmrrdvQEIFRATPRDKQVMMFSATLSQeirpicRRFLQNPlEIFVDDEAKLTLHGlqqyyIKLEEreknrkL 297
Cdd:COG0553 482 EAVLEYLR-----RELEGAEGIRRRGLILAALTRL------RQICSHP-ALLLEEGAELSGRS-----AKLEA------L 538
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  298 AQLLDDL--EFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFE--KRICVSTDVFGRGIDIE 373
Cdd:COG0553 539 LELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLT 618
                       170       180       190
                ....*....|....*....|....*....|.
gi 6320119  374 RINLAINYDLT-NEA--DQylhRVGRAGRFG 401
Cdd:COG0553 619 AADHVIHYDLWwNPAveEQ---AIDRAHRIG 646
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
109-242 8.63e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.41  E-value: 8.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  109 GLGKTAVFVL-----STLQQLDPVPGEVAVVViCNARELAYQiRNEYLRFSKympDVKTAVFYGGTPISK-DAELLKNKD 182
Cdd:cd18034  26 GSGKTLIAVMlikemGELNRKEKNPKKRAVFL-VPTVPLVAQ-QAEAIRSHT---DLKVGEYSGEMGVDKwTKERWKEEL 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  183 TAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQ 242
Cdd:cd18034 101 EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHPYARIMKEFYHLEGRTSR 160
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
310-377 9.43e-05

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: 41.78  E-value: 9.43e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320119  310 IIFVKSTTRANELTKLLNASNFPAITVHGHMKQEER---IARYKAFKDFEKRICVSTDVFGRGIDIERINL 377
Cdd:cd18799  10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDIPEVDN 80
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
293-397 1.94e-04

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: 41.42  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  293 KNRKLAQLLD--DLEFNQV-----IIFVKSTTRANELTKLL--NASNFPAITVH---GH----------MKQEERIARYK 350
Cdd:cd18802   5 VIPKLQKLIEilREYFPKTpdfrgIIFVERRATAVVLSRLLkeHPSTLAFIRCGfliGRgnssqrkrslMTQRKQKETLD 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6320119  351 AFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRA 397
Cdd:cd18802  85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRA 131
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
319-399 1.96e-04

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: 41.56  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  319 ANELTKLLNAsNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDltneADQY----LHRV 394
Cdd:cd18811  51 YEYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED----AERFglsqLHQL 125

                ....*.
gi 6320119  395 -GRAGR 399
Cdd:cd18811 126 rGRVGR 131
PRK13766 PRK13766
Hef nuclease; Provisional
281-399 2.53e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.32  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   281 LQQYYIKLEERE----KNRKLAQLL-DDLEFNQ---VIIFVKSTTRANELTKLLNASNFPAITVHG--------HMKQEE 344
Cdd:PRK13766 332 FRKAVRKAKELDiehpKLEKLREIVkEQLGKNPdsrIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKE 411
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6320119   345 RIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGR 399
Cdd:PRK13766 412 QIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR 466
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
109-216 6.76e-04

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 40.63  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  109 GLGKT--AVFVLSTLQQLDPVPGEVAVVVICNARElayQIRNEylrFSKYMPDVKTAVFYGGTPISKDAELLKNKDTApH 186
Cdd:cd17919  29 GLGKTlqAIAFLAYLLKEGKERGPVLVVCPLSVLE---NWERE---FEKWTPDLRVVVYHGSQRERAQIRAKEKLDKF-D 101
                        90       100       110
                ....*....|....*....|....*....|.
gi 6320119  187 IVVATPGRLKALVRE-KYIDLSHVknfVIDE 216
Cdd:cd17919 102 VVLTTYETLRRDKASlRKFRWDLV---VVDE 129
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
297-399 1.15e-03

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 39.17  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  297 LAQLLDDLEFNQ-VIIFVKSTTRANELTKLLN---ASNFPAITV---HGHMKQEERIARYKAFKDFEKRICVSTDVFGRG 369
Cdd:cd18796  28 YAEVIFLLERHKsTLVFTNTRSQAERLAQRLRelcPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
                        90       100       110
                ....*....|....*....|....*....|
gi 6320119  370 IDIERINLAINYDLTNEADQYLHRVGRAGR 399
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
102-252 1.31e-03

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 39.55  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  102 VLCqAKSGLGKTAVFVLSTLQQLDPVPGEVavVVICNARELAYQIRNE-YLRFSKYMPDVktAVFYGGTPISKDAELlkn 180
Cdd:cd17921  21 LVS-APTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADlRERFGPLGKNV--GLLTGDPSVNKLLLA--- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119  181 kdtAPHIVVATPGRLKALVR---EKYIDlsHVKNFVIDECDK--------VLEELdmrrdVQEIFRATPRDKQVMMfSAT 249
Cdd:cd17921  93 ---EADILVATPEKLDLLLRnggERLIQ--DVRLVVVDEAHLigdgergvVLELL-----LSRLLRINKNARFVGL-SAT 161

                ...
gi 6320119  250 LSQ 252
Cdd:cd17921 162 LPN 164
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
336-399 7.71e-03

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: 36.86  E-value: 7.71e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320119  336 VHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDltneADQY----LH----RVGRAGR 399
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED----ADRFglsqLHqlrgRVGRGKH 133
PRK13766 PRK13766
Hef nuclease; Provisional
103-217 8.06e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 38.70  E-value: 8.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320119   103 LCQAKSGLGKTAVFVLSTLQQLDPVPGEvaVVVICNARELAYQIRNEYLRFSKyMPDVKTAVFYGGTPISKDAELLKNKD 182
Cdd:PRK13766  33 LVVLPTGLGKTAIALLVIAERLHKKGGK--VLILAPTKPLVEQHAEFFRKFLN-IPEEKIVVFTGEVSPEKRAELWEKAK 109
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6320119   183 taphIVVATPGRLKALVREKYIDLSHVKNFVIDEC 217
Cdd:PRK13766 110 ----VIVATPQVIENDLIAGRISLEDVSLLIFDEA 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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