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Conserved domains on  [gi|446511155|ref|WP_000588613|]
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MULTISPECIES: DEAD/DEAH box helicase [Bacillus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

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

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
7-362 9.16e-145

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 417.24  E-value: 9.16e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEV-KQPQVVVLAPTRELVMQIHEE 85
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRELALQVAEE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQivkqkM--MG---A 160
Cdd:COG0513   91 LRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR-----MldMGfieD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 161 VQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESK-SLVEHTYIICERREKNDYVRRIMHMGDV-KAV 238
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATaETIEQRYYLVDKRDKLELLRRLLRDEDPeRAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 239 AFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQY 318
Cdd:COG0513  246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDY 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446511155 319 IHRSGRTGRMGKEGTVVSLVTPQEERKLLQFAKKLGIVFTKQEM 362
Cdd:COG0513  326 VHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
7-362 9.16e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 417.24  E-value: 9.16e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEV-KQPQVVVLAPTRELVMQIHEE 85
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRELALQVAEE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQivkqkM--MG---A 160
Cdd:COG0513   91 LRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR-----MldMGfieD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 161 VQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESK-SLVEHTYIICERREKNDYVRRIMHMGDV-KAV 238
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATaETIEQRYYLVDKRDKLELLRRLLRDEDPeRAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 239 AFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQY 318
Cdd:COG0513  246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDY 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446511155 319 IHRSGRTGRMGKEGTVVSLVTPQEERKLLQFAKKLGIVFTKQEM 362
Cdd:COG0513  326 VHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
9-200 8.62e-84

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: 253.52  E-value: 8.62e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPE----VKQPQVVVLAPTRELVMQIHE 84
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446511155 165 IKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
17-355 3.32e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 240.47  E-value: 3.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTE-I 95
Cdd:PRK11776  23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFIPnI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  96 SGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKqkmMG---AVQDVIKSTMRDR 172
Cdd:PRK11776 103 KVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD---MGfqdAIDAIIRQAPARR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 173 QLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEHTYIICERREKNDYVRRIM-HMGDVKAVAFLNDPFRLDEIT 251
Cdd:PRK11776 180 QTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLlHHQPESCVVFCNTKKECQEVA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 252 EKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKE 331
Cdd:PRK11776 260 DALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSK 339
                        330       340
                 ....*....|....*....|....
gi 446511155 332 GTVVSLVTPQEERKLLQFAKKLGI 355
Cdd:PRK11776 340 GLALSLVAPEEMQRANAIEDYLGR 363
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
22-187 1.04e-51

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: 170.12  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   22 TEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLI 101
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  102 GGADIKRQVEKLKKhPRVIVGSPGRILELIRMKKlKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVFFSATM 181
Cdd:pfam00270  81 GGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*.
gi 446511155  182 TKAAED 187
Cdd:pfam00270 159 PRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
13-212 1.58e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 152.65  E-value: 1.58e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155    13 WEKAGFKELTEIQKQAIPTILEG-QDVIAESPTGTGKTLAYLLPLLHKINPEvKQPQVVVLAPTRELVMQIHEEVQKFTA 91
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155    92 GTEISGASLIGGADIKRQVEKLKK-HPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMR 170
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446511155   171 DRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEH 212
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
cas3_cyano TIGR03158
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ...
42-192 2.97e-06

CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.


Pssm-ID: 274457 [Multi-domain]  Cd Length: 357  Bit Score: 48.74  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   42 SPTGTGKTLAYLLPLLHkinpevKQPQVVVLAPTRELVMQIHEEVQKFTAGTE---------ISGASLIGGADIKRQVEK 112
Cdd:TIGR03158  21 APTGAGKTLAWLTPLLH------GENDTIALYPTNALIEDQTEAIKEFVDVFKperdvnllhVSKATLKDIKEYANDKVG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  113 LKK---------------HPRVIVGSPG------RILELIRMKKLKMHE--VKTIVFDEF-----DQIVKQKMMGAVQDV 164
Cdd:TIGR03158  95 SSKgeklynllrnpigtsTPIILLTNPDifvyltRFAYIDRGDIAAGFYtkFSTVIFDEFhlydaKQLVGMLFLLAYMQL 174
                         170       180
                  ....*....|....*....|....*...
gi 446511155  165 IKSTMRDRQLVFFSATMTKAAEDAARDL 192
Cdd:TIGR03158 175 IRFFECRRKFVFLSATPDPALILRLQNA 202
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
7-362 9.16e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 417.24  E-value: 9.16e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEV-KQPQVVVLAPTRELVMQIHEE 85
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRELALQVAEE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQivkqkM--MG---A 160
Cdd:COG0513   91 LRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR-----MldMGfieD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 161 VQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESK-SLVEHTYIICERREKNDYVRRIMHMGDV-KAV 238
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATaETIEQRYYLVDKRDKLELLRRLLRDEDPeRAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 239 AFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQY 318
Cdd:COG0513  246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDY 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446511155 319 IHRSGRTGRMGKEGTVVSLVTPQEERKLLQFAKKLGIVFTKQEM 362
Cdd:COG0513  326 VHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
9-200 8.62e-84

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: 253.52  E-value: 8.62e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPE----VKQPQVVVLAPTRELVMQIHE 84
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446511155 165 IKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
17-355 3.32e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 240.47  E-value: 3.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTE-I 95
Cdd:PRK11776  23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFIPnI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  96 SGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKqkmMG---AVQDVIKSTMRDR 172
Cdd:PRK11776 103 KVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD---MGfqdAIDAIIRQAPARR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 173 QLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEHTYIICERREKNDYVRRIM-HMGDVKAVAFLNDPFRLDEIT 251
Cdd:PRK11776 180 QTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLlHHQPESCVVFCNTKKECQEVA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 252 EKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKE 331
Cdd:PRK11776 260 DALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSK 339
                        330       340
                 ....*....|....*....|....
gi 446511155 332 GTVVSLVTPQEERKLLQFAKKLGI 355
Cdd:PRK11776 340 GLALSLVAPEEMQRANAIEDYLGR 363
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
4-338 3.79e-69

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 224.05  E-value: 3.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   4 DMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLL-HKIN-PEVK--QPQVVVLAPTRELV 79
Cdd:PRK11192   7 ELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqHLLDfPRRKsgPPRILILTPTRELA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  80 MQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKqkmMG 159
Cdd:PRK11192  87 MQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD---MG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 160 AVQDV--IKSTMRDR-QLVFFSATMT-KAAEDAARDLAVEPQLVRVT--RAESKSLVEHTYIICERREKNDYVRRIMHMG 233
Cdd:PRK11192 164 FAQDIetIAAETRWRkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEpsRRERKKIHQWYYRADDLEHKTALLCHLLKQP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 234 DV-KAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELP 312
Cdd:PRK11192 244 EVtRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMP 323
                        330       340
                 ....*....|....*....|....*.
gi 446511155 313 DTVDQYIHRSGRTGRMGKEGTVVSLV 338
Cdd:PRK11192 324 RSADTYLHRIGRTGRAGRKGTAISLV 349
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
11-348 4.67e-62

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 210.47  E-value: 4.67e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  11 QAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFT 90
Cdd:PRK11634  19 EALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELAVQVAEAMTDFS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  91 AGTE-ISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTM 169
Cdd:PRK11634  99 KHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 170 RDRQLVFFSATMTKAAEDAARDLAVEPQLVRV-TRAESKSLVEHTYIICERREKNDYVRRIMHMGDVKA-VAFLNDPFRL 247
Cdd:PRK11634 179 EGHQTALFSATMPEAIRRITRRFMKEPQEVRIqSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAaIIFVRTKNAT 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 248 DEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGR 327
Cdd:PRK11634 259 LEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGR 338
                        330       340
                 ....*....|....*....|.
gi 446511155 328 MGKEGTVVsLVTPQEERKLLQ 348
Cdd:PRK11634 339 AGRAGRAL-LFVENRERRLLR 358
PTZ00110 PTZ00110
helicase; Provisional
8-352 2.29e-61

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 206.55  E-value: 2.29e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   8 FLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKIN--PEVKQ---PQVVVLAPTRELVMQI 82
Cdd:PTZ00110 140 YILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqPLLRYgdgPIVLVLAPTRELAEQI 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  83 HEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQ 162
Cdd:PTZ00110 220 REQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 163 DVIKSTMRDRQLVFFSATMTKAAEDAARDLAVE-PQLVRV---TRAESKSLVEHTYIICERREK---NDYVRRIMHMGDv 235
Cdd:PTZ00110 300 KIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgslDLTACHNIKQEVFVVEEHEKRgklKMLLQRIMRDGD- 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 236 KAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTV 315
Cdd:PTZ00110 379 KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQI 458
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 446511155 316 DQYIHRSGRTGRMGKEGTVVSLVTPQEER------KLLQFAKK 352
Cdd:PTZ00110 459 EDYVHRIGRTGRAGAKGASYTFLTPDKYRlardlvKVLREAKQ 501
PTZ00424 PTZ00424
helicase 45; Provisional
17-346 5.33e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 196.59  E-value: 5.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEIS 96
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  97 GASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVF 176
Cdd:PTZ00424 127 CHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVAL 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 177 FSATMTKAAEDAARDLAVEPQLVRVTRAE-SKSLVEHTYIICERRE-KNDYVRRIMH-MGDVKAVAFLNDPFRLDEITEK 253
Cdd:PTZ00424 207 FSATMPNEILELTTKFMRDPKRILVKKDElTLEGIRQFYVAVEKEEwKFDTLCDLYEtLTITQAIIYCNTRRKVDYLTKK 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 254 LKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGT 333
Cdd:PTZ00424 287 MHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGV 366
                        330
                 ....*....|...
gi 446511155 334 VVSLVTPQEERKL 346
Cdd:PTZ00424 367 AINFVTPDDIEQL 379
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
4-354 7.86e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 198.21  E-value: 7.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   4 DMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NPEVKQ-----PQVVVLAPTR 76
Cdd:PRK01297  93 NLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqTPPPKErymgePRALIIAPTR 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  77 ELVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLK-KHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQ 155
Cdd:PRK01297 173 ELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDM 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 156 KMMGAVQDVIKSTMR--DRQLVFFSATMTKAAEDAARDLAVEPQLVRV--TRAESKSLVEHTYIICERREKNDYVRRIMH 231
Cdd:PRK01297 253 GFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIepENVASDTVEQHVYAVAGSDKYKLLYNLVTQ 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 232 MGDVKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLEL 311
Cdd:PRK01297 333 NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTL 412
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 446511155 312 PDTVDQYIHRSGRTGRMGKEGTVVSLVTPQEERKLLQFAKKLG 354
Cdd:PRK01297 413 PEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLG 455
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
11-353 1.08e-58

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 197.34  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  11 QAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQVV---VLAPTRELVMQIHE 84
Cdd:PRK10590  14 RAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrQPHAKGRRPVralILTPTRELAAQIGE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKqkmMGAVQD- 163
Cdd:PRK10590  94 NVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD---MGFIHDi 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 164 --VIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKS--LVEHTYIICERReKNDYVRRIMHMGDVKAV- 238
Cdd:PRK10590 171 rrVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASeqVTQHVHFVDKKR-KRELLSQMIGKGNWQQVl 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 239 AFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQY 318
Cdd:PRK10590 250 VFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDY 329
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 446511155 319 IHRSGRTGRMGKEGTVVSLVTpQEERKLLQFAKKL 353
Cdd:PRK10590 330 VHRIGRTGRAAATGEALSLVC-VDEHKLLRDIEKL 363
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
4-337 9.26e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 187.08  E-value: 9.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   4 DMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---------NPEvkQPQVVVLAP 74
Cdd:PRK04537  15 DLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrKPE--DPRALILAP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  75 TRELVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKL-KMHEVKTIVFDEFDQIV 153
Cdd:PRK04537  93 TRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEADRMF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 154 KqkmMGAVQDvIKSTMR------DRQLVFFSATMTKAAEDAARDLAVEPQ-LVRVTRAESKSLVEHTYIICERREKNDYV 226
Cdd:PRK04537 173 D---LGFIKD-IRFLLRrmpergTRQTLLFSATLSHRVLELAYEHMNEPEkLVVETETITAARVRQRIYFPADEEKQTLL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 227 RRIMHMGD-VKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTH 305
Cdd:PRK04537 249 LGLLSRSEgARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446511155 306 VIHLELPDTVDQYIHRSGRTGRMGKEGTVVSL 337
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
7-348 1.58e-53

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 185.38  E-value: 1.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLL-------HKINPEVKQPQVVVLAPTRELV 79
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirSGHPSEQRNPLAMVLTPTRELC 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  80 MQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMG 159
Cdd:PLN00206 210 VQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRD 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 160 AVQDVIKStMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRV--TRAESKSlVEHTYIICERREKNDYVRRIMhMGDVK- 236
Cdd:PLN00206 290 QVMQIFQA-LSQPQVLLFSATVSPEVEKFASSLAKDIILISIgnPNRPNKA-VKQLAIWVETKQKKQKLFDIL-KSKQHf 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 237 ---AVAFLNDPFRLDEITEKL-KFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELP 312
Cdd:PLN00206 367 kppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP 446
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 446511155 313 DTVDQYIHRSGRTGRMGKEGTVVSLVTpQEERKLLQ 348
Cdd:PLN00206 447 NTIKEYIHQIGRASRMGEKGTAIVFVN-EEDRNLFP 481
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
22-187 1.04e-51

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: 170.12  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   22 TEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLI 101
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  102 GGADIKRQVEKLKKhPRVIVGSPGRILELIRMKKlKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVFFSATM 181
Cdd:pfam00270  81 GGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*.
gi 446511155  182 TKAAED 187
Cdd:pfam00270 159 PRNLED 164
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
210-338 4.32e-47

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: 156.90  E-value: 4.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 210 VEHTYIICERREKND--YVRRIMHMGDVKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEI 287
Cdd:cd18787    1 IKQLYVVVEEEEKKLllLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446511155 288 LLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVVSLV 338
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
5-337 1.16e-46

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 164.76  E-value: 1.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   5 MQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NP-----EVKQPQVVVLAPTRE 77
Cdd:PRK04837  15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPapedrKVNQPRALIMAPTRE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  78 LVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDqivkqKM 157
Cdd:PRK04837  95 LAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD-----RM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 158 --MGAVQDvIKSTMR------DRQLVFFSATMTKAAEDAARDLAVEPQLVRVT----------------RAESKSLVEHT 213
Cdd:PRK04837 170 fdLGFIKD-IRWLFRrmppanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEpeqktghrikeelfypSNEEKMRLLQT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 214 YIICERREkndyvrrimhmgdvKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDI 293
Cdd:PRK04837 249 LIEEEWPD--------------RAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446511155 294 AARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVVSL 337
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
14-202 5.19e-45

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: 153.90  E-value: 5.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQ--PQVVVLAPTRELVMQIHEEVQKFTA 91
Cdd:cd17957    6 EESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  92 GTEISGASLIGG-ADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKS-TM 169
Cdd:cd17957   86 GTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAAcTN 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446511155 170 RDRQLVFFSATMTKAAEDAARDLAVEPqlVRVT 202
Cdd:cd17957  166 PNLQRSLFSATIPSEVEELARSVMKDP--IRII 196
DEXDc smart00487
DEAD-like helicases superfamily;
13-212 1.58e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 152.65  E-value: 1.58e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155    13 WEKAGFKELTEIQKQAIPTILEG-QDVIAESPTGTGKTLAYLLPLLHKINPEvKQPQVVVLAPTRELVMQIHEEVQKFTA 91
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155    92 GTEISGASLIGGADIKRQVEKLKK-HPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMR 170
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446511155   171 DRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEH 212
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
4-191 7.76e-44

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: 151.49  E-value: 7.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   4 DMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NP--------EVKQPQVVVLA 73
Cdd:cd17967    6 GLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGppsvgrgrRKAYPSALILA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  74 PTRELVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDqiv 153
Cdd:cd17967   86 PTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEAD--- 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446511155 154 kqKM--MGAVQDVIK----STM---RDRQLVFFSATMTKAAEDAARD 191
Cdd:cd17967  163 --RMldMGFEPQIRKivehPDMppkGERQTLMFSATFPREIQRLAAD 207
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
7-200 2.00e-43

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: 150.15  E-value: 2.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQV--VVLAPTRELVMQIHE 84
Cdd:cd17959   10 PPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGAraLILSPTRELALQTLK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd17959   90 VTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEI 169
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446511155 165 IKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd17959  170 LSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
17-190 2.69e-42

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: 146.63  E-value: 2.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGT 93
Cdd:cd17947    9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  94 EISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIR-MKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDR 172
Cdd:cd17947   89 DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELKEILRLCPRTR 168
                        170
                 ....*....|....*...
gi 446511155 173 QLVFFSATMTKAAEDAAR 190
Cdd:cd17947  169 QTMLFSATMTDEVKDLAK 186
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
9-202 4.53e-42

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: 146.41  E-value: 4.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NPEVKQ---PQVVVLAPTRELVMQIH 83
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKgegPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  84 EEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQD 163
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446511155 164 VIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPqlVRVT 202
Cdd:cd17952  161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDP--IRVV 197
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
6-184 4.08e-41

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: 143.90  E-value: 4.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   6 QPFLQQAWeKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEE 85
Cdd:cd17955    8 SWLVKQCA-SLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELAYQIAEQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIR---MKKLKMHEVKTIVFDEFDQIVKQKMMGAVQ 162
Cdd:cd17955   87 FRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSFEDDLA 166
                        170       180
                 ....*....|....*....|..
gi 446511155 163 DVIKSTMRDRQLVFFSATMTKA 184
Cdd:cd17955  167 TILSALPPKRQTLLFSATLTDA 188
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
5-190 5.19e-41

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: 143.64  E-value: 5.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   5 MQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHE 84
Cdd:cd17950    9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAG-TEISGASLIGGADIKRQVEKLK-KHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQ-KMMGAV 161
Cdd:cd17950   89 EYERFSKYmPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlDMRRDV 168
                        170       180
                 ....*....|....*....|....*....
gi 446511155 162 QDVIKSTMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17950  169 QEIFRATPHDKQVMMFSATLSKEIRPVCK 197
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
7-183 6.93e-41

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: 143.23  E-value: 6.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKInpeVKQPQ---VVVLAPTRELVMQIH 83
Cdd:cd17954    9 EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPTRELAQQIS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  84 EEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILE-LIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQ 162
Cdd:cd17954   86 EQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDFEPEID 165
                        170       180
                 ....*....|....*....|.
gi 446511155 163 DVIKSTMRDRQLVFFSATMTK 183
Cdd:cd17954  166 KILKVIPRERTTYLFSATMTT 186
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
9-196 1.01e-40

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: 143.67  E-value: 1.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NPEVKQ---PQVVVLAPTRELVMQIH 83
Cdd:cd17953   23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPgegPIGLIMAPTRELALQIY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  84 EEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRM---KKLKMHEVKTIVFDEFDQIVKQKMMGA 160
Cdd:cd17953  103 VECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTNLRRVTYVVLDEADRMFDMGFEPQ 182
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446511155 161 VQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEP 196
Cdd:cd17953  183 IMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
14-190 1.42e-39

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: 140.53  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKIN-----PEVKQ---PQVVVLAPTRELVMQIHEE 85
Cdd:cd17945    6 RKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlpplDEETKddgPYALILAPTRELAQQIEEE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVI 165
Cdd:cd17945   86 TQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKIL 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446511155 166 KS--------------------TMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17945  166 DAmpvsnkkpdteeaeklaasgKHRYRQTMMFTATMPPAVEKIAK 210
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
9-190 5.38e-39

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: 138.09  E-value: 5.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQV--VVLAPTRELVMQIH 83
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQVgaLIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  84 EEVQKFTA--GTEISGASLIGGADIKRQVEKLKKH-PRVIVGSPGRILELIRMK--KLKMHEVKTIVFDEFDQIVKqkmM 158
Cdd:cd17960   81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLD---L 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446511155 159 G---AVQDVIKSTMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17960  158 GfeaDLNRILSKLPKQRRTGLFSATQTDAVEELIK 192
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
14-200 7.96e-39

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: 137.40  E-value: 7.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKF-TAG 92
Cdd:cd17943    6 KAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIgKKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  93 TEISGASLIGGADIKRQVEKLKKhPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDR 172
Cdd:cd17943   86 EGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNK 164
                        170       180
                 ....*....|....*....|....*...
gi 446511155 173 QLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd17943  165 QVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
16-180 1.23e-38

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: 137.43  E-value: 1.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  16 AGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEI 95
Cdd:cd17940   17 KGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELALQTSQVCKELGKHMGV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  96 SGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLV 175
Cdd:cd17940   97 KVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPKERQIL 176

                 ....*
gi 446511155 176 FFSAT 180
Cdd:cd17940  177 LFSAT 181
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
14-202 1.70e-37

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: 134.21  E-value: 1.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGT 93
Cdd:cd17962    6 KKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  94 -EISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDR 172
Cdd:cd17962   86 pPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDH 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 446511155 173 QLVFFSATMTKAAEDAARDLAVEPqlVRVT 202
Cdd:cd17962  166 QTILVSATIPRGIEQLAGQLLQNP--VRIT 193
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
17-183 2.62e-37

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: 133.60  E-value: 2.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEIS 96
Cdd:cd17939   16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  97 GASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVF 176
Cdd:cd17939   96 VHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVVL 175

                 ....*..
gi 446511155 177 FSATMTK 183
Cdd:cd17939  176 FSATMPH 182
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
15-196 1.08e-36

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: 132.11  E-value: 1.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  15 KAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKIN--PEVKQ---PQVVVLAPTRELVMQIHEEVQKF 89
Cdd:cd17966    7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaqPPLERgdgPIVLVLAPTRELAQQIQQEANKF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  90 TAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTM 169
Cdd:cd17966   87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIR 166
                        170       180
                 ....*....|....*....|....*..
gi 446511155 170 RDRQLVFFSATMTKAAEDAARDLAVEP 196
Cdd:cd17966  167 PDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
10-190 1.80e-36

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: 131.64  E-value: 1.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  10 QQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQ----VVVLAPTRELVMQIHEE 85
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLkKHPRVIVGSPGRILE-LIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd17941   82 LRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
                        170       180
                 ....*....|....*....|....*.
gi 446511155 165 IKSTMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17941  161 VENLPKSRQTLLFSATQTKSVKDLAR 186
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
7-193 3.92e-36

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: 130.39  E-value: 3.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEG--QDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHE 84
Cdd:cd17963    3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQvEKLKKHprVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd17963   83 VVEKMGKFTGVKVALAVPGNDVPRG-KKITAQ--IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGHGDQSIR 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 446511155 165 IKSTMRDR-QLVFFSATMTKAAEDAARDLA 193
Cdd:cd17963  160 IKRMLPRNcQILLFSATFPDSVRKFAEKIA 189
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
17-181 2.20e-35

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: 128.72  E-value: 2.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEIS 96
Cdd:cd18046   18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQIQKVVMALGDYMGIK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  97 GASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVF 176
Cdd:cd18046   98 CHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDTQVVL 177

                 ....*
gi 446511155 177 FSATM 181
Cdd:cd18046  178 LSATM 182
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
10-190 2.62e-35

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: 128.63  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  10 QQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQ----VVVLAPTRELVMQIHEE 85
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKM-HEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd17942   82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIGFEEEMRQI 161
                        170       180
                 ....*....|....*....|....*.
gi 446511155 165 IKSTMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17942  162 IKLLPKRRQTMLFSATQTRKVEDLAR 187
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
14-180 3.53e-35

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: 130.09  E-value: 3.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLL-----HKINP----EVKQPQVVVLAPTRELVMQIHE 84
Cdd:cd18052   59 RKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLtgmmkEGLTAssfsEVQEPQALIVAPTRELANQIFL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDV 164
Cdd:cd18052  139 EARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKL 218
                        170       180
                 ....*....|....*....|
gi 446511155 165 I-KSTM---RDRQLVFFSAT 180
Cdd:cd18052  219 VsEPGMpskEDRQTLMFSAT 238
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
5-190 6.76e-35

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: 127.70  E-value: 6.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   5 MQPFLQQAWEKAGFKELTEIQKQAIPTILE-GQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQV--VVLAPTREL 78
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntKPAGRRSGVsaLIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  79 VMQIHEEVQKFTAG-TEISGASLIGGADIKRQVEKLKKH-PRVIVGSPGRILELIR--MKKLKMHEVKTIVFDEFDQIVK 154
Cdd:cd17964   81 ALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRGrPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446511155 155 QKMMGAVQDVI----KSTMRDRQLVFFSATMTKAAEDAAR 190
Cdd:cd17964  161 MGFRPDLEQILrhlpEKNADPRQTLLFSATVPDEVQQIAR 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
11-184 1.04e-34

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: 128.13  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  11 QAWEKAGFKELTEIQKQAIP-TILEGQDVIAESPTGTGKTLAYLLPLLHKI---------NPEVKQPQVVVLAPTRELVM 80
Cdd:cd17946    3 RALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTRELAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  81 QIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKL---KMHEVKTIVFDEFDQIVK--- 154
Cdd:cd17946   83 QVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEkgh 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446511155 155 ----QKMMGAVQDVIKSTMRDRQLVFFSATMTKA 184
Cdd:cd17946  163 faelEKILELLNKDRAGKKRKRQTFVFSATLTLD 196
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
7-183 3.79e-34

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 125.77  E-value: 3.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   7 PFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI------NPEVKQPQVVVLAPTRELVM 80
Cdd:cd17961    3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  81 QIHEEVQKFTA--GTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHE-VKTIVFDEFDQIVKQKM 157
Cdd:cd17961   83 QVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGY 162
                        170       180
                 ....*....|....*....|....*.
gi 446511155 158 MGAVQDVIKSTMRDRQLVFFSATMTK 183
Cdd:cd17961  163 EEDLKSLLSYLPKNYQTFLMSATLSE 188
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
14-199 2.40e-32

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: 120.65  E-value: 2.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLP----LLHKINPEVKQ--PQVVVLAPTRELVMQIHEEVQ 87
Cdd:cd17958    6 KKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRngPGVLVLTPTRELALQIEAECS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  88 KFTAgTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKS 167
Cdd:cd17958   86 KYSY-KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLD 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446511155 168 TMRDRQLVFFSATMTKAAEDAARDLAVEPQLV 199
Cdd:cd17958  165 IRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
15-199 4.83e-32

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: 120.14  E-value: 4.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  15 KAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPL-LHKINPEVKQPQV-------VVLAPTRELVMQIHEEV 86
Cdd:cd17951    7 KKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIkgegpygLIVCPSRELARQTHEVI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  87 QKFTAGTEISGAS------LIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGA 160
Cdd:cd17951   87 EYYCKALQEGGYPqlrcllCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEED 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446511155 161 VQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLV 199
Cdd:cd17951  167 IRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
14-200 6.42e-32

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: 120.00  E-value: 6.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQ---VVVLAPTRELVMQIHEEVQ 87
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVDRSDgtlALVLVPTRELALQIYEVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  88 KFT-AGTEISGASLIGGAdiKRQVEK--LKKHPRVIVGSPGRILELIRM-KKLKMHEVKTIVFDEFDQIVKqkmMGAVQD 163
Cdd:cd17949   87 KLLkPFHWIVPGYLIGGE--KRKSEKarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLD---MGFEKD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446511155 164 V--IKSTMRD--------------RQLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd17949  162 ItkILELLDDkrskaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
17-183 1.34e-30

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: 116.03  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEIS 96
Cdd:cd18045   18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGDYMNVQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  97 GASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVF 176
Cdd:cd18045   98 CHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVL 177

                 ....*..
gi 446511155 177 FSATMTK 183
Cdd:cd18045  178 VSATLPQ 184
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
22-191 2.22e-30

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: 116.68  E-value: 2.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  22 TEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI---NPEVKQPQV-------------VVLAPTRELVMQIHEE 85
Cdd:cd18051   45 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSEsgyygrrkqyplaLVLAPTRELASQIYDE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  86 VQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFD------------QIV 153
Cdd:cd18051  125 ARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADrmldmgfepqirRIV 204
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446511155 154 KQKMMGAvqdvikstMRDRQLVFFSATMTKAAEDAARD 191
Cdd:cd18051  205 EQDTMPP--------TGERQTLMFSATFPKEIQMLARD 234
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
5-181 6.05e-30

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: 114.34  E-value: 6.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   5 MQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKInpevkqpQVVVLAPTRELVMQIHE 84
Cdd:cd17938    6 VMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELAEQTYN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  85 EVQKFTA---GTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQkmmgAV 161
Cdd:cd17938   79 CIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ----GN 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 446511155 162 QDVI--------KSTMRDR--QLVFFSATM 181
Cdd:cd17938  155 LETInriynripKITSDGKrlQVIVCSATL 184
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
9-186 1.29e-29

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: 114.27  E-value: 1.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQ---------DVIAESPTGTGKTLAYLLPLLHKINPE-VKQPQVVVLAPTREL 78
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRvVPRLRALIVVPTKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  79 VMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKH--------PRVIVGSPGRILELIRMKK-LKMHEVKTIVFDEF 149
Cdd:cd17956   81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLVIDEA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446511155 150 DQIVKQKMMGAVQDVIKSTMRDR--------------------QLVFFSATMTKAAE 186
Cdd:cd17956  161 DRLLNQSFQDWLETVMKALGRPTapdlgsfgdanllersvrplQKLLFSATLTRDPE 217
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
15-192 8.71e-27

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: 106.63  E-value: 8.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  15 KAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKIN--PEVKQ---PQVVVLAPTRELVMQIHEEVQKF 89
Cdd:cd18049   41 RQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqPFLERgdgPICLVLAPTRELAQQVQQVAAEY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  90 TAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTM 169
Cdd:cd18049  121 GRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 200
                        170       180
                 ....*....|....*....|...
gi 446511155 170 RDRQLVFFSATMTKAAEDAARDL 192
Cdd:cd18049  201 PDRQTLMWSATWPKEVRQLAEDF 223
HELICc smart00490
helicase superfamily c-terminal domain;
248-329 1.40e-26

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 101.52  E-value: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   248 DEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGR 327
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 446511155   328 MG 329
Cdd:smart00490  81 AG 82
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
18-191 2.14e-26

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: 106.63  E-value: 2.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  18 FKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKIN--PEVKQ---PQVVVLAPTRELVMQIHEEVQKFTAG 92
Cdd:cd18050   82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERgdgPICLVLAPTRELAQQVQQVADDYGKS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  93 TEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDR 172
Cdd:cd18050  162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
                        170       180
                 ....*....|....*....|...
gi 446511155 173 QLVFFSATMTKA----AEDAARD 191
Cdd:cd18050  242 QTLMWSATWPKEvrqlAEDFLRD 264
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
9-187 1.06e-25

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: 103.60  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI-----NPEVK--QPQVVVLAPTRELVMQ 81
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlryklLAEGPfnAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  82 IHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAV 161
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446511155 162 QDVIKST-------------MRDRQLVFFSATMTKAAED 187
Cdd:cd17948  161 SHFLRRFplasrrsentdglDPGTQLVLVSATMPSGVGE 199
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
17-180 2.75e-25

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: 101.85  E-value: 2.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQ------PQVVVLAPTRELVMQIHEEVQKFT 90
Cdd:cd17944    9 GVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPrkrgraPKVLVLAPTRELANQVTKDFKDIT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  91 agTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVI----- 165
Cdd:cd17944   89 --RKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsyk 166
                        170
                 ....*....|....*
gi 446511155 166 KSTMRDRQLVFFSAT 180
Cdd:cd17944  167 KDSEDNPQTLLFSAT 181
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
221-329 6.67e-25

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: 97.67  E-value: 6.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  221 EKNDYVRRIMHMGDV-KAVAFLNDPFRLDEitEKLKFRK-MKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGI 298
Cdd:pfam00271   1 EKLEALLELLKKERGgKVLIFSQTKKTLEA--ELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 446511155  299 DIDDLTHVIHLELPDTVDQYIHRSGRTGRMG 329
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
17-205 7.91e-22

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: 93.16  E-value: 7.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEG--QDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQ---IHEEVQKFTA 91
Cdd:cd18048   37 GFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFELALQtgkVVEEMGKFCV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  92 GTE----ISGASLIGGADIKRQveklkkhprVIVGSPGRILE-LIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIK 166
Cdd:cd18048  117 GIQviyaIRGNRPGKGTDIEAQ---------IVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMINVQGHSDHSVRVK 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446511155 167 STM-RDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAE 205
Cdd:cd18048  188 RSMpKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEE 227
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
35-180 4.46e-19

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: 82.84  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  35 GQDVIAESPTGTGKTLAYLLPLLHKINPevKQPQVVVLAPTRELVMQIHEEVQKFtAGTEISGASLIGGADIKRQVEKLK 114
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKL 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446511155 115 KHPRVIVGSPGRILELI-RMKKLKMHEVKTIVFDEFDQIVK--QKMMGAVQDVIKSTMRDRQLVFFSAT 180
Cdd:cd00046   78 GDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIdsRGALILDLAVRKAGLKNAQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
5-200 3.42e-18

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: 82.08  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   5 MQPFLQQAWEKAGFKELTEIQKQAIPTILEG--QDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQ- 81
Cdd:cd18047    8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQt 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  82 --IHEEVQKFTAgtEISGASLIGGADIKRQVeklKKHPRVIVGSPGRILE-LIRMKKLKMHEVKTIVFDEFD-QIVKQKM 157
Cdd:cd18047   88 gkVIEQMGKFYP--ELKLAYAVRGNKLERGQ---KISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADvMIATQGH 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446511155 158 MGAVQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVR 200
Cdd:cd18047  163 QDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
25-353 1.10e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 81.61  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  25 QKQAIPTIL-----EGQDVIAESPTGTGKTLAYLLpLLHKInpeVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGAS 99
Cdd:COG1061   85 QQEALEALLaalerGGGRGLVVAPTGTGKTVLALA-LAAEL---LRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGGK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 100 LIGGADI----------KRQVEKLKKHPRVIV-------GSPG--RILELIRMKKL-------KMHEVKTIVFDEFDQIV 153
Cdd:COG1061  161 KDSDAPItvatyqslarRAHLDELGDRFGLVIideahhaGAPSyrRILEAFPAAYRlgltatpFRSDGREILLFLFDGIV 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 154 kqkmmgavqdvikstmrdrqlvfFSATMTKAAEDAA-RDLAVEPQLVRVTR-----AESKSLVEHTYIICERReKNDYVR 227
Cdd:COG1061  241 -----------------------YEYSLKEAIEDGYlAPPEYYGIRVDLTDeraeyDALSERLREALAADAER-KDKILR 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 228 RIM--HMGDVKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTH 305
Cdd:COG1061  297 ELLreHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446511155 306 VIHLELPDTVDQYIHRSGR---TGRMGKEGTVVSLVTPQEERkLLQFAKKL 353
Cdd:COG1061  377 AILLRPTGSPREFIQRLGRglrPAPGKEDALVYDFVGNDVPV-LEELAKDL 426
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
22-202 6.21e-16

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 76.65  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  22 TEIQKQAIPTILE------GQDVIAESP----------TGTGKTLAYLLPLLHKI---------------NPEVK--QPQ 68
Cdd:cd17965   32 SPIQTLAIKKLLKtlmrkvTKQTSNEEPklevfllaaeTGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyESAKDtgRPR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  69 VVVLAPTRELVMQIHEEVQKF--TAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILEL--IRMKKLKmhEVKTI 144
Cdd:cd17965  112 SVILVPTHELVEQVYSVLKKLshTVKLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLakSRPKILS--RVTHL 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446511155 145 VFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAvePQLVRVT 202
Cdd:cd17965  190 VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF--PDVVRIA 245
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
4-335 1.37e-15

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 78.34  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   4 DMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKI--NPEVKqpqVVVLAPTRELvmq 81
Cdd:COG1205   40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALleDPGAT---ALYLYPTKAL--- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  82 IHEEVQKFTA-----GTEISGASLIGgaDIKRQV-EKLKKHPRVIVGSP--------------GRILElirmkklkmhEV 141
Cdd:COG1205  114 ARDQLRRLRElaealGLGVRVATYDG--DTPPEErRWIREHPDIVLTNPdmlhygllphhtrwARFFR----------NL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 142 KTIVFDE-------FdqivkqkmmGA-VQDVIKSTMR-------DRQLVFFSATMTKAAEDAARDLAVEPQLV------- 199
Cdd:COG1205  182 RYVVIDEahtyrgvF---------GShVANVLRRLRRicrhygsDPQFILASATIGNPAEHAERLTGRPVTVVdedgspr 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 200 -RVTRAesksLVEH-TYIICERREKNDYVRRIMHM---GDVKAVAF-------------LNDPFRLDEITEKLkfrkmka 261
Cdd:COG1205  253 gERTFV----LWNPpLVDDGIRRSALAEAARLLADlvrEGLRTLVFtrsrrgaellaryARRALREPDLADRV------- 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446511155 262 AALHAEASKQEREATMRAFRGGKLEILLATDiaA--RGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVV 335
Cdd:COG1205  322 AAYRAGYLPEERREIERGLRSGELLGVVSTN--AleLGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
9-345 1.15e-14

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 75.32  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWEKAGFKELTEIQKQAIP-TILEGQDVIAESPTGTGKTLAYLLPLLHKINpevKQPQVVVLAPTRELVMQIHEEVQ 87
Cdd:COG1204   11 VIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALL---NGGKALYIVPLRALASEKYREFK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  88 KFTAGTEISGASLIGGADIKRqvEKLKKhPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFdQIVKQKMMGAVQDVIKS 167
Cdd:COG1204   88 RDFEELGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLIDDESRGPTLEVLLA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 168 TMRDR----QLVFFSATMtKAAEDAARDLAVEP-----------------------QLVRVTRAESKSLVEHTY------ 214
Cdd:COG1204  164 RLRRLnpeaQIVALSATI-GNAEEIAEWLDAELvksdwrpvplnegvlydgvlrfdDGSRRSKDPTLALALDLLeeggqv 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 215 -IICERR-------EK-NDYVRRIMHMGDVKAVAFLNDPFRL--DEITEKLKFRKM---KAAALHAEASKQEREATMRAF 280
Cdd:COG1204  243 lVFVSSRrdaeslaKKlADELKRRLTPEEREELEELAEELLEvsEETHTNEKLADClekGVAFHHAGLPSELRRLVEDAF 322
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446511155 281 RGGKLEILLATD-IA------ARGIDIDDLTHVIHLELPdtVDQYIHRSGRTGRMGKE--GTVVSLVTPQEERK 345
Cdd:COG1204  323 REGLIKVLVATPtLAagvnlpARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGYDpyGEAILVAKSSDEAD 394
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
20-195 5.26e-14

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: 69.60  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  20 ELTEIQKQAIPTILEGQD-VIAESPTGTGKTLAYLLPLLHKINpevKQPQVVV-LAPTRELVMQIHEEVQKFTAGTEISG 97
Cdd:cd17921    1 LLNPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALA---TSGGKAVyIAPTRALVNQKEADLRERFGPLGKNV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  98 ASLIGGADIKRQvekLKKHPRVIVGSPGRILELIR-MKKLKMHEVKTIVFDEFdQIVKQKMMGAVQDVIKSTMRDR---- 172
Cdd:cd17921   78 GLLTGDPSVNKL---LLAEADILVATPEKLDLLLRnGGERLIQDVRLVVVDEA-HLIGDGERGVVLELLLSRLLRInkna 153
                        170       180
                 ....*....|....*....|...
gi 446511155 173 QLVFFSATmTKAAEDAARDLAVE 195
Cdd:cd17921  154 RFVGLSAT-LPNAEDLAEWLGVE 175
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
36-148 6.13e-12

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: 64.21  E-value: 6.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  36 QDVIAESPTGTGKTL--AYLLPLLHKINPEVKQP--QVVVLAPTRELVMQIHEEVQKFTAGT--EISGASLIGGADIKRQ 109
Cdd:cd18034   17 RNTIVVLPTGSGKTLiaVMLIKEMGELNRKEKNPkkRAVFLVPTVPLVAQQAEAIRSHTDLKvgEYSGEMGVDKWTKERW 96
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446511155 110 VEKLKKHpRVIVGSPGRILELIRMKKLKMHEVKTIVFDE 148
Cdd:cd18034   97 KEELEKY-DVLVMTAQILLDALRHGFLSLSDINLLIFDE 134
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
248-350 9.04e-12

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 66.32  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 248 DEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATdIA-ARGIDIDDLTHVIHLELPDTVDQYIHRSGRTG 326
Cdd:COG0514  244 EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
                         90       100
                 ....*....|....*....|....
gi 446511155 327 RMGKEGTVVSLVTPQEERKLLQFA 350
Cdd:COG0514  323 RDGLPAEALLLYGPEDVAIQRFFI 346
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
20-189 2.70e-09

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 56.19  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  20 ELTEIQKQAIPT-ILEGQDVIAESPTGTGKTLAYLLPLLHKInpeVKQPQVVVLAPTRELVMQIHEEVQKFtagTEISGA 98
Cdd:cd18028    1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTL---LEGGKALYLVPLRALASEKYEEFKKL---EEIGLK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  99 SLIGGADIKRQVEKLKKHPrVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKmMGAVQDVIKSTMR----DRQL 174
Cdd:cd18028   75 VGISTGDYDEDDEWLGDYD-IIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEE-RGPTLESIVARLRrlnpNTQI 152
                        170
                 ....*....|....*
gi 446511155 175 VFFSATMTKAAEDAA 189
Cdd:cd18028  153 IGLSATIGNPDELAE 167
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
269-328 9.75e-09

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: 53.75  E-value: 9.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 269 SKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRtGRM 328
Cdd:cd18802   75 TQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
284-339 1.15e-08

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: 51.55  E-value: 1.15e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446511155 284 KLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVVSLVT 339
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
188-339 1.85e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.28  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 188 AARDLAVEPQLVRVTRAESKSLVEHT------YIICERREKNDyvrrimhmgDVKAVAFLNdpFR--LDEITEKLKFRKM 259
Cdd:COG1111  310 ASKRLVSDPRFRKAMRLAEEADIEHPklsklrEILKEQLGTNP---------DSRIIVFTQ--YRdtAEMIVEFLSEPGI 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 260 KAAALHAEASKQ--------EREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRmGKE 331
Cdd:COG1111  379 KAGRFVGQASKEgdkgltqkEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KRE 457

                 ....*...
gi 446511155 332 GTVVSLVT 339
Cdd:COG1111  458 GRVVVLIA 465
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
17-329 7.12e-08

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 54.33  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  17 GFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLhkinpeVKQPQVVVLAPtreLVMQIHEEVQKFTAGTeIS 96
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL------VLDGLTLVVSP---LISLMKDQVDQLLANG-VA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  97 GASLIGGADIKRQVEklkkhprVIVGspgrilelIRMKKLKMHEV--KTIVFDEF-DQIVK-QKMMGAVQDV-------- 164
Cdd:PRK11057  92 AACLNSTQTREQQLE-------VMAG--------CRTGQIKLLYIapERLMMDNFlEHLAHwNPALLAVDEAhcisqwgh 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 165 -----------IKSTMRDRQLVFFSATMTKAA-EDAARDLAVEPQLVRVTRAESKSLvehTYIICERREKNDYVRRIMHM 232
Cdd:PRK11057 157 dfrpeyaalgqLRQRFPTLPFMALTATADDTTrQDIVRLLGLNDPLIQISSFDRPNI---RYTLVEKFKPLDQLMRYVQE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 233 GDVKA-VAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLEL 311
Cdd:PRK11057 234 QRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDI 313
                        330
                 ....*....|....*...
gi 446511155 312 PDTVDQYIHRSGRTGRMG 329
Cdd:PRK11057 314 PRNIESYYQETGRAGRDG 331
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
11-72 8.22e-08

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 54.34  E-value: 8.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446511155  11 QAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLP----LLHKINPEVKQPQVVVL 72
Cdd:COG1201   15 RAWFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPaldeLARRPRPGELPDGLRVL 80
PRK13767 PRK13767
ATP-dependent helicase; Provisional
11-51 1.16e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 53.74  E-value: 1.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446511155  11 QAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLA 51
Cdd:PRK13767  23 REWFKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLA 63
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
270-335 2.95e-07

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 49.56  E-value: 2.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446511155 270 KQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVV 335
Cdd:cd18797   78 AEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
25-148 4.69e-07

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 49.51  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  25 QKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKInPEVKQPQVVVLAPTRELvmqIHEEVQKFTA-----GTEISGAS 99
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKAL---AQDQLRSLRElleqlGLGIRVAT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446511155 100 LIGGADIKRQVEKLKKHPRVIVGSPgRILE--LIR--------MKKLKMhevktIVFDE 148
Cdd:cd17923   81 YDGDTPREERRAIIRNPPRILLTNP-DMLHyaLLPhhdrwarfLRNLRY-----VVLDE 133
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
31-76 5.34e-07

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 51.46  E-value: 5.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446511155  31 TILEGQDVIAESPTGTGKTLAYLLPLLhKINPEVKQPqVVVLAPTR 76
Cdd:COG1199   29 ALAEGRHLLIEAGTGTGKTLAYLVPAL-LAARETGKK-VVISTATK 72
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
248-330 6.43e-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: 47.97  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 248 DEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGR 327
Cdd:cd18794   44 EQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123

                 ...
gi 446511155 328 MGK 330
Cdd:cd18794  124 DGL 126
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
25-335 1.99e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 49.89  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   25 QKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLhkINPEVkqpqVVVLAPTRELVM-QIHEEVQkftagTEISGASLIGG 103
Cdd:PLN03137  465 QREIINATMSGYDVFVLMPTGGGKSLTYQLPAL--ICPGI----TLVISPLVSLIQdQIMNLLQ-----ANIPAASLSAG 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  104 ADIKRQVEKLKK-------------HPRVIVGSPG--RILELIRMKKLkmheVKTIVFDEfDQIVKQ---------KMMG 159
Cdd:PLN03137  534 MEWAEQLEILQElsseyskykllyvTPEKVAKSDSllRHLENLNSRGL----LARFVIDE-AHCVSQwghdfrpdyQGLG 608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  160 avqdVIKSTMRDRQLVFFSATMTKAA-EDAARDLA-VEPQLVRVTRAESK---SLVEHTYIICERREKndYVRRiMHMGD 234
Cdd:PLN03137  609 ----ILKQKFPNIPVLALTATATASVkEDVVQALGlVNCVVFRQSFNRPNlwySVVPKTKKCLEDIDK--FIKE-NHFDE 681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  235 VKAVAFLNdpfRLD--EITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELP 312
Cdd:PLN03137  682 CGIIYCLS---RMDceKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLP 758
                         330       340
                  ....*....|....*....|...
gi 446511155  313 DTVDQYIHRSGRTGRMGKEGTVV 335
Cdd:PLN03137  759 KSIEGYHQECGRAGRDGQRSSCV 781
cas3_cyano TIGR03158
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ...
42-192 2.97e-06

CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.


Pssm-ID: 274457 [Multi-domain]  Cd Length: 357  Bit Score: 48.74  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   42 SPTGTGKTLAYLLPLLHkinpevKQPQVVVLAPTRELVMQIHEEVQKFTAGTE---------ISGASLIGGADIKRQVEK 112
Cdd:TIGR03158  21 APTGAGKTLAWLTPLLH------GENDTIALYPTNALIEDQTEAIKEFVDVFKperdvnllhVSKATLKDIKEYANDKVG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  113 LKK---------------HPRVIVGSPG------RILELIRMKKLKMHE--VKTIVFDEF-----DQIVKQKMMGAVQDV 164
Cdd:TIGR03158  95 SSKgeklynllrnpigtsTPIILLTNPDifvyltRFAYIDRGDIAAGFYtkFSTVIFDEFhlydaKQLVGMLFLLAYMQL 174
                         170       180
                  ....*....|....*....|....*...
gi 446511155  165 IKSTMRDRQLVFFSATMTKAAEDAARDL 192
Cdd:TIGR03158 175 IRFFECRRKFVFLSATPDPALILRLQNA 202
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
43-148 3.39e-06

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 47.12  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  43 PTGTGKTLAYLLPLLHKInpEVKQPQVVVLAPTRELVMQiHEEVQKFTAGTEISGASLIGGADIKRQvEKLKKHPRVIVG 122
Cdd:cd18035   24 PTGLGKTIIAILVAADRL--TKKGGKVLILAPSRPLVEQ-HAENLKRVLNIPDKITSLTGEVKPEER-AERWDASKIIVA 99
                         90       100
                 ....*....|....*....|....*.
gi 446511155 123 SPGRILELIRMKKLKMHEVKTIVFDE 148
Cdd:cd18035  100 TPQVIENDLLAGRITLDDVSLLIFDE 125
ResIII pfam04851
Type III restriction enzyme, res subunit;
18-149 5.45e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.13  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   18 FKELTEIQKQAIPTILEGQD-----VIAESPTGTGKTL--AYLLPLLHKINPEVKqpqVVVLAPTRELVMQIHEEVQKFT 90
Cdd:pfam04851   1 KLELRPYQIEAIENLLESIKngqkrGLIVMATGSGKTLtaAKLIARLFKKGPIKK---VLFLVPRKDLLEQALEEFKKFL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446511155   91 AGTEISGASLIGGADIKRQVEKlkkhpRVIVGSP---GRILELIRMKKLKmHEVKTIVFDEF 149
Cdd:pfam04851  78 PNYVEIGEIISGDKKDESVDDN-----KIVVTTIqslYKALELASLELLP-DFFDVIIIDEA 133
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
20-180 7.48e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 45.87  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  20 ELTEIQKQAIPTILegQDVIAESP--------TGTGKTLAYLLPLLHKINpevKQPQVVVLAPTRELVMQIHEEVQKFTA 91
Cdd:cd17918   15 SLTKDQAQAIKDIE--KDLHSPEPmdrllsgdVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKFLP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  92 gtEISGASLIGGADikrqvEKLKKHPRVIVGSPGRILElirmkKLKMHEVKTIVFDEfdqivkQKMMGAVQDVIKSTMRD 171
Cdd:cd17918   90 --FINVELVTGGTK-----AQILSGISLLVGTHALLHL-----DVKFKNLDLVIVDE------QHRFGVAQREALYNLGA 151

                 ....*....
gi 446511155 172 RQLVFFSAT 180
Cdd:cd17918  152 THFLEATAT 160
Cas3_I-D cd09710
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ...
42-192 1.11e-05

CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D


Pssm-ID: 187841 [Multi-domain]  Cd Length: 353  Bit Score: 46.79  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  42 SPTGTGKTLAYLLPLLHkinpevKQPQVVVLAPTRELVMQIHEEVQkftagteisgaSLIGGADIKRQVEKLK------- 114
Cdd:cd09710   21 APTGAGKTLAWLTPLLH------GENKAIALYPTNALIEDQTEAIK-----------EFVDDANPRHQVKSLSasditlw 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 115 ---KHPRVivgSPGRILELIRMKKLKMHE--------------------------------VKTIVFDEF-----DQIVK 154
Cdd:cd09710   84 pndKNVGS---SKGEKLYNLLRNDIGTSTpiilltnpdifvyltrfayidrgdiaagfytkFSTVIFDEFhlydaKQLVG 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446511155 155 QKMMGAVQDVIKSTMRDRQLVFFSATMTKAAEDAARDL 192
Cdd:cd09710  161 LLFYLAYMQLIRFFECRRKFVFLSATPDPALILRLQNA 198
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
15-102 1.49e-05

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 45.59  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  15 KAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLhkINPEVkqpqVVVLAPTRELvmqIHEEVQKFTAgTE 94
Cdd:cd18016   12 KFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC--VSPGV----TVVISPLRSL---IVDQVQKLTS-LD 81

                 ....*...
gi 446511155  95 ISGASLIG 102
Cdd:cd18016   82 IPATYLTG 89
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
9-148 1.72e-05

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 45.22  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   9 LQQAWekaGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLhkinpeVKQPQVVVLAPtreLVMQIHEEVQK 88
Cdd:cd17920    4 LKEVF---GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGVTLVVSP---LISLMQDQVDR 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  89 FTAgTEISGASLIGGADI--KRQVEKLKKHPR---VIVgSP-----GRILELIRmKKLKMHEVKTIVFDE 148
Cdd:cd17920   72 LQQ-LGIRAAALNSTLSPeeKREVLLRIKNGQyklLYV-TPerllsPDFLELLQ-RLPERKRLALIVVDE 138
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
265-327 1.74e-05

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: 44.56  E-value: 1.74e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446511155 265 HAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGR 327
Cdd:cd18796   75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
PRK01172 PRK01172
ATP-dependent DNA helicase;
20-326 4.48e-05

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 45.64  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  20 ELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVvlaPTRELVMQIHEEVQKFTA-GTEISga 98
Cdd:PRK01172  22 ELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIV---PLRSLAMEKYEELSRLRSlGMRVK-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  99 slIGGADIKRQVEKLKKHPRVIVGSPgRILELIRMKKLKMHEVKTIVFDEFdQIVKQKMMGAVQDVIKSTMR----DRQL 174
Cdd:PRK01172  97 --ISIGDYDDPPDFIKRYDVVILTSE-KADSLIHHDPYIINDVGLIVADEI-HIIGDEDRGPTLETVLSSARyvnpDARI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 175 VFFSATMTKAAEDAA-----------RDLAVEPQLVRVTR----AESKSLVEHTYIICE--------------RREKNDY 225
Cdd:PRK01172 173 LALSATVSNANELAQwlnasliksnfRPVPLKLGILYRKRlildGYERSQVDINSLIKEtvndggqvlvfvssRKNAEDY 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 226 VRR-IMHMG---DVKAVAFLNDPFrlDEITEKLKFRKMkaAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDI- 300
Cdd:PRK01172 253 AEMlIQHFPefnDFKVSSENNNVY--DDSLNEMLPHGV--AFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLp 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446511155 301 --------------DDLTHVIHLElpdtVDQYIHRSGRTG 326
Cdd:PRK01172 329 arlvivrditrygnGGIRYLSNME----IKQMIGRAGRPG 364
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
247-348 5.38e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 45.22  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 247 LDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGK--LEILLATDIAARGIdidDLT---HVIHLEL---PDTVDQy 318
Cdd:COG0553  562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGL---NLTaadHVIHYDLwwnPAVEEQ- 637
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446511155 319 ihRSGRTGRMG--KEGTVVSLVTPQ--EER--KLLQ 348
Cdd:COG0553  638 --AIDRAHRIGqtRDVQVYKLVAEGtiEEKilELLE 671
PRK13766 PRK13766
Hef nuclease; Provisional
178-339 6.24e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.25  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 178 SATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEH------TYIICERREKNDyvrrimhmgDVKAVAFLNdpFR--LDE 249
Cdd:PRK13766 312 EEARSSGGSKASKRLVEDPRFRKAVRKAKELDIEHpkleklREIVKEQLGKNP---------DSRIIVFTQ--YRdtAEK 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 250 ITEKLKFRKMKAAALHAEASK--------QEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHR 321
Cdd:PRK13766 381 IVDLLEKEGIKAVRFVGQASKdgdkgmsqKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQR 460
                        170
                 ....*....|....*...
gi 446511155 322 SGRTGRmGKEGTVVSLVT 339
Cdd:PRK13766 461 KGRTGR-QEEGRVVVLIA 477
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
257-338 6.74e-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: 42.62  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 257 RKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLE-LPDTVDQYIHRSGRTGR----MGKE 331
Cdd:cd18789   67 KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQISgHGGSRRQEAQRLGRILRpkkgGGKN 146

                 ....*..
gi 446511155 332 GTVVSLV 338
Cdd:cd18789  147 AFFYSLV 153
PRK00254 PRK00254
ski2-like helicase; Provisional
15-188 8.21e-05

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.81  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  15 KAGFKELTEIQKQAIPT-ILEGQDVIAESPTGTGKTLAYLLPLLHKINPEvkQPQVVVLAPTRELVMQIHEEVQKFTA-G 92
Cdd:PRK00254  18 ERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLRE--GGKAVYLVPLKALAEEKYREFKDWEKlG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  93 TEISGASliggADIKRQVEKLKKHPrVIVGSPGRILELIRMKKLKMHEVKTIVFDEFdQIVKQKMMGAVQDVIKSTMRDR 172
Cdd:PRK00254  96 LRVAMTT----GDYDSTDEWLGKYD-IIIATAEKFDSLLRHGSSWIKDVKLVVADEI-HLIGSYDRGATLEMILTHMLGR 169
                        170
                 ....*....|....*..
gi 446511155 173 -QLVFFSATMTKAAEDA 188
Cdd:PRK00254 170 aQILGLSATVGNAEELA 186
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
247-329 1.17e-04

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: 41.69  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 247 LDEITEKLKFRKMKAAALHAEASKQEREATMRAFR--GGKLEILLATDIAARGIDIDDLTHVIHLEL---PDTVDQyihR 321
Cdd:cd18793   40 LDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLNLTAANRVILYDPwwnPAVEEQ---A 116

                 ....*...
gi 446511155 322 SGRTGRMG 329
Cdd:cd18793  117 IDRAHRIG 124
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
43-148 1.26e-04

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 42.31  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  43 PTGTGKTL--AYLLPLLHKINPEVKqpqVVVLAPTRELVMQIHEEVQKFTaGTEISGASLIGGADIKRQVEKLKKHPRVI 120
Cdd:cd18033   24 PTGLGKTFiaAVVMLNYYRWFPKGK---IVFMAPTKPLVSQQIEACYKIT-GIPSSQTAELTGSVPPTKRAELWASKRVF 99
                         90       100
                 ....*....|....*....|....*...
gi 446511155 121 VGSPGRILELIRMKKLKMHEVKTIVFDE 148
Cdd:cd18033  100 FLTPQTLENDLKEGDCDPKSIVCLVIDE 127
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
17-59 1.54e-04

DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350772 [Multi-domain]  Cd Length: 205  Bit Score: 42.46  E-value: 1.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446511155  17 GFKELTEIQKQAIPTILEG-QDVIAESPTGTGKTLAYLLP-LLHK 59
Cdd:cd18014   10 HSDFKSPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPaLLAK 54
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
35-149 1.63e-04

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: 41.80  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  35 GQDVIAESPTGTGKTLAYLLPLLHKINPEVKQP-QVVVLAPTRELVMQIHEEVQKFTAG--TEISGASLIGGADIKRQVE 111
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGvQVLYISPLKALINDQERRLEEPLDEidLEIPVAVRHGDTSQSEKAK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446511155 112 KLKKHPRVIVGSPGRILELIRMKKL--KMHEVKTIVFDEF 149
Cdd:cd17922   81 QLKNPPGILITTPESLELLLVNKKLreLFAGLRYVVVDEI 120
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
9-57 1.76e-04

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 42.24  E-value: 1.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446511155   9 LQQAWekaGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLL 57
Cdd:cd18018    4 LRRVF---GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL 49
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
2-196 2.02e-04

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs 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: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 42.36  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155   2 IKDMQPFLQQAWEkaGFKELTEIQKQAIPTILEGQD-VIAESPTGTGKTLAYLLPLLHKI----NPE----VKQPQVVVL 72
Cdd:cd18019    1 IEELPDWAQPAFE--GFKSLNRIQSKLFPAAFETDEnLLLCAPTGAGKTNVALLTILREIgkhrNPDgtinLDAFKIVYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  73 APTRELVMQIHEEVQKFTAGTEISGASLIGGADI-KRQVEKLKkhprVIVGSPGRiLELIRMK---KLKMHEVKTIVFDE 148
Cdd:cd18019   79 APMKALVQEMVGNFSKRLAPYGITVAELTGDQQLtKEQISETQ----IIVTTPEK-WDIITRKsgdRTYTQLVRLIIIDE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446511155 149 FDQI------VKQKMMGAVQDVIKSTMRDRQLVFFSATMTKaAEDAARDLAVEP 196
Cdd:cd18019  154 IHLLhddrgpVLESIVARTIRQIEQTQEYVRLVGLSATLPN-YEDVATFLRVDP 206
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
246-342 2.55e-04

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: 41.10  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 246 RLDEITEKLK--FRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLThVIHLELPDT--VDQYIHR 321
Cdd:cd18792   46 SIEALAEELKelVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNAN-TMIIEDADRfgLSQLHQL 124
                         90       100
                 ....*....|....*....|.
gi 446511155 322 SGRTGRMGKEGTVVSLVTPQE 342
Cdd:cd18792  125 RGRVGRGKHQSYCYLLYPDPK 145
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
261-350 3.01e-04

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 42.99  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  261 AAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTG-RMGkeGTVVSLVT 339
Cdd:PRK09751  304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFF 381
                          90
                  ....*....|.
gi 446511155  340 PQEERKLLQFA 350
Cdd:PRK09751  382 PRTRRDLVDSA 392
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
214-331 3.76e-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: 40.79  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 214 YIICERREKNDYVrrimhmgDVKAVAflndpfrldEITEKLK---FRKMKAAALHAEASKQEREATMRAFRGGKLEILLA 290
Cdd:cd18811   30 YVIYPLIEESEKL-------DLKAAV---------AMYEYLKerfRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVS 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446511155 291 TDIAARGIDIDDLThVIHLELPDT--VDQYIHRSGRTGRMGKE 331
Cdd:cd18811   94 TTVIEVGVDVPNAT-VMVIEDAERfgLSQLHQLRGRVGRGDHQ 135
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
14-115 8.42e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 40.00  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  14 EKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKT---LAYLLPLlhkinpEVKQPQVVVLAPTRELVMQIHEEVQKFT 90
Cdd:cd17924   11 KKKTGFPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYL------ASKGKRSYLIFPTKSLVKQAYERLSKYA 84
                         90       100
                 ....*....|....*....|....*..
gi 446511155  91 AGTEISGASLI--GGADIKRQVEKLKK 115
Cdd:cd17924   85 EKAGVEVKILVyhSRLKKKEKEELLEK 111
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
20-148 1.16e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 39.77  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  20 ELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQ---VVVLAPTRELVMQIHE-EVQKFTAGTEI 95
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgrVVVLVNKVPLVEQQLEkFFKYFRKGYKV 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446511155  96 SGASliGGADIKRQVEKLKKHPRVIVGSP---------GRILELIRMKKLKMhevktIVFDE 148
Cdd:cd18036   82 TGLS--GDSSHKVSFGQIVKASDVIICTPqilinnllsGREEERVYLSDFSL-----LIFDE 136
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
35-106 1.35e-03

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members 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: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 38.57  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446511155  35 GQDVIAESPTGTGKTLAyLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLIG-GADI 106
Cdd:cd17915    1 GGHVALESPTGSGKTLS-LLCSALSYQREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIRALALSSrDADI 72
PRK07246 PRK07246
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
41-85 1.41e-03

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180905 [Multi-domain]  Cd Length: 820  Bit Score: 40.83  E-value: 1.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446511155  41 ESPTGTGKTLAYLLPLLHKinpeVKQPQVVVLAPTRELVMQIHEE 85
Cdd:PRK07246 270 EAQTGIGKTYGYLLPLLAQ----SDQRQIIVSVPTKILQDQIMAE 310
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
209-337 1.87e-03

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: 38.49  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 209 LVEHTYIICERREKNDYVRrimhmgDVKAVAFLNdpFR--LDEITEKL-KFRKMKAAAL---HAEA------SKQEREAT 276
Cdd:cd18801   11 LEKLEEIVKEHFKKKQEGS------DTRVIIFSE--FRdsAEEIVNFLsKIRPGIRATRfigQASGksskgmSQKEQKEV 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446511155 277 MRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRmGKEGTVVSL 337
Cdd:cd18801   83 IEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
33-148 1.89e-03

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 39.34  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  33 LEGQDVIAESPTGTGKTLAYLL---PLLHKInPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLIGGADIKRQ 109
Cdd:cd17927   15 LKGKNTIICLPTGSGKTFVAVLiceHHLKKF-PAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVS 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446511155 110 VEKLKKHPRVIVGSPgRILE--LIRMKKLKMHEVKTIVFDE 148
Cdd:cd17927   94 VEQIVESSDVIIVTP-QILVndLKSGTIVSLSDFSLLVFDE 133
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
9-57 1.94e-03

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 39.27  E-value: 1.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446511155   9 LQQAWEKAGFKELteiQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLL 57
Cdd:cd18015   10 LKNVFKLEKFRPL---QLETINATMAGRDVFLVMPTGGGKSLCYQLPAL 55
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
35-89 2.35e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 38.81  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446511155  35 GQDVIAESPTGTGKTLAYLLPLLHKInPEVKQPQVVVLAPTRELVMQIHEEVQKF 89
Cdd:cd17930    1 PGLVILEAPTGSGKTEAALLWALKLA-ARGGKRRIIYALPTRATINQMYERIREI 54
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
269-352 2.37e-03

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 39.15  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 269 SKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHV------IHLELPD------TVDQYIHRSGRTGRMGKEGTVVs 336
Cdd:cd18804  129 KKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgilnadSGLNSPDfraserAFQLLTQVSGRAGRGDKPGKVI- 207
                         90
                 ....*....|....*.
gi 446511155 337 LVTPQEERKLLQFAKK 352
Cdd:cd18804  208 IQTYNPEHPLIQAAKE 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
43-153 2.87e-03

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 38.06  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  43 PTGTGKTLayllpLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEIsgaSLIGGADIKrqveklkkhprvivG 122
Cdd:cd17926   26 PTGSGKTL-----TALALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSI---GLIGGGKKK--------------D 83
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446511155 123 SPGRILELIRMKKLKMH-EVKTIVFDEFDQIV 153
Cdd:cd17926   84 FDDANVVVATYQSLSNLaEEEKDLFDQFGLLI 115
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
22-81 2.91e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs 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: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 38.49  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446511155  22 TEIQKQAIPTILEGQD-VIAESPTGTGKT----LAyLLPLLHKINPEVK-QPQVVVLAPTRELVMQ 81
Cdd:cd18023    3 NRIQSEVFPDLLYSDKnFVVSAPTGSGKTvlfeLA-ILRLLKERNPLPWgNRKVVYIAPIKALCSE 67
Csf4_U cd09708
CRISPR/Cas system-associated DinG family helicase Csf4; CRISPR (Clustered Regularly ...
35-102 3.47e-03

CRISPR/Cas system-associated DinG family helicase Csf4; 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; DinG family DNA helicase


Pssm-ID: 187839 [Multi-domain]  Cd Length: 632  Bit Score: 39.57  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446511155  35 GQDVIAESPTGTGKTLAYLLPlLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTA---GTEISGASLIG 102
Cdd:cd09708   16 KRIGMLEASTGVGKTLAMIMA-ALTMLKERPDQKIAIAVPTLALMGQLWSELERLTAeglAGPVQAGFFPG 85
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
258-342 3.65e-03

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


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 37.71  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155 258 KMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIhLELPDT--VDQYIHRSGRTGRMGKEGTVV 335
Cdd:cd18810   51 EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII-IERADKfgLAQLYQLRGRVGRSKERAYAY 129

                 ....*..
gi 446511155 336 SLVTPQE 342
Cdd:cd18810  130 FLYPDQK 136
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
38-55 6.68e-03

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 38.65  E-value: 6.68e-03
                         10
                 ....*....|....*...
gi 446511155  38 VIAESPTGTGKTLAYLLP 55
Cdd:PRK11747  52 LVIEAGTGVGKTLSYLLA 69
PRK13766 PRK13766
Hef nuclease; Provisional
43-148 7.09e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 38.70  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  43 PTGTGKTLAYLL---PLLHKinpevKQPQVVVLAPTRELVMQiHEE-VQKFTAGTEISGASLIGgaDI---KRqvEKLKK 115
Cdd:PRK13766  37 PTGLGKTAIALLviaERLHK-----KGGKVLILAPTKPLVEQ-HAEfFRKFLNIPEEKIVVFTG--EVspeKR--AELWE 106
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446511155 116 HPRVIVGSPGRILELIRMKKLKMHEVKTIVFDE 148
Cdd:PRK13766 107 KAKVIVATPQVIENDLIAGRISLEDVSLLIFDE 139
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
25-149 7.10e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 37.16  E-value: 7.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446511155  25 QKQAIPTILE----GQD-VIAESPTGTGKTL--AYLLPLLHKINPevkQPQVVVLAPTRELVMQIHEEVQKFTAGTEISG 97
Cdd:cd18032    5 QQEAIEALEEarekGQRrALLVMATGTGKTYtaAFLIKRLLEANR---KKRILFLAHREELLEQAERSFKEVLPDGSFGN 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446511155  98 asliggadikrqVEKLKKHP---RVIVGSPGRILELIRMKKLKMHEVKTIVFDEF 149
Cdd:cd18032   82 ------------LKGGKKKPddaRVVFATVQTLNKRKRLEKFPPDYFDLIIIDEA 124
 
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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