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Conserved domains on  [gi|6324366|ref|NP_014436|]
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putative ATP-dependent RNA helicase DBP6 [Saccharomyces cerevisiae S288C]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13028779)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as Bacillus cereus ATP-dependent RNA helicase DbpA that is involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
185-402 2.03e-92

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: 284.91  E-value: 2.03e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  185 LLQNICKNFSTNTFPIQSIILDSILPVLNFTlnvskrnFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCII 264
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-------PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  265 IVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLE-------PDILITTPGRLVDHLNM-KSINLKNLK 336
Cdd:cd17956  74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrVDILVATPGRLVDHLNStPGFTLKHLR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324366  337 FLIIDEADRLLNQSFQGWCPKLMSHLKTDK------------LDTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLFL 402
Cdd:cd17956 154 FLVIDEADRLLNQSFQDWLETVMKALGRPTapdlgsfgdanlLERSVRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
450-572 1.49e-28

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: 110.67  E-value: 1.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  450 KILIFVKSNESSIRLSKLLQLI---CES----RSQssvlknlqnlavsinsvnsnnskAENKKIVANFShhseSAGITIL 522
Cdd:cd18787  29 KAIIFVNTKKRVDRLAELLEELgikVAAlhgdLSQ-----------------------EERERALKKFR----SGKVRVL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6324366  523 ITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLL 572
Cdd:cd18787  82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
185-402 2.03e-92

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: 284.91  E-value: 2.03e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  185 LLQNICKNFSTNTFPIQSIILDSILPVLNFTlnvskrnFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCII 264
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-------PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  265 IVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLE-------PDILITTPGRLVDHLNM-KSINLKNLK 336
Cdd:cd17956  74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrVDILVATPGRLVDHLNStPGFTLKHLR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324366  337 FLIIDEADRLLNQSFQGWCPKLMSHLKTDK------------LDTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLFL 402
Cdd:cd17956 154 FLVIDEADRLLNQSFQDWLETVMKALGRPTapdlgsfgdanlLERSVRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
174-601 3.10e-56

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 196.14  E-value: 3.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  174 FSDYanELEAKLLQNICK-NFSTNTfPIQSiilDSILPVLNftlnvskrnftrriG-DILVNAATGSGKTLAYSIPIVQT 251
Cdd:COG0513   4 FADL--GLSPPLLKALAElGYTTPT-PIQA---QAIPLILA--------------GrDVLGQAQTGTGKTAAFLLPLLQR 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  252 LFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIV-------SIAKLENSLKDEhkklsnlePDILITTPGRLVDH 324
Cdd:COG0513  64 LDPSRPRAPQALILAPTRELALQVAEELRKLAKYLGLRVatvyggvSIGRQIRALKRG--------VDIVVATPGRLLDL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  325 LNMKSINLKNLKFLIIDEADRLLNQSFQgwcP---KLMSHLKTDKLdtlpgnviKMIFSATLTTNTEKLNGLNLYKPKLF 401
Cdd:COG0513 136 IERGALDLSGVETLVLDEADRMLDMGFI---EdieRILKLLPKERQ--------TLLFSATMPPEIRKLAKRYLKNPVRI 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  402 lkQTDKLYQLPNKLNEFNINIPTAKsvyKPLILLYSICQfmaHSPIAAkiLIFVKSNESSIRLSKLLQ---LICES---- 474
Cdd:COG0513 205 --EVAPENATAETIEQRYYLVDKRD---KLELLRRLLRD---EDPERA--IVFCNTKRGADRLAEKLQkrgISAAAlhgd 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  475 RSQSsvlknlqnlavsinsvnsnnskaENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVH 554
Cdd:COG0513 275 LSQG-----------------------QRERALDAFRNGK----IRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVH 327
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 6324366  555 RVGRTARANELGSAYnLLVGRGERTFFDDLNKDLdrdGKSVQPLELD 601
Cdd:COG0513 328 RIGRTGRAGAEGTAI-SLVTPDERRLLRAIEKLI---GQKIEEEELP 370
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
199-390 1.57e-40

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 145.08  E-value: 1.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366    199 PIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIPIVQTLFKRQiNRLRCIIIVPTKLLINQVYTT 278
Cdd:pfam00270   2 PIQAEAIPAIL---------EGR-------DVLVQAPTGSGKTLAFLLPALEALDKLD-NGPQALVLAPTRELAEQIYEE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366    279 LTKLTQGTSLIVSIAKLENSLKDEHKKLSNlePDILITTPGRLVDHLNmKSINLKNLKFLIIDEADRLLNQSFQGWCPKL 358
Cdd:pfam00270  65 LKKLGKGLGLKVASLLGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEI 141
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6324366    359 MSHlktdkldtLPGNVIKMIFSATLTTNTEKL 390
Cdd:pfam00270 142 LRR--------LPKKRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
189-401 4.58e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.46  E-value: 4.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366     189 ICKNFSTNTFPIQSIILDSILpvlnftlnvskrnftRRIGDILVNAATGSGKTLAYSIPIVQTLFKRqiNRLRCIIIVPT 268
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALL---------------SGLRDVILAAPTGSGKTLAALLPALEALKRG--KGGRVLVLVPT 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366     269 KLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLN 348
Cdd:smart00487  64 RELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 6324366     349 QSFQgwcPKLMSHLKtdkldTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLF 401
Cdd:smart00487 144 GGFG---DQLEKLLK-----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
229-578 4.89e-31

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 126.21  E-value: 4.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQTLF---KRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLivSIAKLENSLK-DEHK 304
Cdd:PRK11192  40 DVLGSAPTGTGKTAAFLLPALQHLLdfpRRKSGPPRILILTPTRELAMQVADQARELAKHTHL--DIATITGGVAyMNHA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   305 KLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFqgwcpklmshlktdkldtlpGNVIK-------- 376
Cdd:PRK11192 118 EVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGF--------------------AQDIEtiaaetrw 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   377 ----MIFSATLTTNteklnGLNLYKPKLfLKQTDKLYQLPNKLNEFNIN--IPTAKSVYKPLILLYSICQfmahSPIAAK 450
Cdd:PRK11192 178 rkqtLLFSATLEGD-----AVQDFAERL-LNDPVEVEAEPSRRERKKIHqwYYRADDLEHKTALLCHLLK----QPEVTR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   451 ILIFVKSNEssiRLSKLLQLICESRSQSSVLKNlqnlavsinsvnsNNSKAENKKIVANFShhseSAGITILITTDIMSR 530
Cdd:PRK11192 248 SIVFVRTRE---RVHELAGWLRKAGINCCYLEG-------------EMVQAKRNEAIKRLT----DGRVNVLVATDVAAR 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6324366   531 GIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNL-------LVGRGER 578
Cdd:PRK11192 308 GIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLveahdhlLLGKIER 362
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
450-572 1.49e-28

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: 110.67  E-value: 1.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  450 KILIFVKSNESSIRLSKLLQLI---CES----RSQssvlknlqnlavsinsvnsnnskAENKKIVANFShhseSAGITIL 522
Cdd:cd18787  29 KAIIFVNTKKRVDRLAELLEELgikVAAlhgdLSQ-----------------------EERERALKKFR----SGKVRVL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6324366  523 ITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLL 572
Cdd:cd18787  82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
500-563 2.69e-16

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: 74.94  E-value: 2.69e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366    500 KAENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARAN 563
Cdd:pfam00271  50 QEEREEILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
500-563 2.15e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.47  E-value: 2.15e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366     500 KAENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARAN 563
Cdd:smart00490  23 QEEREEILDKFNNGK----IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
519-564 8.16e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 39.33  E-value: 8.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6324366  519 ITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANE 564
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE 457
 
Name Accession Description Interval E-value
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
185-402 2.03e-92

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: 284.91  E-value: 2.03e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  185 LLQNICKNFSTNTFPIQSIILDSILPVLNFTlnvskrnFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCII 264
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKST-------PPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  265 IVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLE-------PDILITTPGRLVDHLNM-KSINLKNLK 336
Cdd:cd17956  74 VVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrVDILVATPGRLVDHLNStPGFTLKHLR 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324366  337 FLIIDEADRLLNQSFQGWCPKLMSHLKTDK------------LDTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLFL 402
Cdd:cd17956 154 FLVIDEADRLLNQSFQDWLETVMKALGRPTapdlgsfgdanlLERSVRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
174-601 3.10e-56

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 196.14  E-value: 3.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  174 FSDYanELEAKLLQNICK-NFSTNTfPIQSiilDSILPVLNftlnvskrnftrriG-DILVNAATGSGKTLAYSIPIVQT 251
Cdd:COG0513   4 FADL--GLSPPLLKALAElGYTTPT-PIQA---QAIPLILA--------------GrDVLGQAQTGTGKTAAFLLPLLQR 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  252 LFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIV-------SIAKLENSLKDEhkklsnlePDILITTPGRLVDH 324
Cdd:COG0513  64 LDPSRPRAPQALILAPTRELALQVAEELRKLAKYLGLRVatvyggvSIGRQIRALKRG--------VDIVVATPGRLLDL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  325 LNMKSINLKNLKFLIIDEADRLLNQSFQgwcP---KLMSHLKTDKLdtlpgnviKMIFSATLTTNTEKLNGLNLYKPKLF 401
Cdd:COG0513 136 IERGALDLSGVETLVLDEADRMLDMGFI---EdieRILKLLPKERQ--------TLLFSATMPPEIRKLAKRYLKNPVRI 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  402 lkQTDKLYQLPNKLNEFNINIPTAKsvyKPLILLYSICQfmaHSPIAAkiLIFVKSNESSIRLSKLLQ---LICES---- 474
Cdd:COG0513 205 --EVAPENATAETIEQRYYLVDKRD---KLELLRRLLRD---EDPERA--IVFCNTKRGADRLAEKLQkrgISAAAlhgd 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  475 RSQSsvlknlqnlavsinsvnsnnskaENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVH 554
Cdd:COG0513 275 LSQG-----------------------QRERALDAFRNGK----IRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVH 327
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 6324366  555 RVGRTARANELGSAYnLLVGRGERTFFDDLNKDLdrdGKSVQPLELD 601
Cdd:COG0513 328 RIGRTGRAGAEGTAI-SLVTPDERRLLRAIEKLI---GQKIEEEELP 370
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
199-390 1.57e-40

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 145.08  E-value: 1.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366    199 PIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIPIVQTLFKRQiNRLRCIIIVPTKLLINQVYTT 278
Cdd:pfam00270   2 PIQAEAIPAIL---------EGR-------DVLVQAPTGSGKTLAFLLPALEALDKLD-NGPQALVLAPTRELAEQIYEE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366    279 LTKLTQGTSLIVSIAKLENSLKDEHKKLSNlePDILITTPGRLVDHLNmKSINLKNLKFLIIDEADRLLNQSFQGWCPKL 358
Cdd:pfam00270  65 LKKLGKGLGLKVASLLGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEI 141
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6324366    359 MSHlktdkldtLPGNVIKMIFSATLTTNTEKL 390
Cdd:pfam00270 142 LRR--------LPKKRQILLLSATLPRNLEDL 165
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
195-400 3.53e-38

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: 139.88  E-value: 3.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  195 TNTFPIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIPIVQTLFKRQINR---LRCIIIVPTKLL 271
Cdd:cd00268  11 EKPTPIQAQAIPLIL---------SGR-------DVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgrgPQALVLAPTREL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  272 INQVYTTLTKLTQGTSLivSIAKL--ENSLKDEHKKLSNlEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQ 349
Cdd:cd00268  75 AMQIAEVARKLGKGTGL--KVAAIygGAPIKKQIEALKK-GPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDM 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6324366  350 SFQGWCPKLMSHlktdkldtLPGNVIKMIFSATLTTNTEKLNGLNLYKPKL 400
Cdd:cd00268 152 GFEEDVEKILSA--------LPKDRQTLLFSATLPEEVKELAKKFLKNPVR 194
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
228-400 6.41e-37

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: 136.95  E-value: 6.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  228 GDILVNAATGSGKTLAYSIPIVQTL--FKRQINR---LRCIIIVPTKLLINQVYTTLTKLTQGTSLIV--SIAKLENSlK 300
Cdd:cd17949  29 RDVLVRSQTGSGKTLAYLLPIIQRLlsLEPRVDRsdgTLALVLVPTRELALQIYEVLEKLLKPFHWIVpgYLIGGEKR-K 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  301 DEHKKLS---NlepdILITTPGRLVDHL-NMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHL-----KTDKLDTLP 371
Cdd:cd17949 108 SEKARLRkgvN----ILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELLddkrsKAGGEKSKP 183
                       170       180
                ....*....|....*....|....*....
gi 6324366  372 GNVIKMIFSATLTTNTEKLNGLNLYKPKL 400
Cdd:cd17949 184 SRRQTVLVSATLTDGVKRLAGLSLKDPVY 212
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
185-390 5.23e-36

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: 133.87  E-value: 5.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  185 LLQNICK-NFSTNTfPIQsiiLDSIlPVLnftlnVSKRnftrrigDILVNAATGSGKTLAYSIPIVQTLFKRQINR-LRC 262
Cdd:cd17957   1 LLNNLEEsGYREPT-PIQ---MQAI-PIL-----LHGR-------DLLACAPTGSGKTLAFLIPILQKLGKPRKKKgLRA 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  263 IIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDE 342
Cdd:cd17957  64 LILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDE 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6324366  343 ADRLLNQSFQGWCPKLMSHLktdkldTLPgNVIKMIFSATLTTNTEKL 390
Cdd:cd17957 144 ADKLFEPGFREQTDEILAAC------TNP-NLQRSLFSATIPSEVEEL 184
DEXDc smart00487
DEAD-like helicases superfamily;
189-401 4.58e-35

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 131.46  E-value: 4.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366     189 ICKNFSTNTFPIQSIILDSILpvlnftlnvskrnftRRIGDILVNAATGSGKTLAYSIPIVQTLFKRqiNRLRCIIIVPT 268
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALL---------------SGLRDVILAAPTGSGKTLAALLPALEALKRG--KGGRVLVLVPT 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366     269 KLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLN 348
Cdd:smart00487  64 RELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 6324366     349 QSFQgwcPKLMSHLKtdkldTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLF 401
Cdd:smart00487 144 GGFG---DQLEKLLK-----LLPKNVQLLLLSATPPEEIENLLELFLNDPVFI 188
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
229-399 2.82e-34

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: 128.91  E-value: 2.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLF--KRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKL 306
Cdd:cd17947  29 DICASAVTGSGKTAAFLLPILERLLyrPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAAL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  307 sNLEPDILITTPGRLVDHL-NMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFSATLTT 385
Cdd:cd17947 109 -RARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL--------CPRTRQTMLFSATMTD 179
                       170
                ....*....|....
gi 6324366  386 NTEKLNGLNLYKPK 399
Cdd:cd17947 180 EVKDLAKLSLNKPV 193
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
229-398 7.30e-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: 128.09  E-value: 7.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINR-----LRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKD-E 302
Cdd:cd17961  33 DILARARTGSGKTAAYALPIIQKILKAKAESgeeqgTRALILVPTRELAQQVSKVLEQLTAYCRKDVRVVNLSASSSDsV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  303 HKKLSNLEPDILITTPGRLVDHLNMKSI-NLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFSA 381
Cdd:cd17961 113 QRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSY--------LPKNYQTFLMSA 184
                       170
                ....*....|....*..
gi 6324366  382 TLTTNTEKLNGLNLYKP 398
Cdd:cd17961 185 TLSEDVEALKKLVLHNP 201
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
229-398 1.31e-32

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: 124.74  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQiNRLRCIIIVPTKLLINQVYTTLTKLtqGTSLIVSIAKLEN--SLKDEHKKL 306
Cdd:cd17954  39 DIIGLAETGSGKTAAFALPILQALLENP-QRFFALVLAPTRELAQQISEQFEAL--GSSIGLKSAVLVGgmDMMAQAIAL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  307 SNlEPDILITTPGRLVDHL-NMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFSATLTT 385
Cdd:cd17954 116 AK-KPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDFEPEIDKILKV--------IPRERTTYLFSATMTT 186
                       170
                ....*....|...
gi 6324366  386 NTEKLNGLNLYKP 398
Cdd:cd17954 187 KVAKLQRASLKNP 199
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
229-578 4.89e-31

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 126.21  E-value: 4.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQTLF---KRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLivSIAKLENSLK-DEHK 304
Cdd:PRK11192  40 DVLGSAPTGTGKTAAFLLPALQHLLdfpRRKSGPPRILILTPTRELAMQVADQARELAKHTHL--DIATITGGVAyMNHA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   305 KLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFqgwcpklmshlktdkldtlpGNVIK-------- 376
Cdd:PRK11192 118 EVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGF--------------------AQDIEtiaaetrw 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   377 ----MIFSATLTTNteklnGLNLYKPKLfLKQTDKLYQLPNKLNEFNIN--IPTAKSVYKPLILLYSICQfmahSPIAAK 450
Cdd:PRK11192 178 rkqtLLFSATLEGD-----AVQDFAERL-LNDPVEVEAEPSRRERKKIHqwYYRADDLEHKTALLCHLLK----QPEVTR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   451 ILIFVKSNEssiRLSKLLQLICESRSQSSVLKNlqnlavsinsvnsNNSKAENKKIVANFShhseSAGITILITTDIMSR 530
Cdd:PRK11192 248 SIVFVRTRE---RVHELAGWLRKAGINCCYLEG-------------EMVQAKRNEAIKRLT----DGRVNVLVATDVAAR 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6324366   531 GIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNL-------LVGRGER 578
Cdd:PRK11192 308 GIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLveahdhlLLGKIER 362
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
229-383 1.52e-30

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: 118.84  E-value: 1.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQI----NRLRCIIIVPTKLLINQVYTTLTKLTQG-TSLIVSIAKLENSLKDEH 303
Cdd:cd17964  34 DVLARAKTGTGKTLAFLLPAIQSLLNTKPagrrSGVSALIISPTRELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAEL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  304 KKLSNLEPDILITTPGRLVDHLN--MKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTLPGnvikMIFSA 381
Cdd:cd17964 114 NRLRRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMGFRPDLEQILRHLPEKNADPRQT----LLFSA 189

                ..
gi 6324366  382 TL 383
Cdd:cd17964 190 TV 191
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
229-402 6.04e-30

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: 116.69  E-value: 6.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFK---RQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKK 305
Cdd:cd17942  29 DVLGAAKTGSGKTLAFLIPAIELLYKlkfKPRNGTGVIIISPTRELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEK 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  306 LSNLEPdILITTPGRLVDHL-NMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMShlktdkldTLPGNVIKMIFSATLT 384
Cdd:cd17942 109 LGKGVN-ILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK--------LLPKRRQTMLFSATQT 179
                       170
                ....*....|....*...
gi 6324366  385 TNTEKLNGLNLYKPKLFL 402
Cdd:cd17942 180 RKVEDLARISLKKKPLYV 197
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
229-399 2.54e-29

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: 115.08  E-value: 2.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINR---LRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKK 305
Cdd:cd17941  29 DILGAAKTGSGKTLAFLVPLLEKLYRERWTPedgLGALIISPTRELAMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKER 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  306 LSNLepDILITTPGRLVDHLNMK-SINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKlDTLpgnvikmIFSATLT 384
Cdd:cd17941 109 INRM--NILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLPKSR-QTL-------LFSATQT 178
                       170
                ....*....|....*
gi 6324366  385 TNTEKLNGLNLYKPK 399
Cdd:cd17941 179 KSVKDLARLSLKNPE 193
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
450-572 1.49e-28

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: 110.67  E-value: 1.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  450 KILIFVKSNESSIRLSKLLQLI---CES----RSQssvlknlqnlavsinsvnsnnskAENKKIVANFShhseSAGITIL 522
Cdd:cd18787  29 KAIIFVNTKKRVDRLAELLEELgikVAAlhgdLSQ-----------------------EERERALKKFR----SGKVRVL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6324366  523 ITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLL 572
Cdd:cd18787  82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
229-390 2.68e-28

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: 112.28  E-value: 2.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQIN----RLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKL--ENSLKDE 302
Cdd:cd17960  29 DVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkgQVGALIISPTRELATQIYEVLQSFLEHHLPKLKCQLLigGTNVEED 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  303 HKKLSNLEPDILITTPGRLVDHLNMKS--INLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFS 380
Cdd:cd17960 109 VKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFEADLNRILSK--------LPKQRRTGLFS 180
                       170
                ....*....|
gi 6324366  381 ATLTTNTEKL 390
Cdd:cd17960 181 ATQTDAVEEL 190
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
229-578 8.10e-27

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 115.33  E-value: 8.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSN 308
Cdd:PRK11634  45 DVLGMAQTGSGKTAAFSLPLLHNL-DPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   309 LEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFSATLttnte 388
Cdd:PRK11634 124 QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQ--------IPEGHQTALFSATM----- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   389 klnglnlykPKLFLKQTDKLYQLPNKLnEFNINIPTAKSVYKPLILLY------SICQFMAHSPIAAKIlIFVKSNESSI 462
Cdd:PRK11634 191 ---------PEAIRRITRRFMKEPQEV-RIQSSVTTRPDISQSYWTVWgmrkneALVRFLEAEDFDAAI-IFVRTKNATL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   463 RLSKLLQlicESRSQSSVLKNLQNLAVSINSVnsnnskaENKKivanfshhseSAGITILITTDIMSRGIDINDITQVIN 542
Cdd:PRK11634 260 EVAEALE---RNGYNSAALNGDMNQALREQTL-------ERLK----------DGRLDILIATDVAARGLDVERISLVVN 319
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 6324366   543 YDPPMSSQQYVHRVGRTARANELGSAYnLLVGRGER 578
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRAL-LFVENRER 354
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
192-416 6.71e-26

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: 106.55  E-value: 6.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  192 NFSTNTfPIQSIILDSILpvlnftlnvskrnftRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQ--------INRLRCI 263
Cdd:cd17946   9 GFSEPT-PIQALALPAAI---------------RDGKDVIGAAETGSGKTLAFGIPILERLLSQKssngvggkQKPLRAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  264 IIVPTKLLINQVYTTLTKLTQGTSL----IV---SIAKLENSLKDehkklsnlEPDILITTPGRL-------VDHLNmks 329
Cdd:cd17946  73 ILTPTRELAVQVKDHLKAIAKYTNIkiasIVgglAVQKQERLLKK--------RPEIVVATPGRLweliqegNEHLA--- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  330 iNLKNLKFLIIDEADRLL-NQSFQGWcPKLMSHLKTDKldtlPGNVIK---MIFSATLTTNTEKLNGLNLYKPKLFLKQT 405
Cdd:cd17946 142 -NLKSLRFLVLDEADRMLeKGHFAEL-EKILELLNKDR----AGKKRKrqtFVFSATLTLDHQLPLKLNSKKKKKKKEKK 215
                       250
                ....*....|.
gi 6324366  406 DKLYQLPNKLN 416
Cdd:cd17946 216 QKLELLIEKVG 226
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
223-566 1.66e-25

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 110.39  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   223 FTRRIGDILVNAATGSGKTLAYSIPIVQTLF------KRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLivSIAKLE 296
Cdd:PRK01297 120 YTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppkERYMGEPRALIIAPTRELVVQIAKDAAALTKYTGL--NVMTFV 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   297 NSLkDEHKKLSNLEP---DILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNqsfQGWCPKLMSHLKtdklDTLP-G 372
Cdd:PRK01297 198 GGM-DFDKQLKQLEArfcDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLD---MGFIPQVRQIIR----QTPRkE 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   373 NVIKMIFSATLTTNTeklngLNLYKPKLFLKQTDKL--YQLPNKLNEFNINIPTAKSVYKpliLLYSIcqfMAHSPIaAK 450
Cdd:PRK01297 270 ERQTLLFSATFTDDV-----MNLAKQWTTDPAIVEIepENVASDTVEQHVYAVAGSDKYK---LLYNL---VTQNPW-ER 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   451 ILIFVKSNESSIRLSKLLQLICESRSQSSvlknlqnlavsinsvnsnNSKAENKKI--VANFshhsESAGITILITTDIM 528
Cdd:PRK01297 338 VMVFANRKDEVRRIEERLVKDGINAAQLS------------------GDVPQHKRIktLEGF----REGKIRVLVATDVA 395
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 6324366   529 SRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELG 566
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASG 433
PTZ00110 PTZ00110
helicase; Provisional
229-572 3.66e-25

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 109.86  E-value: 3.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIP-IVQTLFKrqiNRLR------CIIIVPTKLLINQVYTTLTKLTqgtslivSIAKLENSL-- 299
Cdd:PTZ00110 169 DMIGIAETGSGKTLAFLLPaIVHINAQ---PLLRygdgpiVLVLAPTRELAEQIREQCNKFG-------ASSKIRNTVay 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   300 -----KDEHKKLSNlEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKlDTLpgnv 374
Cdd:PTZ00110 239 ggvpkRGQIYALRR-GVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDR-QTL---- 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   375 ikmIFSATLTTNTEKLnglnlykpklflkQTDKLYQLPNKLNEFNINIPTAKSVYKPLILLYS----------ICQFMAH 444
Cdd:PTZ00110 313 ---MWSATWPKEVQSL-------------ARDLCKEEPVHVNVGSLDLTACHNIKQEVFVVEEhekrgklkmlLQRIMRD 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   445 SPiaaKILIFVKSNESSIRLSKLLQL-----ICesrsqssvlknlqnlavsinsvNSNNSKAENKKIVANFSHHSESAgi 519
Cdd:PTZ00110 377 GD---KILIFVETKKGADFLTKELRLdgwpaLC----------------------IHGDKKQEERTWVLNEFKTGKSP-- 429
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6324366   520 tILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLL 572
Cdd:PTZ00110 430 -IMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFL 481
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
229-571 4.92e-25

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 108.74  E-value: 4.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQTLfkrQINRLRC--IIIVPTKLLINQVYTTLTKLTQGTSLI--------VSIAKLENS 298
Cdd:PRK11776  43 DVIAQAKTGSGKTAAFGLGLLQKL---DVKRFRVqaLVLCPTRELADQVAKEIRRLARFIPNIkvltlcggVPMGPQIDS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   299 LkdEHKklsnlePDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQ-------GWCPKlmshlktdKLDTLp 371
Cdd:PRK11776 120 L--EHG------AHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQdaidaiiRQAPA--------RRQTL- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   372 gnvikmIFSATLTTNTEKLNGLNLYKPKLFlkqtdklyqlpnKLNEFNINIPTAKSVYKplillysicqfmahspiaaki 451
Cdd:PRK11776 183 ------LFSATYPEGIAAISQRFQRDPVEV------------KVESTHDLPAIEQRFYE--------------------- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   452 lifVKSNEssiRLSKLLQLICESRSQSSVL-----KNLQNLAVSINSVNSNNS-------KAENKKIVANFSHHSESagi 519
Cdd:PRK11776 224 ---VSPDE---RLPALQRLLLHHQPESCVVfcntkKECQEVADALNAQGFSALalhgdleQRDRDQVLVRFANRSCS--- 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6324366   520 tILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNL 571
Cdd:PRK11776 295 -VLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSL 345
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
174-568 7.31e-25

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 107.75  E-value: 7.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   174 FSDYAneLEAKLLQNI-CKNFSTNTfPIQSIILdsilPVLnftlnVSKRnftrrigDILVNAATGSGKTLAY-------- 244
Cdd:PRK04837  10 FSDFA--LHPQVVEALeKKGFHNCT-PIQALAL----PLT-----LAGR-------DVAGQAQTGTGKTMAFltatfhyl 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   245 -SIPIVQtlfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNlEPDILITTPGRLVD 323
Cdd:PRK04837  71 lSHPAPE---DRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLES-GVDILIGTTGRLID 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   324 HLNMKSINLKNLKFLIIDEADRLLNQSFQG---W----CPKLMSHLktdkldtlpgnviKMIFSATLTtnteklnglnlY 396
Cdd:PRK04837 147 YAKQNHINLGAIQVVVLDEADRMFDLGFIKdirWlfrrMPPANQRL-------------NMLFSATLS-----------Y 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   397 KPKlflkqtdklyqlpnKLNEFNINIPTaKSVYKPLillysicQFMAHSpiaAKILIFVKSNESSIRLskLLQLICE--- 473
Cdd:PRK04837 203 RVR--------------ELAFEHMNNPE-YVEVEPE-------QKTGHR---IKEELFYPSNEEKMRL--LQTLIEEewp 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   474 ------SRSQSSVLKNLQNLAVSINSVNSNNSKAENKK---IVANFShhseSAGITILITTDIMSRGIDINDITQVINYD 544
Cdd:PRK04837 256 draiifANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKrlrILEEFT----RGDLDILVATDVAARGLHIPAVTHVFNYD 331
                        410       420
                 ....*....|....*....|....
gi 6324366   545 PPMSSQQYVHRVGRTARANELGSA 568
Cdd:PRK04837 332 LPDDCEDYVHRIGRTGRAGASGHS 355
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
181-383 1.81e-24

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: 101.61  E-value: 1.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  181 LEAKLLQNIC-KNFSTNTfPIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIPIVQTLFKR-QIN 258
Cdd:cd17959   8 LSPPLLRAIKkKGYKVPT-PIQRKTIPLIL---------DGR-------DVVAMARTGSGKTAAFLIPMIEKLKAHsPTV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  259 RLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNlEPDILITTPGRLVDHLNMKSINLKNLKFL 338
Cdd:cd17959  71 GARALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALAS-NPDIIIATPGRLLHLLVEMNLKLSSVEYV 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6324366  339 IIDEADRLLNQSFQGWCPKLMSHlktdkldtLPGNVIKMIFSATL 383
Cdd:cd17959 150 VFDEADRLFEMGFAEQLHEILSR--------LPENRQTLLFSATL 186
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
229-402 2.51e-24

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: 102.74  E-value: 2.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINRLR--------CIIIVPTKLLINQVYTTLTKLTQGTSL--IV-------- 290
Cdd:cd18052  82 DLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfsevqepqALIVAPTRELANQIFLEARKFSYGTCIrpVVvyggvsvg 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  291 -SIAKLEnslKDEHkklsnlepdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHL----KTD 365
Cdd:cd18052 162 hQIRQIE---KGCH---------ILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKED 229
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6324366  366 KlDTLpgnvikmIFSATLTTNTEKLNGLNLYKPKLFL 402
Cdd:cd18052 230 R-QTL-------MFSATFPEEIQRLAAEFLKEDYLFL 258
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
174-390 6.80e-24

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


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 100.25  E-value: 6.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  174 FSDyaNELEAKLLQNICK-NFSTNTfPIQ--SIildsilPVLnftlnVSKRnftrrigDILVNAATGSGKTLAYSIPIVQ 250
Cdd:cd17967   2 FEE--AGLRELLLENIKRaGYTKPT-PVQkyAI------PII-----LAGR-------DLMACAQTGSGKTAAFLLPIIS 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  251 TLFKRQINRL---------RCIIIVPTKLLINQVYTTLTKLTQGTSLIVSI----AKLENSLKDEHKKLsnlepDILITT 317
Cdd:cd17967  61 KLLEDGPPSVgrgrrkaypSALILAPTRELAIQIYEEARKFSYRSGVRSVVvyggADVVHQQLQLLRGC-----DILVAT 135
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  318 PGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHlktdklDTLP--GNVIKMIFSATLTTNTEKL 390
Cdd:cd17967 136 PGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVEH------PDMPpkGERQTLMFSATFPREIQRL 204
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
229-402 8.31e-24

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 99.61  E-value: 8.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTL-------FkrqinrlrCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKD 301
Cdd:cd17955  38 DVIGGAKTGSGKTAAFALPILQRLsedpygiF--------ALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVK 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  302 EHKKLSNLePDILITTPGRLVDHL---NMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKlDTLpgnvikmI 378
Cdd:cd17955 110 QALELSKR-PHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSALPPKR-QTL-------L 180
                       170       180
                ....*....|....*....|....
gi 6324366  379 FSATLTTNTEKLNGLNLYKPKLFL 402
Cdd:cd17955 181 FSATLTDALKALKELFGNKPFFWE 204
PTZ00424 PTZ00424
helicase 45; Provisional
229-573 2.37e-23

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 102.60  E-value: 2.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQtLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQ-----------GTSLIVSIAKLEN 297
Cdd:PTZ00424  67 DTIGQAQSGTGKTATFVIAALQ-LIDYDLNACQALILAPTRELAQQIQKVVLALGDylkvrchacvgGTVVRDDINKLKA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   298 SLKdehkklsnlepdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFqgwcpKLMSHlktDKLDTLPGNVIKM 377
Cdd:PTZ00424 146 GVH------------MVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF-----KGQIY---DVFKKLPPDVQVA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   378 IFSATLTTNTEKLNGLNLYKPKLFLKQTDKLYQlpNKLNEFNINIptAKSVYKplilLYSICQFMAHSPIAAKILIfvks 457
Cdd:PTZ00424 206 LFSATMPNEILELTTKFMRDPKRILVKKDELTL--EGIRQFYVAV--EKEEWK----FDTLCDLYETLTITQAIIY---- 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   458 nessirlskllqliCESRSQSSVL-KNLQNLAVSINSVNSNNSKAENKKIVANFshhsESAGITILITTDIMSRGIDIND 536
Cdd:PTZ00424 274 --------------CNTRRKVDYLtKKMHERDFTVSCMHGDMDQKDRDLIMREF----RSGSTRVLITTDLLARGIDVQQ 335
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 6324366   537 ITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLLV 573
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVT 372
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
172-568 3.00e-23

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 104.26  E-value: 3.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   172 KPFSDY---ANELEAKLLQNICKNFSTNTFPIQSIILDSILPVlnftlnvskrnftrriGDILVNAATGSGKTLAYSIPI 248
Cdd:PRK04537   4 KPLTDLtfsSFDLHPALLAGLESAGFTRCTPIQALTLPVALPG----------------GDVAGQAQTGTGKTLAFLVAV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   249 VQTLFKRQ--INRL----RCIIIVPTKLLINQVYTTLTKLtqGTSLIVSIAKLENSLK-DEHKKLSNLEPDILITTPGRL 321
Cdd:PRK04537  68 MNRLLSRPalADRKpedpRALILAPTRELAIQIHKDAVKF--GADLGLRFALVYGGVDyDKQRELLQQGVDVIIATPGRL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   322 VDHLNM-KSINLKNLKFLIIDEADRLLNQSFqgwcPKLMSHLktdkLDTLP--GNVIKMIFSATLTTNTEKLNGLNLYKP 398
Cdd:PRK04537 146 IDYVKQhKVVSLHACEICVLDEADRMFDLGF----IKDIRFL----LRRMPerGTRQTLLFSATLSHRVLELAYEHMNEP 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   399 KLFLKQTDKLyqLPNKLNEfNINIPtAKSVYKPLILlysicQFMAHSPiAAKILIFVKSNESSIRLSKLLQlicESRSQS 478
Cdd:PRK04537 218 EKLVVETETI--TAARVRQ-RIYFP-ADEEKQTLLL-----GLLSRSE-GARTMVFVNTKAFVERVARTLE---RHGYRV 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   479 SVLKNlqnlavsinsvnsNNSKAENKKIVANFshhsESAGITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGR 558
Cdd:PRK04537 285 GVLSG-------------DVPQKKRESLLNRF----QKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGR 347
                        410
                 ....*....|
gi 6324366   559 TARANELGSA 568
Cdd:PRK04537 348 TARLGEEGDA 357
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
229-591 1.45e-22

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 101.04  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQTLFKRQINR-----LRCIIIVPTKLLINQV---------YTTLTKLT--QGTSLIVSI 292
Cdd:PRK10590  40 DLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrpVRALILTPTRELAAQIgenvrdyskYLNIRSLVvfGGVSINPQM 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   293 AKLENSLkdehkklsnlepDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFqgwcpklmSHLKTDKLDTLPG 372
Cdd:PRK10590 120 MKLRGGV------------DVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGF--------IHDIRRVLAKLPA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   373 NVIKMIFSATLTTNTEKLnglnlykpklflkqTDKLYQLPNKLNEFNINIPT---AKSVY------KPLILlysicQFMA 443
Cdd:PRK10590 180 KRQNLLFSATFSDDIKAL--------------AEKLLHNPLEIEVARRNTASeqvTQHVHfvdkkrKRELL-----SQMI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   444 HSPIAAKILIFVKSNESSIRLSKLLQ-------LICESRSQSSVLKNLqnlavsinsvnsnnskaenkkivANFshhsES 516
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNkdgirsaAIHGNKSQGARTRAL-----------------------ADF----KS 293
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366   517 AGITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNlLVGRGERTFFDDLNKDLDRD 591
Cdd:PRK10590 294 GDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS-LVCVDEHKLLRDIEKLLKKE 367
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
228-383 2.85e-22

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: 95.08  E-value: 2.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  228 GDILVNAATGSGKTLAYSIPIVQTLfkrqinrlRCIIIVPTKLLINQVYTTLTKLtqgtSLIVSIAKLENSL-------K 300
Cdd:cd17938  37 GDVLMAAETGSGKTGAFCLPVLQIV--------VALILEPSRELAEQTYNCIENF----KKYLDNPKLRVALliggvkaR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  301 DEHKKLSNlEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTdklDTLPGNVIKMI-F 379
Cdd:cd17938 105 EQLKRLES-GVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPK---ITSDGKRLQVIvC 180

                ....
gi 6324366  380 SATL 383
Cdd:cd17938 181 SATL 184
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
185-390 5.62e-22

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


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 94.02  E-value: 5.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  185 LLQNICKNFSTNTFPIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIP-IVQTLFKRQINRLR-- 261
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVAL---------SGR-------DMIGIAKTGSGKTAAFIWPmLVHIMDQRELEKGEgp 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  262 -CIIIVPTKLLINQVYTTLTKLTQGTSLIVSiAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLII 340
Cdd:cd17952  65 iAVIVAPTRELAQQIYLEAKKFGKAYNLRVV-AVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVL 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6324366  341 DEADRLLNQSFQGWCPKLMSHLKTDKlDTLpgnvikmIFSATLTTNTEKL 390
Cdd:cd17952 144 DEADRMFDMGFEYQVRSIVGHVRPDR-QTL-------LFSATFKKKIEQL 185
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
229-600 2.49e-21

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 97.94  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   229 DILVNAATGSGKTLAYSIPIVQ--TLFKRQ-INRLR---CIIIVPTKLLINQVYTTLTKLTQG----TSLIVSIAKLENS 298
Cdd:PLN00206 160 SLLVSADTGSGKTASFLVPIISrcCTIRSGhPSEQRnplAMVLTPTRELCVQVEDQAKVLGKGlpfkTALVVGGDAMPQQ 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   299 LkdeHKKLSNLEpdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLdtlpgnvikMI 378
Cdd:PLN00206 240 L---YRIQQGVE--LIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQPQV---------LL 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   379 FSATLTTNTEKLnglnlykpklflkqtdklyqlpnklnefniniptAKSVYKPLILLySICQFMAHSPIAAKILIFVKSN 458
Cdd:PLN00206 306 FSATVSPEVEKF----------------------------------ASSLAKDIILI-SIGNPNRPNKAVKQLAIWVETK 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   459 ESSIRLSKLLQ----------LICESRSQSSVLKNLQNLAVSINSVNSNNSKA--ENKKIVANFSHHSesagITILITTD 526
Cdd:PLN00206 351 QKKQKLFDILKskqhfkppavVFVSSRLGADLLANAITVVTGLKALSIHGEKSmkERREVMKSFLVGE----VPVIVATG 426
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366   527 IMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYnLLVGRGERTFFDDLNKDLDRDGKSVqPLEL 600
Cdd:PLN00206 427 VLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAI-VFVNEEDRNLFPELVALLKSSGAAI-PREL 498
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
229-382 5.61e-21

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: 91.21  E-value: 5.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSN 308
Cdd:cd17940  38 DILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQ 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366  309 lEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGwcpkLMSHLktdkLDTLPGNVIKMIFSAT 382
Cdd:cd17940 117 -TVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP----IIEKI----LNFLPKERQILLFSAT 181
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
199-409 7.33e-21

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: 92.44  E-value: 7.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  199 PIQSIILDSILPVLNFTLNVSKRNFTRRIGDILVNAATGSGKTLAYSIPIVQTLfKRQ-----------------INRLR 261
Cdd:cd17965  33 PIQTLAIKKLLKTLMRKVTKQTSNEEPKLEVFLLAAETGSGKTLAYLAPLLDYL-KRQeqepfeeaeeeyesakdTGRPR 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  262 CIIIVPTKLLINQVYTTLTKLTQGTSLivSIAKLENSLKDEHKKLSNLEP---DILITTPGRLvdhLNMKSINLKNLK-- 336
Cdd:cd17965 112 SVILVPTHELVEQVYSVLKKLSHTVKL--GIKTFSSGFGPSYQRLQLAFKgriDILVTTPGKL---ASLAKSRPKILSrv 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  337 -FLIIDEADRLLNQSFqgwcpklmSHLKTDKLDTLPgNVIKMIF-SATLttnteklnglnlykPKLFLKQTDKLY 409
Cdd:cd17965 187 tHLVVDEADTLFDRSF--------LQDTTSIIKRAP-KLKHLILcSATI--------------PKEFDKTLRKLF 238
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
228-390 5.78e-20

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: 89.35  E-value: 5.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  228 GDILVNAATGSGKTLAYSIPIVQTLF------KRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSI---AKLENS 298
Cdd:cd17948  28 RNTLCAAETGSGKTLTYLLPIIQRLLrykllaEGPFNAPRGLVITPSRELAEQIGSVAQSLTEGLGLKVKVitgGRTKRQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  299 LKDEHKKlsnlEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHL--------KTDKLDtl 370
Cdd:cd17948 108 IRNPHFE----EVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRRFplasrrseNTDGLD-- 181
                       170       180
                ....*....|....*....|
gi 6324366  371 PGNVIKMIfSATLTTNTEKL 390
Cdd:cd17948 182 PGTQLVLV-SATMPSGVGEV 200
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
229-390 9.03e-19

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


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 85.45  E-value: 9.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTL-------FKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSL-IVSIAKLEnSLK 300
Cdd:cd17945  29 DIIGIAETGSGKTAAFLIPLLVYIsrlppldEETKDDGPYALILAPTRELAQQIEEETQKFAKPLGIrVVSIVGGH-SIE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  301 DEHKKLSNlEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTLPGNVIK---- 376
Cdd:cd17945 108 EQAFSLRN-GCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDAMPVSNKKPDTEEAEKlaas 186
                       170       180
                ....*....|....*....|..
gi 6324366  377 --------MIFSATLTTNTEKL 390
Cdd:cd17945 187 gkhryrqtMMFTATMPPAVEKI 208
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
172-398 2.84e-18

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


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 83.97  E-value: 2.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  172 KPFSDYAN-ELEAKLLQNICKNFSTNTFPIQSIILDSILpvlnftlnvSKRnftrrigDILVNAATGSGKTLAYSIPIVq 250
Cdd:cd17953   9 KPIQKWSQcGLSEKVLDLIKKLGYEKPTPIQAQALPAIM---------SGR-------DVIGIAKTGSGKTLAFLLPMF- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  251 tlfkRQINRLR---------CIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEhkkLSNLE--PDILITTPG 319
Cdd:cd17953  72 ----RHIKDQRpvkpgegpiGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQ---IAELKrgAEIVVCTPG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  320 RLVDHLNMKS---INLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTLpgnvikmiFSATLTTNTEKLNGLNLY 396
Cdd:cd17953 145 RMIDILTANNgrvTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVL--------FSATFPRKVEALARKVLH 216

                ..
gi 6324366  397 KP 398
Cdd:cd17953 217 KP 218
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
229-382 6.56e-18

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: 82.42  E-value: 6.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIP-IVQtlfkrqIN---RLR------CIIIVPTKLLINQVYTTLTKLTqGTSLIVSIAKLENS 298
Cdd:cd17966  29 DMVGIAQTGSGKTLAFLLPaIVH------INaqpPLErgdgpiVLVLAPTRELAQQIQQEANKFG-GSSRLRNTCVYGGA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  299 LKdeHKKLSNLE--PDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKlDTLpgnvik 376
Cdd:cd17966 102 PK--GPQIRDLRrgVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR-QTL------ 172

                ....*.
gi 6324366  377 mIFSAT 382
Cdd:cd17966 173 -MWSAT 177
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
229-386 7.33e-17

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: 79.23  E-value: 7.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQ-GTSLIVSIAKLENSLKDEHKKLS 307
Cdd:cd17943  29 DLIVQAKSGTGKTLVFVVIALESL-DLERRHPQVLILAPTREIAVQIHDVFKKIGKkLEGLKCEVFIGGTPVKEDKKKLK 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  308 NlePDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLktdkldtlpGNVIKMI-FSATLTTN 386
Cdd:cd17943 108 G--CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL---------PKNKQVIaFSATYPKN 176
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
500-563 2.69e-16

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: 74.94  E-value: 2.69e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366    500 KAENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARAN 563
Cdd:pfam00271  50 QEEREEILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
229-398 4.96e-16

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: 76.82  E-value: 4.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINRLrCIIIVPTKLLINQVYTTLTKLTQG-----TSLIVSIAKLENSLkdeH 303
Cdd:cd17962  29 DILASADTGSGKTAAFLLPVIIRCLTEHRNPS-ALILTPTRELAVQIEDQAKELMKGlppmkTALLVGGLPLPPQL---Y 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  304 KKLSNLEpdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQgwcPKLMshlktDKLDTLPGNVIKMIFSATL 383
Cdd:cd17962 105 RLQQGVK--VIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQ---QQVL-----DILENISHDHQTILVSATI 174
                       170
                ....*....|....*
gi 6324366  384 TTNTEKLNGLNLYKP 398
Cdd:cd17962 175 PRGIEQLAGQLLQNP 189
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
229-352 7.90e-16

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: 76.21  E-value: 7.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSN 308
Cdd:cd17939  36 DVIAQAQSGTGKTATFSIGALQRI-DTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQY 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6324366  309 lEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQ 352
Cdd:cd17939 115 -GPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFK 157
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
229-370 1.74e-15

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: 75.19  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIP-----IVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTslIVSIAKLENSLKDEH 303
Cdd:cd17958  29 DLIGVAQTGTGKTLAYLLPgfihlDLQPIPREQRNGPGVLVLTPTRELALQIEAECSKYSYKG--LKSVCVYGGGNRNEQ 106
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324366  304 KKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTL 370
Cdd:cd17958 107 IEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRPDRQTIM 173
HELICc smart00490
helicase superfamily c-terminal domain;
500-563 2.15e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.47  E-value: 2.15e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366     500 KAENKKIVANFSHHSesagITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARAN 563
Cdd:smart00490  23 QEEREEILDKFNNGK----IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
220-610 2.73e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 79.30  E-value: 2.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  220 KRNFTRRIGDILVNAATGSGKTLaysipIVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTqGTSLIVSIAKlensl 299
Cdd:COG1061  93 LAALERGGGRGLVVAPTGTGKTV-----LALALAAELLRGKRVLVLVPRRELLEQWAEELRRFL-GDPLAGGGKK----- 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  300 kdehkklsNLEPDILITTPGRLVDHLNMKSINlKNLKFLIIDEADRLLNQSFQgwcpKLMSHLK-------------TDK 366
Cdd:COG1061 162 --------DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYR----RILEAFPaayrlgltatpfrSDG 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  367 LDTLPGNVIKMIFSATLTtntEKLNGlNLYKPKLFLKQTDKLYQLPNKLNEFNINIPTA---KSVYKPLILlysiCQFMA 443
Cdd:COG1061 229 REILLFLFDGIVYEYSLK---EAIED-GYLAPPEYYGIRVDLTDERAEYDALSERLREAlaaDAERKDKIL----RELLR 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  444 HSPIAAKILIFVKSNESSIRLSKLLQLICES----RSQSSvlknlqnlavsinsvnsnnsKAENKKIVANFshhsESAGI 519
Cdd:COG1061 301 EHPDDRKTLVFCSSVDHAEALAELLNEAGIRaavvTGDTP--------------------KKEREEILEAF----RDGEL 356
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  520 TILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSA---YNlLVGRGERTFFDDLNKDLDRDGKSVQ 596
Cdd:COG1061 357 RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDalvYD-FVGNDVPVLEELAKDLRDLAGYRVE 435
                       410
                ....*....|....
gi 6324366  597 PLELDFTLLESDSE 610
Cdd:COG1061 436 FLDEEESEELALLI 449
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
229-342 3.33e-15

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: 73.77  E-value: 3.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKL--ENSLKDEHKKL 306
Cdd:cd17922   3 NVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRhgDTSQSEKAKQL 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6324366  307 SNLePDILITTPGRLVDHLNMKSIN--LKNLKFLIIDE 342
Cdd:cd17922  83 KNP-PGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
231-382 1.11e-14

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 71.67  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  231 LVNAATGSGKTLAYSIPIVQTLFKRqinRLRCIIIVPTKLLINQVYTTLTKLTQGTsliVSIAKLENSLKDEHK-KLSNL 309
Cdd:cd00046   5 LITAPTGSGKTLAALLAALLLLLKK---GKKVLVLVPTKALALQTAERLRELFGPG---IRVAVLVGGSSAEEReKNKLG 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324366  310 EPDILITTPGRLVDHLN-MKSINLKNLKFLIIDEADRLLNQSFQGWcpklMSHLKTDKLdtLPGNVIKMIFSAT 382
Cdd:cd00046  79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGAL----ILDLAVRKA--GLKNAQVILLSAT 146
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
229-382 5.00e-14

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


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 71.03  E-value: 5.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINRLR-----CIIIVPTKLLINQVYTTLTKLTQ---------GTSLIVSIAK 294
Cdd:cd17944  29 DLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRgrapkVLVLAPTRELANQVTKDFKDITRklsvacfygGTPYQQQIFA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  295 LENSLkdehkklsnlepDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMS-HLKTDKLDtlpgN 373
Cdd:cd17944 109 IRNGI------------DILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSED----N 172

                ....*....
gi 6324366  374 VIKMIFSAT 382
Cdd:cd17944 173 PQTLLFSAT 181
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
229-366 1.29e-13

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


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 70.81  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIV-----QTLFKRQINRLrCIIIVPTKLLINQVYTTLTKLTQGTSL----IVSIAKLENSL 299
Cdd:cd18049  63 DMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPI-CLVLAPTRELAQQVQQVAAEYGRACRLkstcIYGGAPKGPQI 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324366  300 KDEHKKLsnlepDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDK 366
Cdd:cd18049 142 RDLERGV-----EICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 203
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
229-383 1.80e-13

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: 69.68  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRQINRLRC-------IIIVPTKLLINQVYTTLTKLTQ----------GTSLIV- 290
Cdd:cd17951  29 DMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIkgegpygLIVCPSRELARQTHEVIEYYCKalqeggypqlRCLLCIg 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  291 --SIAKLENSLKDE-HkklsnlepdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKtdkl 367
Cdd:cd17951 109 gmSVKEQLEVIRKGvH---------IVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIFSYFK---- 175
                       170
                ....*....|....*.
gi 6324366  368 dtlpGNVIKMIFSATL 383
Cdd:cd17951 176 ----GQRQTLLFSATM 187
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
230-382 2.07e-13

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: 69.14  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  230 ILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAklensLKDEHKKLS-N 308
Cdd:cd17963  36 LIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQALCLAPTRELARQIGEVVEKMGKFTGVKVALA-----VPGNDVPRGkK 109
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  309 LEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLN-QSFQGWCPKLMSHlktdkldtLPGNVIKMIFSAT 382
Cdd:cd17963 110 ITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGDQSIRIKRM--------LPRNCQILLFSAT 176
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
192-366 2.74e-13

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: 70.42  E-value: 2.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  192 NFSTNTFP--IQSIILD------SILPVLNFTLNVSKRnftrrigDILVNAATGSGKTLAYSIPIV-----QTLFKRQIN 258
Cdd:cd18050  63 AFHQANFPqyVMDVLLDqnfkepTPIQCQGFPLALSGR-------DMVGIAQTGSGKTLAYLLPAIvhinhQPYLERGDG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  259 RLrCIIIVPTKLLINQV------YTTLTKLTqgTSLIVSIAKLENSLKDEHKKLsnlepDILITTPGRLVDHLNMKSINL 332
Cdd:cd18050 136 PI-CLVLAPTRELAQQVqqvaddYGKSSRLK--STCIYGGAPKGPQIRDLERGV-----EICIATPGRLIDFLEAGKTNL 207
                       170       180       190
                ....*....|....*....|....*....|....
gi 6324366  333 KNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDK 366
Cdd:cd18050 208 RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
229-382 1.96e-12

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: 67.37  E-value: 1.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFK-----------RQINRLR----CIIIVPTKLLINQVYTTLTKLTQGTSLIVSI- 292
Cdd:cd18051  60 DLMACAQTGSGKTAAFLLPILSQIYEqgpgeslpsesGYYGRRKqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVv 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  293 ---AKLENSLKDehkklsnLEP--DILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQgwcPKLMSHLKTdkl 367
Cdd:cd18051 140 yggADIGQQMRD-------LERgcHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFE---PQIRRIVEQ--- 206
                       170
                ....*....|....*..
gi 6324366  368 DTLP--GNVIKMIFSAT 382
Cdd:cd18051 207 DTMPptGERQTLMFSAT 223
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
229-343 3.33e-12

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: 65.30  E-value: 3.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRqiNRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKL--ENSLKDEHKKL 306
Cdd:cd17923  17 SVVVTTGTASGKSLCYQLPILEALLRD--PGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVATYdgDTPREERRAII 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6324366  307 SNlEPDILITTPGRLvdHLNM------KSINLKNLKFLIIDEA 343
Cdd:cd17923  95 RN-PPRILLTNPDML--HYALlphhdrWARFLRNLRYVVLDEA 134
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
228-349 3.59e-12

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: 65.83  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  228 GDILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQV---YTTLTKLTQGTSLIV-----SIAKLENSL 299
Cdd:cd17950  40 MDVLCQAKSGMGKTAVFVLSTLQQL-EPVDGQVSVLVICHTRELAFQIsneYERFSKYMPNVKTAVffggvPIKKDIEVL 118
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6324366  300 KDEHkklsnlePDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQ 349
Cdd:cd17950 119 KNKC-------PHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQ 161
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
229-383 7.14e-12

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: 64.77  E-value: 7.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLfKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSN 308
Cdd:cd18046  38 DVIAQAQSGTGKTATFSISILQQI-DTSLKATQALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  309 lEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCpklmshlkTDKLDTLPGNVIKMIFSATL 383
Cdd:cd18046 117 -GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQI--------YDIFQKLPPDTQVVLLSATM 182
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
229-352 8.59e-12

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: 64.80  E-value: 8.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTlFKRQINRLRCIIIVPTKLLINQVYTTLTKLtqGTSLIVSI-AKLE-NSLKDEHKKL 306
Cdd:cd18045  38 DVIAQSQSGTGKTATFSISVLQC-LDIQVRETQALILSPTRELAVQIQKVLLAL--GDYMNVQChACIGgTSVGDDIRKL 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6324366  307 SNLEpDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQ 352
Cdd:cd18045 115 DYGQ-HIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
198-354 2.67e-10

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: 59.97  E-value: 2.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  198 FPIQSIILDSILPvlnftlnvSKRNFtrrigdiLVNAATGSGKTLAYSIPIVQTLFKrqiNRLRCIIIVPTKLLINQVYT 277
Cdd:cd17921   3 NPIQREALRALYL--------SGDSV-------LVSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  278 TLTKLTQGTSLIVSIAKLENSLKDEHKklsnLEPDILITTPGRLvdhLNM----KSINLKNLKFLIIDEAdRLLNQSFQG 353
Cdd:cd17921  65 DLRERFGPLGKNVGLLTGDPSVNKLLL----AEADILVATPEKL---DLLlrngGERLIQDVRLVVVDEA-HLIGDGERG 136

                .
gi 6324366  354 W 354
Cdd:cd17921 137 V 137
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
229-343 1.93e-09

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: 60.62  E-value: 1.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPIVQTLFKRqiNRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSN 308
Cdd:COG1205  73 NVVIATPTASGKSLAYLLPVLEALLED--PGATALYLYPTKALARDQLRRLRELAEALGLGVRVATYDGDTPPEERRWIR 150
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6324366  309 LEPDILITTPgrlvDHLNMkSI---------NLKNLKFLIIDEA 343
Cdd:COG1205 151 EHPDIVLTNP----DMLHY-GLlphhtrwarFFRNLRYVVIDEA 189
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
234-350 3.51e-09

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: 56.57  E-value: 3.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  234 AATGSGKT---LAYSIPIVQtlfKRQinrlRCIIIVPTKLLINQVYTTLTKLTQGTS----LIVSIAKLENSLKDE-HKK 305
Cdd:cd17924  39 APTGVGKTtfgLATSLYLAS---KGK----RSYLIFPTKSLVKQAYERLSKYAEKAGvevkILVYHSRLKKKEKEElLEK 111
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6324366  306 LSNLEPDILITTPGRLvdHLNMKSINLKNLKFLIIDEADRLLNQS 350
Cdd:cd17924 112 IEKGDFDILVTTNQFL--SKNFDLLSNKKFDFVFVDDVDAVLKSS 154
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
230-343 5.23e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 59.14  E-value: 5.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  230 ILVNAATGSGKTLAYSIPIVQTLFkrqiNRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEhkKLSNl 309
Cdd:COG1204  41 LVVSAPTASGKTLIAELAILKALL----NGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGR- 113
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6324366  310 ePDILITTPGRLvDHLNMKSIN-LKNLKFLIIDEA 343
Cdd:COG1204 114 -YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
506-573 3.63e-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: 50.78  E-value: 3.63e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  506 IVANFSHHSESAG--ITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLLV 573
Cdd:cd18785   8 VFTNSIEHAEEIAssLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
ResIII pfam04851
Type III restriction enzyme, res subunit;
230-346 7.21e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 52.29  E-value: 7.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366    230 ILVNAATGSGKTLAySIPIVQTLFKRQINRlRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIaklensLKDEHKKLSNL 309
Cdd:pfam04851  26 GLIVMATGSGKTLT-AAKLIARLFKKGPIK-KVLFLVPRKDLLEQALEEFKKFLPNYVEIGEI------ISGDKKDESVD 97
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6324366    310 EPDILITTPGRLVDHLNMKSINLKNLKF--LIIDEADRL 346
Cdd:pfam04851  98 DNKIVVTTIQSLYKALELASLELLPDFFdvIIIDEAHRS 136
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
158-383 1.24e-06

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 51.62  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  158 WLNTEKIYYDNSLIKpfSDYANELEAKLLQNicKNFSTNTFPIQSIILDSILPvlnftlnvskrNFTRRIGDILVNAATG 237
Cdd:COG1203  93 WLDSANFDMARQALD--HLLAERLERLLPKK--SKPRTPINPLQNEALELALE-----------AAEEEPGLFILTAPTG 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  238 SGKTLAySIPIVQTLFKRQINRlRCIIIVPTKLLINQVYTTLTKLTqGTSLI-------VSIAKLENSLKDEHKKLS--- 307
Cdd:COG1203 158 GGKTEA-ALLFALRLAAKHGGR-RIIYALPFTSIINQTYDRLRDLF-GEDVLlhhsladLDLLEEEEEYESEARWLKllk 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  308 -NLEPDILITTpgrlVDHL-----------NMKSINLKNlKFLIIDEAdrllnQSFQgwcPKLMSHLKT--DKLDTLPGN 373
Cdd:COG1203 235 eLWDAPVVVTT----IDQLfeslfsnrkgqERRLHNLAN-SVIILDEV-----QAYP---PYMLALLLRllEWLKNLGGS 301
                       250
                ....*....|
gi 6324366  374 VIKMifSATL 383
Cdd:COG1203 302 VILM--TATL 309
PRK13767 PRK13767
ATP-dependent helicase; Provisional
230-342 5.62e-06

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 49.50  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366   230 ILVNAATGSGKTLAYSIPIVQTLFKRQI-----NRLRCIIIVPTKLLINQVYTTLTKLTQGtslIVSIAKLENSLKDE-- 302
Cdd:PRK13767  50 VLISSPTGSGKTLAAFLAIIDELFRLGRegeleDKVYCLYVSPLRALNNDIHRNLEEPLTE---IREIAKERGEELPEir 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6324366   303 ----------HKKLSNLE--PDILITTPGRLVDHLNMKSIN--LKNLKFLIIDE 342
Cdd:PRK13767 127 vairtgdtssYEKQKMLKkpPHILITTPESLAILLNSPKFRekLRTVKWVIVDE 180
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
229-383 6.95e-06

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: 47.71  E-value: 6.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYsipIVQTLFKRQINRL--RCIIIVPT---KLLINQVYTTLTKLTQGTSLIVSIAKlenslkDEH 303
Cdd:cd18048  59 NLIAQSQSGTGKTAAF---VLAMLSRVDALKLypQCLCLSPTfelALQTGKVVEEMGKFCVGIQVIYAIRG------NRP 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  304 KKLSNLEPDILITTPGRLVDH-LNMKSINLKNLKFLIIDEADRLLN-QSFQGWCPKLMShlktdkldTLPGNVIKMIFSA 381
Cdd:cd18048 130 GKGTDIEAQIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMINvQGHSDHSVRVKR--------SMPKECQMLLFSA 201

                ..
gi 6324366  382 TL 383
Cdd:cd18048 202 TF 203
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
231-346 2.05e-05

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: 44.99  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  231 LVNAATGSGKTLAySIPIVQTLFKRqinrlRCIIIVPTKLLINQVYTTLTKLTQGTSLivsiaKLENSLKDEHKKLSNle 310
Cdd:cd17926  22 ILVLPTGSGKTLT-ALALIAYLKEL-----RTLIVVPTDALLDQWKERFEDFLGDSSI-----GLIGGGKKKDFDDAN-- 88
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6324366  311 pdILITTPGRLVDHLNMKSINLKNLKFLIIDEADRL 346
Cdd:cd17926  89 --VVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL 122
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
230-342 4.35e-05

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: 44.63  E-value: 4.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  230 ILVNAATGSGKTLAYSIPIVQTLfkrqINRLRCIIIVPTKLLINQVYTTLTKLTQ-GTSLIVSIAKLENslKDEHKKlsn 308
Cdd:cd18028  20 LLISIPTASGKTLIAEMAMVNTL----LEGGKALYLVPLRALASEKYEEFKKLEEiGLKVGISTGDYDE--DDEWLG--- 90
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6324366  309 lEPDILITTPGRLvDHLNMKSIN-LKNLKFLIIDE 342
Cdd:cd18028  91 -DYDIIVATYEKF-DSLLRHSPSwLRDVGVVVVDE 123
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
229-343 4.94e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 44.56  E-value: 4.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLaysIPIVQTL-FKRQINRL-----RCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDE 302
Cdd:cd18034  18 NTIVVLPTGSGKTL---IAVMLIKeMGELNRKEknpkkRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYSGEMGVDKWTKE 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6324366  303 HKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEA 343
Cdd:cd18034  95 RWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
229-343 5.38e-04

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: 41.75  E-value: 5.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAYSIPivqTLFKRQInrlrCIIIVPTKLLIN-QVyttlTKLTQgtsLIVSIAKLENSLKDEHK--- 304
Cdd:cd17920  29 DVLVVMPTGGGKSLCYQLP---ALLLDGV----TLVVSPLISLMQdQV----DRLQQ---LGIRAAALNSTLSPEEKrev 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6324366  305 --KLSNLEPDILITTPGRLVDHLNMKSIN----LKNLKFLIIDEA 343
Cdd:cd17920  95 llRIKNGQYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEA 139
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
502-561 1.09e-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: 39.65  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  502 ENKKIVANFshhsESAGITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTAR 561
Cdd:cd18801  78 EQKEVIEQF----RKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
519-573 1.10e-03

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: 39.88  E-value: 1.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  519 ITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRtARANelGSAYNLLV 573
Cdd:cd18802  91 LNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAP--NSKYILMV 142
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
200-342 1.43e-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: 40.42  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  200 IQSIILDSILPvlnftlnvSKRNFtrrigdiLVNAATGSGKTLAYSIPIVQTLFKRQIN---RLRCIIIVPTKLLINQVY 276
Cdd:cd18023   5 IQSEVFPDLLY--------SDKNF-------VVSAPTGSGKTVLFELAILRLLKERNPLpwgNRKVVYIAPIKALCSEKY 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324366  277 TTLT-KLTQgtsLIVSIAKL--ENSLKDEhKKLSNLepDILITTPGRLvDHLNMKSINLKNL----KFLIIDE 342
Cdd:cd18023  70 DDWKeKFGP---LGLSCAELtgDTEMDDT-FEIQDA--DIILTTPEKW-DSMTRRWRDNGNLvqlvALVLIDE 135
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
211-345 1.78e-03

DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. It 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: 350788 [Multi-domain]  Cd Length: 208  Bit Score: 40.29  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  211 VLNFTLNVSKRNFTRRIGdiLVNAATGSGKTLaysipivqTLFK------RQINRLRCIIIVPTKLLINQVYTTLTKLtq 284
Cdd:cd18030  33 ALERIKTATNKDGDKKGG--YIWHTQGSGKSL--------TMFKaaklliEDPKNPKVVFVVDRKDLDYQTSSTFSRF-- 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324366  285 gTSLIVSIAKLENSLKDEhkkLSNLEPDILITTP---GRLV-DHLNMKSINLKNLkFLIIDEADR 345
Cdd:cd18030 101 -AAEDVVRANSTKELKEL---LKNLSGGIIVTTIqkfNNAVkEESKPVLIYRKNI-VVIVDEAHR 160
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
229-468 1.86e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.88  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  229 DILVNAATGSGKTLAySIPIVQTLFKRQInRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKL----ENSLKDEHK 304
Cdd:cd09639   1 LLVIEAPTGYGKTEA-ALLWALHSLKSQK-ADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSsrikEMGDSEEFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  305 KLSNL----------------EPDILITTPGRLVDHLNMKSINLKNlKFLIIDEADrLLNQSFQGWCPKLMSHLKtDKld 368
Cdd:cd09639  79 HLFPLyihsndtlfldpitvcTIDQVLKSVFGEFGHYEFTLASIAN-SLLIFDEVH-FYDEYTLALILAVLEVLK-DN-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  369 tlpgNVIKMIFSATLTTNTEKLNGLNLY--KPKLFLKQTDKLYQLPNKLNEFNINIPtaksvykplillySICQFMAHSP 446
Cdd:cd09639 154 ----DVPILLMSATLPKFLKEYAEKIGYveENEPLDLKPNERAPFIKIESDKVGEIS-------------SLERLLEFIK 216
                       250       260
                ....*....|....*....|..
gi 6324366  447 IAAKILIFVKSNESSIRLSKLL 468
Cdd:cd09639 217 KGGSVAIIVNTVDRAQEFYQQL 238
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
228-383 3.18e-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: 39.20  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  228 GDILVNAATGSGKTLAYSIPIvQTLFKRQINRlRCIIIVPTKLLINQVYTTLTKLTQ--GTSLIVSIAKLENSLKDEHKK 305
Cdd:cd17930   2 GLVILEAPTGSGKTEAALLWA-LKLAARGGKR-RIIYALPTRATINQMYERIREILGrlDDEDKVLLLHSKAALELLESD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  306 LS-----------------NLEPDILITTPGRL------VDHLNMKSINLKNlKFLIIDEAdrllnQSFQgwcPKLMS-H 361
Cdd:cd17930  80 EEpdddpveavdwalllkrSWLAPIVVTTIDQLlesllkYKHFERRLHGLAN-SVVVLDEV-----QAYD---PEYMAlL 150
                       170       180
                ....*....|....*....|....
gi 6324366  362 LKT--DKLDTLPGNVIKMifSATL 383
Cdd:cd17930 151 LKAllELLGELGGPVVLM--TATL 172
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
182-345 6.04e-03

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: 38.17  E-value: 6.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  182 EAKLLQNICKNFSTNTFPIQSIILDSILPVLNftlnvSKRNFTRrigdiLVNAATGSGKTLAYSIPIVQTLfkrqINRLR 261
Cdd:cd17918   1 DRALIQELCKSLPFSLTKDQAQAIKDIEKDLH-----SPEPMDR-----LLSGDVGSGKTLVALGAALLAY----KNGKQ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324366  262 CIIIVPTKLLINQVYTTLTK-LTQGTSLIVSIAKLENSLKdehkklsnlEPDILITTPGRLvdHLNMKSinlKNLKFLII 340
Cdd:cd17918  67 VAILVPTEILAHQHYEEARKfLPFINVELVTGGTKAQILS---------GISLLVGTHALL--HLDVKF---KNLDLVIV 132

                ....*
gi 6324366  341 DEADR 345
Cdd:cd17918 133 DEQHR 137
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
519-561 7.47e-03

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 37.63  E-value: 7.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6324366  519 ITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTAR 561
Cdd:cd18796  95 LKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
519-564 8.16e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 39.33  E-value: 8.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6324366  519 ITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANE 564
Cdd:COG1111 412 FNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE 457
 
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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