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Conserved domains on  [gi|967504803|ref|XP_014982568|]
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DEAD box protein 53 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
231-623 1.33e-140

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 415.70  E-value: 1.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQRNGPGMLVLTPTRELAL 310
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:COG0513   86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 390 IMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNlAAVNTVKQNIIVTTEEEKRALTQEFIENMSPnDK 469
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN-ATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 470 VIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIE 549
Cdd:COG0513  244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967504803 550 EYVHRVGRIGRAGKTGTSVTLITQRDAKMageLIKILERANQSVPEDLVVIAEQYKLNQQKRDTETRSRKPGQR 623
Cdd:COG0513  324 DYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGK 394
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
50-115 2.42e-26

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. 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.


:

Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 101.98  E-value: 2.42e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  50 PLCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEALVRIFGNREMKAKAKAIIETLTRK 115
Cdd:cd22430    1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
231-623 1.33e-140

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 415.70  E-value: 1.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQRNGPGMLVLTPTRELAL 310
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:COG0513   86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 390 IMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNlAAVNTVKQNIIVTTEEEKRALTQEFIENMSPnDK 469
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN-ATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 470 VIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIE 549
Cdd:COG0513  244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967504803 550 EYVHRVGRIGRAGKTGTSVTLITQRDAKMageLIKILERANQSVPEDLVVIAEQYKLNQQKRDTETRSRKPGQR 623
Cdd:COG0513  324 DYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGK 394
PTZ00110 PTZ00110
helicase; Provisional
170-611 6.29e-138

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 413.40  E-value: 6.29e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 170 DLPPVKKNFYIESKATSCMSEMQVINWRKENfnimcdDLKSGEKRLIPKPTCRF-KDAFQQYpdLLKSITRVGFVKPTPI 248
Cdd:PTZ00110  85 NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK------EITIIAGENVPKPVVSFeYTSFPDY--ILKSLKNAGFTEPTPI 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 249 QSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQrNGPGMLVLTPTRELALQVEAECSKYSYKD-LKSI 327
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG-DGPIVLVLAPTRELAEQIREQCNKFGASSkIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 328 CICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHPDRQTVMIS 407
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 408 ATWPDTVRRLARSYLKD-PMIVYVGNLNLAAVNTVKQNIIVTTEEEKRALTQEFIEN-MSPNDKVIMFVSQKRIADDLSS 485
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADFLTK 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 486 DFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTG 565
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKG 475
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 967504803 566 TSVTLITQRDAKMAGELIKILERANQSVPEDLVVIAEQYKLNQQKR 611
Cdd:PTZ00110 476 ASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERR 521
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
233-429 8.62e-128

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: 374.49  E-value: 8.62e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYSYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMK 392
Cdd:cd17958   81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 393 ILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVY 429
Cdd:cd17958  161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
246-417 2.00e-52

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: 177.43  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803  246 TPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDsqplsrEQRNGPGMLVLTPTRELALQVEAECSKY-SYKDL 324
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD------KLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803  325 KSICICGGRNRIGQIEDIsKDVDIIIATPGRLNDLqMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHPDRQTV 404
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 967504803  405 MISATWPDTVRRL 417
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
237-435 3.50e-47

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 164.59  E-value: 3.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803   237 ITRVGFVKPTPIQSQAWPIILQGI-DLIEVAQTGTGKTLSYLMPGFIHVDSQPlsreqrnGPGMLVLTPTRELALQVEAE 315
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGK-------GGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803   316 CSKY-SYKDLKSICICGGRNRIGQIEDI-SKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKI 393
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 967504803   394 LLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNL 435
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
50-115 2.42e-26

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. 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.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 101.98  E-value: 2.42e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  50 PLCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEALVRIFGNREMKAKAKAIIETLTRK 115
Cdd:cd22430    1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
53-110 9.14e-11

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 57.68  E-value: 9.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967504803   53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEA---LVRIFGNREMKAKAKAIIE 110
Cdd:pfam00013   4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGnerIVTITGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
53-110 2.25e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803    53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQII-KGESEALVRIFGNREMKAKAKAIIE 110
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPgPGSEERVVEITGPPENVEKAAELIL 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
51-115 6.01e-07

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 52.74  E-value: 6.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  51 LCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIikgESEALVRIFG-NREMKAKAKAIIETLTRK 115
Cdd:PRK11824 556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDI---EDDGTVKIAAtDGEAAEAAKERIEGITAE 618
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
231-623 1.33e-140

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 415.70  E-value: 1.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQRNGPGMLVLTPTRELAL 310
Cdd:COG0513   11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:COG0513   86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 390 IMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNlAAVNTVKQNIIVTTEEEKRALTQEFIENMSPnDK 469
Cdd:COG0513  166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPEN-ATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 470 VIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIE 549
Cdd:COG0513  244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967504803 550 EYVHRVGRIGRAGKTGTSVTLITQRDAKMageLIKILERANQSVPEDLVVIAEQYKLNQQKRDTETRSRKPGQR 623
Cdd:COG0513  324 DYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGK 394
PTZ00110 PTZ00110
helicase; Provisional
170-611 6.29e-138

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 413.40  E-value: 6.29e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 170 DLPPVKKNFYIESKATSCMSEMQVINWRKENfnimcdDLKSGEKRLIPKPTCRF-KDAFQQYpdLLKSITRVGFVKPTPI 248
Cdd:PTZ00110  85 NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK------EITIIAGENVPKPVVSFeYTSFPDY--ILKSLKNAGFTEPTPI 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 249 QSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQrNGPGMLVLTPTRELALQVEAECSKYSYKD-LKSI 327
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG-DGPIVLVLAPTRELAEQIREQCNKFGASSkIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 328 CICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHPDRQTVMIS 407
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 408 ATWPDTVRRLARSYLKD-PMIVYVGNLNLAAVNTVKQNIIVTTEEEKRALTQEFIEN-MSPNDKVIMFVSQKRIADDLSS 485
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADFLTK 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 486 DFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTG 565
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKG 475
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 967504803 566 TSVTLITQRDAKMAGELIKILERANQSVPEDLVVIAEQYKLNQQKR 611
Cdd:PTZ00110 476 ASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERR 521
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
233-429 8.62e-128

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: 374.49  E-value: 8.62e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYSYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMK 392
Cdd:cd17958   81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 393 ILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVY 429
Cdd:cd17958  161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
233-428 6.83e-90

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: 277.02  E-value: 6.83e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPlsREQRNGPGMLVLTPTRELALQV 312
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIM 391
Cdd:cd00268   79 AEVARKLGkGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 392 KILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd00268  159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
233-428 6.75e-85

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: 264.23  E-value: 6.75e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLsREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPP-LERGDGPIVLVLAPTRELAQQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYSYK-DLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIM 391
Cdd:cd17966   80 QQEANKFGGSsRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 392 KILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
231-588 2.87e-83

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 268.99  E-value: 2.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNGPGMLVLTPTRELAL 310
Cdd:PRK10590  10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTRELAA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:PRK10590  90 QIGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 390 IMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNLAAvNTVKQNIIVTTEEEKRALTQEFIEnmSPN-D 468
Cdd:PRK10590 170 IRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTAS-EQVTQHVHFVDKKRKRELLSQMIG--KGNwQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 469 KVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNI 548
Cdd:PRK10590 247 QVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 967504803 549 EEYVHRVGRIGRAGKTGTSVTLITQRDAKMAGELIKILER 588
Cdd:PRK10590 327 EDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
217-431 5.21e-75

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: 239.91  E-value: 5.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 217 PKPTCRFKDAfqQYP-DLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLsREQRN 295
Cdd:cd18049   20 PKPVLNFYEA--NFPaNVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF-LERGD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 296 GPGMLVLTPTRELALQVEAECSKYSYK-DLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLV 374
Cdd:cd18049   97 GPICLVLAPTRELAQQVQQVAAEYGRAcRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLV 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 375 MDEADKMLDMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVG 431
Cdd:cd18049  177 LDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
231-582 8.20e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 247.02  E-value: 8.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKT-------LSYLMPGFIHVDSqplsreqrngpgmLVLT 303
Cdd:PRK11776  13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTaafglglLQKLDVKRFRVQA-------------LVLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 304 PTRELALQVEAECSKY--SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKM 381
Cdd:PRK11776  80 PTRELADQVAKEIRRLarFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 382 LDMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPmivyvgnlnlaavntvkQNIIVTTEEEKRALTQEFI 461
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDP-----------------VEVKVESTHDLPAIEQRFY 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 462 EnMSPNDK---------------VIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDL 526
Cdd:PRK11776 223 E-VSPDERlpalqrlllhhqpesCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDV 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803 527 VARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLITQRDAKMAGEL 582
Cdd:PRK11776 302 AARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
193-588 1.16e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 247.13  E-value: 1.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 193 VINWRKENFNIMCDDLKSgekrlipkptcRFKDaFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGK 272
Cdd:PRK01297  70 ASLWKLEDFVVEPQEGKT-----------RFHD-FNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 273 TLSYLMPGFIHVDSQPLSREQRNG-PGMLVLTPTRELALQVE---AECSKYSykDLKSICICGGRNRIGQIEDI-SKDVD 347
Cdd:PRK01297 138 TAAFLISIINQLLQTPPPKERYMGePRALIIAPTRELVVQIAkdaAALTKYT--GLNVMTFVGGMDFDKQLKQLeARFCD 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 348 IIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHP--DRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:PRK01297 216 ILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDP 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 426 MIVYVGNLNLAAvNTVKQNIIVTTEEEKRALTQEFIeNMSPNDKVIMFVSQK----RIADDLSSDfniqGISVESLHGNS 501
Cdd:PRK01297 296 AIVEIEPENVAS-DTVEQHVYAVAGSDKYKLLYNLV-TQNPWERVMVFANRKdevrRIEERLVKD----GINAAQLSGDV 369
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 502 EESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLITQRDAKMAGE 581
Cdd:PRK01297 370 PQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPE 449

                 ....*..
gi 967504803 582 LIKILER 588
Cdd:PRK01297 450 IEELLGR 456
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
232-426 4.89e-74

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: 236.89  E-value: 4.89e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 232 DLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQrNGPGMLVLTPTRELALQ 311
Cdd:cd17953   22 KVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPG-EGPIGLIMAPTRELALQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 312 VEAECSKYSYK-DLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNS---VNLRSITYLVMDEADKMLDMEFE 387
Cdd:cd17953  101 IYVECKKFSKAlGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMGFE 180
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 967504803 388 PQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPM 426
Cdd:cd17953  181 PQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
227-580 9.80e-72

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 237.92  E-value: 9.80e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 227 FQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPlsREQRNGPGMLVLTPTR 306
Cdd:PRK11192   6 LELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP--RRKSGPPRILILTPTR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 307 ELALQVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDME 385
Cdd:PRK11192  84 ELAMQVADQARELAkHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 386 FEPQIMKILLDVHPDRQTVMISATWP-DTVRRLARSYLKDPMIVyvgnlNLAAVNTVKQNI-----IVTTEEEKRALTQE 459
Cdd:PRK11192 164 FAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV-----EAEPSRRERKKIhqwyyRADDLEHKTALLCH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 460 FIENMSPnDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHV 539
Cdd:PRK11192 239 LLKQPEV-TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 967504803 540 YNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLITQRDAKMAG 580
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLG 358
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
222-570 4.25e-70

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 233.32  E-value: 4.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 222 RFKDaFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSRE-QRNGPGML 300
Cdd:PRK04837   9 KFSD-FALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrKVNQPRAL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 301 VLTPTRELALQVeaecskysYKD---------LKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSIT 371
Cdd:PRK04837  88 IMAPTRELAVQI--------HADaeplaqatgLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 372 YLVMDEADKMLDMEFEPQImKILLDVHPD---RQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNLAAVNtVKQNIIVT 448
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDI-RWLFRRMPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHR-IKEELFYP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 449 TEEEKRALTQEFIENMSPnDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVA 528
Cdd:PRK04837 238 SNEEKMRLLQTLIEEEWP-DRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 967504803 529 RGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTL 570
Cdd:PRK04837 317 RGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
166-431 8.88e-70

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: 227.59  E-value: 8.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 166 RKW--ADLPPVKKNFYIESKATSCMSEMQVINWR-KENFNImcddlksgEKRLIPKPTCRFKDA-FQQYpdLLKSITRVG 241
Cdd:cd18050   12 KKWdlSELPKFEKNFYVEHPEVARMTQYDVEELRrKKEITI--------RGVGCPKPVFAFHQAnFPQY--VMDVLLDQN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 242 FVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLsREQRNGPGMLVLTPTRELALQVEAECSKYSY 321
Cdd:cd18050   82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY-LERGDGPICLVLAPTRELAQQVQQVADDYGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 322 KD-LKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHPD 400
Cdd:cd18050  161 SSrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 967504803 401 RQTVMISATWPDTVRRLARSYLKDPMIVYVG 431
Cdd:cd18050  241 RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
231-431 4.18e-67

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: 218.51  E-value: 4.18e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPgFIHV---DSQPLSREQRNG--PGMLVLTPT 305
Cdd:cd17967    9 ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLP-IISKlleDGPPSVGRGRRKayPSALILAPT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 306 RELALQVEAECSKYSYKD-LKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDM 384
Cdd:cd17967   88 RELAIQIYEEARKFSYRSgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDM 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 967504803 385 EFEPQIMKILLdvHPD------RQTVMISATWPDTVRRLARSYLKDPMIVYVG 431
Cdd:cd17967  168 GFEPQIRKIVE--HPDmppkgeRQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
233-429 1.23e-66

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: 217.19  E-value: 1.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQP--LSREQRNGPGMLVLTPTRELAL 310
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPplDEETKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKY-SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:cd17945   81 QIEEETQKFaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 390 IMKIL--LDV---HPD---------------RQTVMISATWPDTVRRLARSYLKDPMIVY 429
Cdd:cd17945  161 VTKILdaMPVsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
231-598 3.58e-65

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 222.74  E-value: 3.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIH---VDSQPLSrEQRNgPGMLVLTPTRE 307
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctIRSGHPS-EQRN-PLAMVLTPTRE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 308 LALQVEaECSKYSYKDL--KSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDME 385
Cdd:PLN00206 208 LCVQVE-DQAKVLGKGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 386 FEPQIMKILLDVhPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNlAAVNTVKQNII-VTTEEEKRALTQEFIENM 464
Cdd:PLN00206 287 FRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPN-RPNKAVKQLAIwVETKQKKQKLFDILKSKQ 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 465 SPNDKVIMFVSQKRIADDLSSDFNI-QGISVESLHGnsEESDKER--ALQDFESGNIKILITTDLVARGLDVNDVTHVYN 541
Cdd:PLN00206 365 HFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHG--EKSMKERreVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVII 442
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 542 YDFPWNIEEYVHRVGRIGRAGKTGTSVTLITQRDAKMAGELIKILERANQSVPEDLV 598
Cdd:PLN00206 443 FDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELA 499
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
226-576 6.92e-64

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 220.98  E-value: 6.92e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 226 AFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQP-LSREQRNGPGMLVLTP 304
Cdd:PRK04537  13 SFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaLADRKPEDPRALILAP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 305 TRELALQVEAECSKY-SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLND-LQMNNSVNLRSITYLVMDEADKML 382
Cdd:PRK04537  93 TRELAIQIHKDAVKFgADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADRMF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 383 DMEFEPQImKILLDVHPDR---QTVMISATWPDTVRRLARSYLKDPMIVYVGNLNLAAVNtVKQNIIVTTEEEKRALTQE 459
Cdd:PRK04537 173 DLGFIKDI-RFLLRRMPERgtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPADEEKQTLLLG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 460 FIENmSPNDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHV 539
Cdd:PRK04537 251 LLSR-SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 967504803 540 YNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLITQRDA 576
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYA 366
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
233-428 5.19e-62

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: 204.19  E-value: 5.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPlSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQR-ELEKGEGPIAVIVAPTRELAQQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIM 391
Cdd:cd17952   80 YLEAKKFGkAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 392 KILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
233-595 6.88e-60

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 211.25  E-value: 6.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQplsreqRNGPGMLVLTPTRELALQV 312
Cdd:PRK11634  17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE------LKAPQILVLAPTRELAVQV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYS--YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQI 390
Cdd:PRK11634  91 AEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 391 MKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGnlnlAAVNT---VKQNIIVTTEEEKRALTQEFIEnMSPN 467
Cdd:PRK11634 171 ETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQ----SSVTTrpdISQSYWTVWGMRKNEALVRFLE-AEDF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 468 DKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWN 547
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 967504803 548 IEEYVHRVGRIGRAGKTGTSVTLITQRDAKmageLIKILERANQ-SVPE 595
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERR----LLRNIERTMKlTIPE 370
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
216-433 5.34e-59

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: 198.65  E-value: 5.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 216 IPKPTCRFKDAfQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMP---GFIHVDSQPLSRE 292
Cdd:cd18052   38 PPPAILTFEEA-NLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMKEGLTASSFS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 293 QRNGPGMLVLTPTRELALQVEAECSKYSYKD-LKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSIT 371
Cdd:cd18052  117 EVQEPQALIVAPTRELANQIFLEARKFSYGTcIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLK 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 372 YLVMDEADKMLDMEFEPQIMKILLDVH-P---DRQTVMISATWPDTVRRLARSYLK-DPMIVYVGNL 433
Cdd:cd18052  197 YLILDEADRMLDMGFGPEIRKLVSEPGmPskeDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTVGRV 263
PTZ00424 PTZ00424
helicase 45; Provisional
225-575 6.63e-55

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 191.96  E-value: 6.63e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 225 DAFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREqrngpgMLVLTP 304
Cdd:PTZ00424  31 DALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQ------ALILAP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 305 TRELALQVE-AECSKYSYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLD 383
Cdd:PTZ00424 105 TRELAQQIQkVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 384 MEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNLAAVNTVKQNIIVTTEEEKRALTQEFIEN 463
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 464 MSPNdKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYD 543
Cdd:PTZ00424 265 LTIT-QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
                        330       340       350
                 ....*....|....*....|....*....|..
gi 967504803 544 FPWNIEEYVHRVGRIGRAGKTGTSVTLITQRD 575
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
231-425 9.74e-53

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: 179.82  E-value: 9.74e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHV--DSQPLSreqrngpgMLVLTPTREL 308
Cdd:cd17954    9 EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALleNPQRFF--------ALVLAPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 309 ALQVEAECSKY-SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLND-LQMNNSVNLRSITYLVMDEADKMLDMEF 386
Cdd:cd17954   81 AQQISEQFEALgSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMDF 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 967504803 387 EPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:cd17954  161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
231-428 1.47e-52

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: 179.42  E-value: 1.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSqplsREQRNGPGMLVLTPTRELAL 310
Cdd:cd17959   10 PPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA----HSPTVGARALILSPTRELAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 Q---VEAECSKYSykDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFE 387
Cdd:cd17959   86 QtlkVTKELGKFT--DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 967504803 388 PQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17959  164 EQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
246-417 2.00e-52

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: 177.43  E-value: 2.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803  246 TPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDsqplsrEQRNGPGMLVLTPTRELALQVEAECSKY-SYKDL 324
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD------KLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803  325 KSICICGGRNRIGQIEDIsKDVDIIIATPGRLNDLqMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVHPDRQTV 404
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 967504803  405 MISATWPDTVRRL 417
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
231-423 9.42e-51

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: 174.69  E-value: 9.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQ-GIDLIEVAQTGTGKTLSYLMPGFIHVDSQPlSREQRNGPGMLVLTPTRELA 309
Cdd:cd17964    3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTK-PAGRRSGVSALIISPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 310 LQVEAECSK--YSYKDLKSICICGGRNRIGQIEDISKD-VDIIIATPGRLNDLQMNNSV--NLRSITYLVMDEADKMLDM 384
Cdd:cd17964   82 LQIAAEAKKllQGLRKLRVQSAVGGTSRRAELNRLRRGrPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDM 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 967504803 385 EFEPQIMKILLDVHP----DRQTVMISATWPDTVRRLARSYLK 423
Cdd:cd17964  162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
216-431 1.27e-49

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: 172.92  E-value: 1.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 216 IPKPTCRFKDAfqQYPDLLKS-ITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQ----PLS 290
Cdd:cd18051   16 CPPHIETFSDL--DLGEIIRNnIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeSLP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 291 REQRNG------PGMLVLTPTRELALQVEAECSKYSYKDLKSICIC-GGRNRIGQIEDISKDVDIIIATPGRLNDLQMNN 363
Cdd:cd18051   94 SESGYYgrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVyGGADIGQQMRDLERGCHLLVATPGRLVDMLERG 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967504803 364 SVNLRSITYLVMDEADKMLDMEFEPQIMKILL-DVHP---DRQTVMISATWPDTVRRLARSYLKDPMIVYVG 431
Cdd:cd18051  174 KIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
238-428 6.91e-49

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: 169.69  E-value: 6.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 238 TRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGF--IHVDSQPLSREQrnGPGMLVLTPTRELALQVEAE 315
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIqrLLSLEPRVDRSD--GTLALVLVPTRELALQIYEV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 316 CSKY--SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLND-LQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMK 392
Cdd:cd17949   85 LEKLlkPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 967504803 393 IL--LDVHPD-----------RQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17949  165 ILelLDDKRSkaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
233-431 1.30e-48

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: 168.54  E-value: 1.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVdsqpLSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL----GKPRKKKGLRALILAPTRELASQI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKYSYKDLKSICIC--GGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQI 390
Cdd:cd17957   77 YRELLKLSKGTGLRIVLLskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 967504803 391 MKILLD-VHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVG 431
Cdd:cd17957  157 DEILAAcTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
441-571 2.57e-48

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: 164.99  E-value: 2.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 441 VKQNIIVTTEEEKRALTQEFIENMSPNDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKI 520
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 967504803 521 LITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLI 571
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
233-425 5.12e-48

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: 166.66  E-value: 5.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQRNGPG--MLVLTPTRELAL 310
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL-----ERLLYRPKKKAAtrVLVLVPTRELAM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNN-SVNLRSITYLVMDEADKMLDMEFEP 388
Cdd:cd17947   76 QCFSVLQQLAqFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFAD 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 389 QIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:cd17947  156 ELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
227-425 1.61e-47

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: 165.55  E-value: 1.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 227 FQQY---PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREqrngpgMLVLT 303
Cdd:cd17940    1 FEDYglkRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ------ALILV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 304 PTRELALQVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKML 382
Cdd:cd17940   75 PTRELALQTSQVCKELGkHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 967504803 383 DMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:cd17940  155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEXDc smart00487
DEAD-like helicases superfamily;
237-435 3.50e-47

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 164.59  E-value: 3.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803   237 ITRVGFVKPTPIQSQAWPIILQGI-DLIEVAQTGTGKTLSYLMPGFIHVDSQPlsreqrnGPGMLVLTPTRELALQVEAE 315
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGK-------GGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803   316 CSKY-SYKDLKSICICGGRNRIGQIEDI-SKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKI 393
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 967504803   394 LLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYVGNLNL 435
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
233-428 2.09e-45

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: 160.20  E-value: 2.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQP--LSREQRNGPGMLVLTPTRELAL 310
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkkLPFIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYS-------YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLD 383
Cdd:cd17951   81 QTHEVIEYYCkalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 967504803 384 MEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
234-430 2.74e-44

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: 156.68  E-value: 2.74e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 234 LKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQ---RNGPGMLVLTPTRELAL 310
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLL-----EKLYRERwtpEDGLGALIISPTRELAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QV-EAECSKYSYKDLKSICICGGRN------RIGQIediskdvDIIIATPGRLndLQ-MNNSVNLRS--ITYLVMDEADK 380
Cdd:cd17941   77 QIfEVLRKVGKYHSFSAGLIIGGKDvkeekeRINRM-------NILVCTPGRL--LQhMDETPGFDTsnLQMLVLDEADR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 967504803 381 MLDMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYV 430
Cdd:cd17941  148 ILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
233-425 9.13e-43

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: 152.73  E-value: 9.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVdSQPLSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIL-LKRKANLKKGQVGALIISPTRELATQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECS---KYSYKDLKSICICGGRNRIGQIEDISKD-VDIIIATPGRLNDL--QMNNSVNLRSITYLVMDEADKMLDMEF 386
Cdd:cd17960   80 YEVLQsflEHHLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGF 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 967504803 387 EPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:cd17960  160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
234-431 5.09e-42

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: 150.59  E-value: 5.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 234 LKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPG--FIHvdsqPLSREQRNGPGMLVLTPTRELALQ 311
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLY----KLKFKPRNGTGVIIISPTRELALQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 312 ---VEAECSKYSYKDLKsiCICGGRNRIGQIEDISKDVDIIIATPGRLND-LQMNNSVNLRSITYLVMDEADKMLDMEFE 387
Cdd:cd17942   78 iygVAKELLKYHSQTFG--IVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 967504803 388 PQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIvYVG 431
Cdd:cd17942  156 EEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPL-YVG 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
233-426 9.69e-42

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: 150.07  E-value: 9.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFihvdsQPLSREQrNGPGMLVLTPTRELALQV 312
Cdd:cd17955   10 LVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDP-YGIFALVLTPTRELAYQI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 eAECSKYSYK--DLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSV---NLRSITYLVMDEADKMLDMEFE 387
Cdd:cd17955   84 -AEQFRALGAplGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADRLLTGSFE 162
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 967504803 388 PQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPM 426
Cdd:cd17955  163 DDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
233-428 2.88e-41

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: 148.47  E-value: 2.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHvdsqplSREQRNGPGMLVLTPTRELALQV 312
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR------CLTEHRNPSALILTPTRELAVQI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 EAECSKY--SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQI 390
Cdd:cd17962   75 EDQAKELmkGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQV 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 967504803 391 MKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17962  155 LDILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
232-428 1.54e-37

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 138.23  E-value: 1.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 232 DLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQplsreqRNGPGMLVLTPTRELALQ 311
Cdd:cd17939    7 DLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTT------VRETQALVLAPTRELAQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 312 VEAECSKY-SYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQI 390
Cdd:cd17939   81 IQKVVKALgDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 967504803 391 MKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17939  161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
233-409 2.82e-37

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: 138.53  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWP-IILQGIDLIEVAQTGTGKTLSYLMP---GFI-HVDSQPLSREQRnGPGMLVLTPTRE 307
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPileRLLsQKSSNGVGGKQK-PLRALILTPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 308 LALQV----EAECskySYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDL-QMNNS--VNLRSITYLVMDEADK 380
Cdd:cd17946   80 LAVQVkdhlKAIA---KYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiQEGNEhlANLKSLRFLVLDEADR 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 967504803 381 MLD----MEFEpQIMKILLDVHP----DRQTVMISAT 409
Cdd:cd17946  157 MLEkghfAELE-KILELLNKDRAgkkrKRQTFVFSAT 192
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
247-423 5.60e-36

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: 134.20  E-value: 5.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 247 PIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGF--IHVDSQPLSREQrnGPGMLVLTPTRELALQVEAECSKYSYKdL 324
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPRKRGR--APKVLVLAPTRELANQVTKDFKDITRK-L 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 325 KSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKIL-----LDVHP 399
Cdd:cd17944   92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSED 171
                        170       180
                 ....*....|....*....|....
gi 967504803 400 DRQTVMISATWPDTVRRLARSYLK 423
Cdd:cd17944  172 NPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
233-428 9.56e-36

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: 133.16  E-value: 9.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYlmpGFIHVDSqpLSREQRnGPGMLVLTPTRELALQV 312
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVF---VVIALES--LDLERR-HPQVLILAPTREIAVQI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 313 eAECSKYSYKDLKSICIC---GGRnrigqieDISKDVD------IIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLD 383
Cdd:cd17943   75 -HDVFKKIGKKLEGLKCEvfiGGT-------PVKEDKKklkgchIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 967504803 384 MEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17943  147 GSFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
231-428 1.31e-35

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: 133.09  E-value: 1.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNGPGMLVLTPTRELAL 310
Cdd:cd17961    3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVeaecskysYKDLKSICI-CGGRNRIGQIEDISKDV----------DIIIATPGRLND-LQMNNSVNLRSITYLVMDEA 378
Cdd:cd17961   83 QV--------SKVLEQLTAyCRKDVRVVNLSASSSDSvqrallaekpDIVVSTPARLLShLESGSLLLLSTLKYLVIDEA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 967504803 379 DKMLDMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17961  155 DLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
231-428 1.82e-35

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: 132.31  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGID--LIEVAQTGTGKTLSYLMPGFIHVDsqplsrEQRNGPGMLVLTPTREL 308
Cdd:cd17963    3 PELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRVD------PTLKSPQALCLAPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 309 ALQVEAECSKY-SYKDLKSICICGGRNRigqieDISKDVD--IIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDME 385
Cdd:cd17963   77 ARQIGEVVEKMgKFTGVKVALAVPGNDV-----PRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQ 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 967504803 386 -FEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd17963  152 gHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
223-430 3.75e-35

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: 131.70  E-value: 3.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 223 FKDaFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKT----LSYL-----MPGFIHVdsqplsreq 293
Cdd:cd17950    4 FRD-FLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTavfvLSTLqqlepVDGQVSV--------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 294 rngpgmLVLTPTRELALQVEAE---CSKYsYKDLKSICICGGRNRIGQIEDISKDV-DIIIATPGRLNDLQMNNSVNLRS 369
Cdd:cd17950   74 ------LVICHTRELAFQISNEyerFSKY-MPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSH 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967504803 370 ITYLVMDEADKML-DMEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIVYV 430
Cdd:cd17950  147 VKHFVLDECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
233-417 4.25e-35

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: 132.49  E-value: 4.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQR-NGPGMLVLTPTRELALQ 311
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfNAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 312 VEAECSKYS-YKDLKSICICGGRNRiGQIEDIS-KDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ 389
Cdd:cd17948   81 IGSVAQSLTeGLGLKVKVITGGRTK-RQIRNPHfEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 967504803 390 IMKILLDVH-------------PDRQTVMISATWPDTVRRL 417
Cdd:cd17948  160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
231-428 8.05e-30

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 116.65  E-value: 8.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSqplsreqrngpgmLVLTPTRELAL 310
Cdd:cd17938    8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA-------------LILEPSRELAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 311 QVEAECSKYSY----KDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEF 386
Cdd:cd17938   75 QTYNCIENFKKyldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGN 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 967504803 387 EPQIMKIL--LDVHPDR----QTVMISATW-PDTVRRLARSYLKDPMIV 428
Cdd:cd17938  155 LETINRIYnrIPKITSDgkrlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
225-425 1.63e-29

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: 115.62  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 225 DAFQQYPDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQplsreqRNGPGMLVLTP 304
Cdd:cd18046    2 DDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS------LKATQALVLAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 305 TRELALQVEAECSKYS-YKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLD 383
Cdd:cd18046   76 TRELAQQIQKVVMALGdYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 967504803 384 MEFEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDP 425
Cdd:cd18046  156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
232-428 3.85e-29

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: 114.87  E-value: 3.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 232 DLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDsqPLSREqrngPGMLVLTPTRELALQ 311
Cdd:cd18045    9 DLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD--IQVRE----TQALILSPTRELAVQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 312 VEAECSKYSYKDLKSICICGGRNRIGqiEDISK---DVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEP 388
Cdd:cd18045   83 IQKVLLALGDYMNVQCHACIGGTSVG--DDIRKldyGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 967504803 389 QIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd18045  161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
452-562 2.37e-27

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: 106.53  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803  452 EKRALTQEFIENmSPNDKVIMFV-SQKRIADDLSsdFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARG 530
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSqTKKTLEAELL--LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 967504803  531 LDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAG 562
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
233-416 4.66e-27

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: 109.64  E-value: 4.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 233 LLKSITRVGFVKPTPIQSQAWPIILQGI---------DLIEVAQTGTGKTLSYLMPgfIhvdSQPLSreQRNGPGM--LV 301
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLP--I---VQALS--KRVVPRLraLI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 302 LTPTRELALQVEAECSKYSYK-DLKSICICGGRNRIGQIEDISKD--------VDIIIATPGRLND-LQMNNSVNLRSIT 371
Cdd:cd17956   74 VVPTKELVQQVYKVFESLCKGtGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLR 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 967504803 372 YLVMDEADKMLDMEFE---PQIMKILLDVHPDRQTVMISATWPDTVRR 416
Cdd:cd17956  154 FLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDANLLERSVR 201
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
50-115 2.42e-26

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. 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.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 101.98  E-value: 2.42e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  50 PLCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEALVRIFGNREMKAKAKAIIETLTRK 115
Cdd:cd22430    1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
HELICc smart00490
helicase superfamily c-terminal domain;
481-562 3.41e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 99.21  E-value: 3.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803   481 DDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGR 560
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 967504803   561 AG 562
Cdd:smart00490  81 AG 82
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
232-428 2.50e-21

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


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 93.16  E-value: 2.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 232 DLLKSITRVGFVKPTPIQSQAWPIILQG--IDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSreqrngPGMLVLTPTRELA 309
Cdd:cd18048   28 ELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY------PQCLCLSPTFELA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 310 LQ---VEAECSKYSyKDLKSICICGGrNRIGQIEDISKdvDIIIATPGRLND----LQMnnsVNLRSITYLVMDEADKML 382
Cdd:cd18048  102 LQtgkVVEEMGKFC-VGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDwcfkLRL---IDVTNISVFVLDEADVMI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 967504803 383 DME-FEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd18048  175 NVQgHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
243-411 7.31e-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: 7.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 243 VKPTPIQSQAWPIILQG-----------------IDLIeVAQTGTGKTLSYLMP--GFI--------HVDSQPLSREQRN 295
Cdd:cd17965   29 IKPSPIQTLAIKKLLKTlmrkvtkqtsneepkleVFLL-AAETGSGKTLAYLAPllDYLkrqeqepfEEAEEEYESAKDT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 296 G-PGMLVLTPTRELALQVEA---ECSKYSYKDLKSICICGGRNRIGQIEDISKDVDIIIATPGRLNDLQMNNSVNLRSIT 371
Cdd:cd17965  108 GrPRSVILVPTHELVEQVYSvlkKLSHTVKLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVT 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 967504803 372 YLVMDEADKMLDMEFEPQIMKILLDVHPDRQTVMISATWP 411
Cdd:cd17965  188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
265-409 8.45e-17

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: 77.44  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 265 VAQTGTGKTLSYLMPGFIHVDSQplsreqrnGPGMLVLTPTRELALQVEAECSKYSYKDLKSICICGGRNRIGQIEDISK 344
Cdd:cd00046    7 TAPTGSGKTLAALLAALLLLLKK--------GKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEEREKNKLG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967504803 345 DVDIIIATPGRL-NDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLDVH--PDRQTVMISAT 409
Cdd:cd00046   79 DADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAglKNAQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
231-428 2.16e-16

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 78.22  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQG--IDLIEVAQTGTGKTLSYLMPGFIHVDsqPLSREQRngpgMLVLTPTREL 308
Cdd:cd18047   10 PQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANKYPQ----CLCLSPTYEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 309 ALQ---VEAECSKYSYKDLKSICICGGRNRIG-QIEDiskdvDIIIATPGRLNDLQMN-NSVNLRSITYLVMDEADKMLD 383
Cdd:cd18047   84 ALQtgkVIEQMGKFYPELKLAYAVRGNKLERGqKISE-----QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 967504803 384 ME-FEPQIMKILLDVHPDRQTVMISATWPDTVRRLARSYLKDPMIV 428
Cdd:cd18047  159 TQgHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
265-571 2.51e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 82.38  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 265 VAQTGTGKTlsYLMPGFIhvdsqplsREQRNGPGMLVLTPTRELALQVEAECSKYSYKDLKSicicGGRNRIgqiedisk 344
Cdd:COG1061  106 VAPTGTGKT--VLALALA--------AELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG----GGKKDS-------- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 345 DVDIIIATpgrLNDLQMNNSVNL--RSITYLVMDEA--------DKMLDMeFEPQimKIL--------LDVHPDRQTVMI 406
Cdd:COG1061  164 DAPITVAT---YQSLARRAHLDElgDRFGLVIIDEAhhagapsyRRILEA-FPAA--YRLgltatpfrSDGREILLFLFD 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 407 SATWPDTVRRLARS-YLKDPMIV-YVGNLN-----LAAVNTVKQNIIVTTEEEKRALTQEFIENMSPNDKVIMFVSQKRI 479
Cdd:COG1061  238 GIVYEYSLKEAIEDgYLAPPEYYgIRVDLTderaeYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVDH 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 480 ADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVNDVTHVY---NYDFPWnieEYVHRVG 556
Cdd:COG1061  318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIllrPTGSPR---EFIQRLG 394
                        330
                 ....*....|....*
gi 967504803 557 RIGRAGKTGTSVTLI 571
Cdd:COG1061  395 RGLRPAPGKEDALVY 409
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
256-608 9.59e-12

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 67.47  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 256 ILQGIDLIEVAQTGTGKTLSYLMPGFIhvdsqplsreqRNGPGmLVLTPTreLAL---QVEAecskysykdLKSI----- 327
Cdd:COG0514   29 VLAGRDALVVMPTGGGKSLCYQLPALL-----------LPGLT-LVVSPL--IALmkdQVDA---------LRAAgiraa 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 328 CICGGRNR--IGQIED--ISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEA--------DkmldmeFEPQIMKI-- 393
Cdd:COG0514   86 FLNSSLSAeeRREVLRalRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD------FRPDYRRLge 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 394 LLDVHPDRQTVMISATWPDTVRR--LARSYLKDPMiVYVG-----NLNLAavntvkqnIIVTTEEEKRALTQEFIENMSP 466
Cdd:COG0514  160 LRERLPNVPVLALTATATPRVRAdiAEQLGLEDPR-VFVGsfdrpNLRLE--------VVPKPPDDKLAQLLDFLKEHPG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 467 NDKVIMFVSQKRiADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTdlVARGLDVN--DVTHVYNYDF 544
Cdd:COG0514  231 GSGIVYCLSRKK-VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGMGIDkpDVRFVIHYDL 307
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967504803 545 PWNIEEYVHRVGRIGRAGKTGTSVTLITQRDakmagelIKILER-ANQSVPEDLVVIAEQYKLNQ 608
Cdd:COG0514  308 PKSIEAYYQEIGRAGRDGLPAEALLLYGPED-------VAIQRFfIEQSPPDEERKRVERAKLDA 365
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
53-110 9.14e-11

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 57.68  E-value: 9.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967504803   53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEA---LVRIFGNREMKAKAKAIIE 110
Cdd:pfam00013   4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGnerIVTITGTPEAVEAAKALIE 64
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
247-607 5.05e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 62.42  E-value: 5.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 247 PIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIhvdsqplsreqRNGPgMLVLTPTREL---------ALQVEAEC- 316
Cdd:PRK11057  28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV-----------LDGL-TLVVSPLISLmkdqvdqllANGVAAACl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 317 -SKYSYKDLKSICicgGRNRIGQIEdiskdvdIIIATPGRL-NDLQMNNSVNLRsITYLVMDEAD--KMLDMEFEPQIMK 392
Cdd:PRK11057  96 nSTQTREQQLEVM---AGCRTGQIK-------LLYIAPERLmMDNFLEHLAHWN-PALLAVDEAHciSQWGHDFRPEYAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 393 I--LLDVHPDRQTVMISATWPDTVRR--LARSYLKDPMIvYVGNLNlaavntvKQNIIVTTEEEKRALTQ--EFIENMSP 466
Cdd:PRK11057 165 LgqLRQRFPTLPFMALTATADDTTRQdiVRLLGLNDPLI-QISSFD-------RPNIRYTLVEKFKPLDQlmRYVQEQRG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 467 NDKVIMFVSQKRIaDDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTdlVARGLDVN--DVTHVYNYDF 544
Cdd:PRK11057 237 KSGIIYCNSRAKV-EDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVAT--VAFGMGINkpNVRFVVHFDI 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967504803 545 PWNIEEYVHRVGRIGRAGKTGTSVTLITQRDakMAGeLIKILERANQSVPEDLvviaEQYKLN 607
Cdd:PRK11057 314 PRNIESYYQETGRAGRDGLPAEAMLFYDPAD--MAW-LRRCLEEKPAGQQQDI----ERHKLN 369
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
231-597 1.84e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 60.29  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWP-IILQGIDLIEVAQTGTGKTLSYLMpgFIHvdsqplsREQRNGPGMLVLTPTRELA 309
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAEL--AIL-------KALLNGGKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 310 LQVEAECSKySYKDLK-SICICGGRNRIGqiEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEP 388
Cdd:COG1204   80 SEKYREFKR-DFEELGiKVGVSTGDYDSD--DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 389 QI-MKI--LLDVHPDRQTVMISAT-------------------WPDTVRRLArsylkdpmIVYVGNLNLAAVNTVKQNII 446
Cdd:COG1204  157 TLeVLLarLRRLNPEAQIVALSATignaeeiaewldaelvksdWRPVPLNEG--------VLYDGVLRFDDGSRRSKDPT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 447 VtteeekrALTQEFIENmspNDKVIMFVSQKR----IADDLSSDFNIQGISVES---------LHGNSEESDKERALQD- 512
Cdd:COG1204  229 L-------ALALDLLEE---GGQVLVFVSSRRdaesLAKKLADELKRRLTPEEReeleelaeeLLEVSEETHTNEKLADc 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 513 -----------------------FESGNIKILITTD-------LVARGLDVNDVTHVYNYDFP----WNIeeyvhrVGRI 558
Cdd:COG1204  299 lekgvafhhaglpselrrlvedaFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIPvlefKQM------AGRA 372
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 967504803 559 GRAGK--TGTSVtlITQRDAKMAGELIKILERANqsvPEDL 597
Cdd:COG1204  373 GRPGYdpYGEAI--LVAKSSDEADELFERYILGE---PEPI 408
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
53-110 3.59e-09

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 53.07  E-value: 3.59e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK---GESEALVRIFGNREMKAKAKAIIE 110
Cdd:cd00105    3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKegeGSGERVVTITGTPEAVEKAKELIE 63
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
53-115 7.66e-09

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 52.48  E-value: 7.66e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIikgESEALVRIFG-NREMKAKAKAIIETLTRK 115
Cdd:cd02393    8 IKIPPDKIGDVIGPGGKTIRAIIEETGAKIDI---EDDGTVTIFAtDKESAEAAKAMIEDIVAE 68
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
518-572 1.02e-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: 52.32  E-value: 1.02e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967504803 518 IKILITTDLVARGLDVNDVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTLIT 572
Cdd:cd18785   23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
454-559 1.71e-08

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 53.25  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 454 RALTQEFIENMSPNDKVIMFvSQ-KRIADDLSSDFNIQGISVESLHGNSEESDKERALQDF-ESGNIKI-LITTDLVARG 530
Cdd:cd18793   14 EALLELLEELREPGEKVLIF-SQfTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGGVG 92
                         90       100       110
                 ....*....|....*....|....*....|..
gi 967504803 531 LDVNDVTHVYNYDFPWN--IEEY-VHRVGRIG 559
Cdd:cd18793   93 LNLTAANRVILYDPWWNpaVEEQaIDRAHRIG 124
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
451-570 2.70e-08

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 52.98  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 451 EEKRALTQEFIENMSPNDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESGNIKILITTdlVARG 530
Cdd:cd18794   14 KDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT--VAFG 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 967504803 531 LDVN--DVTHVYNYDFPWNIEEYVHRVGRIGRAGKTGTSVTL 570
Cdd:cd18794   92 MGIDkpDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
53-111 1.69e-07

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 48.40  E-value: 1.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK---GESEALVRIFGNREMKAKAKAIIET 111
Cdd:cd22396    5 YKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPdsgGLPERPCTLTGTPDAIETAKRLIDQ 66
KH smart00322
K homology RNA-binding domain;
53-110 2.25e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803    53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQII-KGESEALVRIFGNREMKAKAKAIIE 110
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPgPGSEERVVEITGPPENVEKAAELIL 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
59-113 5.64e-07

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 47.18  E-value: 5.64e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  59 MVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEA-LVRIFGNREMKAKAKAIIETLT 113
Cdd:cd02394   12 FHGHIIGKGGANIKRIREESGVSIRIPDDEANSdEIRIEGSPEGVKKAKAEILELV 67
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
51-115 6.01e-07

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 52.74  E-value: 6.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  51 LCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIikgESEALVRIFG-NREMKAKAKAIIETLTRK 115
Cdd:PRK11824 556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDI---EDDGTVKIAAtDGEAAEAAKERIEGITAE 618
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
471-561 3.88e-06

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: 46.82  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 471 IMFVSQKRIADDLS----------SDFNIQ-----GISVESLHGNSEESDKERALQDFESGNIKILITTDLVARGLDVND 535
Cdd:cd18802   29 IIFVERRATAVVLSrllkehpstlAFIRCGfligrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                         90       100
                 ....*....|....*....|....*.
gi 967504803 536 VTHVYNYDFPWNIEEYVHRVGRiGRA 561
Cdd:cd18802  109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
246-419 3.98e-06

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: 47.64  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 246 TPIQSQAW-PIILQGIDLIEVAQTGTGKTL-SYLMpgfIhvdsqpLSREQRNGPGMLVLTPTRELALQVEAECSKYSYKD 323
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLiAELA---I------LRALATSGGKAVYIAPTRALVNQKEADLRERFGPL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 324 LKSICICGGRNRIGQIEDISKdvDIIIATPGRLnDLQMNN--SVNLRSITYLVMDEADKMLDMEFEP---QIMKILLDVH 398
Cdd:cd17921   74 GKNVGLLTGDPSVNKLLLAEA--DILVATPEKL-DLLLRNggERLIQDVRLVVVDEAHLIGDGERGVvleLLLSRLLRIN 150
                        170       180
                 ....*....|....*....|.
gi 967504803 399 PDRQTVMISATWPDTvRRLAR 419
Cdd:cd17921  151 KNARFVGLSATLPNA-EDLAE 170
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
453-561 4.73e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 49.84  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 453 KRALTQEFIEN-MSPNDKVIMFVSQKRIADDLSSDFNIQGISVESLHGNSEESDKERALQDFESG-NIK-ILITTDLVAR 529
Cdd:COG0553  534 KLEALLELLEElLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPvFLISLKAGGE 613
                         90       100       110
                 ....*....|....*....|....*....|....
gi 967504803 530 GLDVNDVTHVYNYDFPWN--IEEYvhrvgRIGRA 561
Cdd:COG0553  614 GLNLTAADHVIHYDLWWNpaVEEQ-----AIDRA 642
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
256-409 7.66e-06

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: 46.56  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 256 ILQGIDLIEVAQTGTGKTLSYLMPGFIHVDsqplsreqrNGPGMLVLTPTRELALQVEAECSKYSYKDLKsICICGGRNR 335
Cdd:cd18028   14 LLKGENLLISIPTASGKTLIAEMAMVNTLL---------EGGKALYLVPLRALASEKYEEFKKLEEIGLK-VGISTGDYD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 336 IGqiEDISKDVDIIIATPGRLNDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQ---IMKILLDVHPDRQTVMISAT 409
Cdd:cd18028   84 ED--DEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTlesIVARLRRLNPNTQIIGLSAT 158
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
63-117 1.54e-05

second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the second one.


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 43.45  E-value: 1.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  63 VIGHSGSKIKDLQHSTNTKIQIIKGESEA-LVRIFGNREMKAKAKAIIETLTRKQK 117
Cdd:cd22406   19 ILGKKGKKLQELELKTATKIVIPRQEDNSdEIKITGTKEGIEKARHEIQLISDEQA 74
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
242-309 2.52e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 47.40  E-value: 2.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803 242 FVKPTPIQSQAWPIILQGID-LIeVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNGPGMLVLTPTRELA 309
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLYISPLKALA 89
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
55-110 7.48e-05

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4.


Pssm-ID: 411890 [Multi-domain]  Cd Length: 66  Bit Score: 41.08  E-value: 7.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803  55 IKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGES---EALVRIFGNREMKAKAKAIIE 110
Cdd:cd22462    5 IPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSatgERIVLISGTPDQARHAQNLIE 63
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
60-111 8.60e-05

second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding proteins; The MEX-3 protein family includes four members, MEX3A/RKHD4, MEX3B/RKHD3/RNF195, MEX3C/ RKHD2/RNF194, and MEX3D/RKHD1/RNF193/TINO. They are homologous of Caenorhabditis elegans MEX-3 protein, a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. Mex-3 proteins are RNA-binding phosphoproteins involved in post-transcriptional regulatory mechanisms. They are characterized by containing two K-homology (KH) RNA-binding domains and a C-terminal RING finger. They bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The model corresponds to the second KH domain.


Pssm-ID: 411852 [Multi-domain]  Cd Length: 72  Bit Score: 41.17  E-value: 8.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 967504803  60 VGAVIGHSGSKIKDLQHSTNTKIQIIKGESEALVRIFGNREMKAKAKAIIET 111
Cdd:cd22424   15 VGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVERAREEIEA 66
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
50-112 1.04e-04

first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the first one.


Pssm-ID: 411828 [Multi-domain]  Cd Length: 68  Bit Score: 40.72  E-value: 1.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967504803  50 PLCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK----GESEALVRIFGNREMKAKA-KAIIETL 112
Cdd:cd22400    1 PLRILVPSEFVGAIIGKGGATIRQITQQTGARIDIHRkenaGAAEKAITIYGTPEGCSSAcKQILEIM 68
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
55-105 1.26e-04

third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the third one.


Pssm-ID: 411830 [Multi-domain]  Cd Length: 66  Bit Score: 40.31  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967504803  55 IKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGES----EALVRIFGNREMKAKA 105
Cdd:cd22402    7 IPNKAVGAIIGTKGSHIRYIKRFSGASIKIAPADSpdapERKVTITGPPEAQWKA 61
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
265-378 1.79e-04

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 42.89  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 265 VAQTGTGKTLSYLMPGfihvdsqpLSREQRNGPGMLVLTPTRELALQVEAECSKYSYKDLKSICICGgRNRIGQIEDISK 344
Cdd:cd18035   22 VLPTGLGKTIIAILVA--------ADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTG-EVKPEERAERWD 92
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 967504803 345 DVDIIIATPGRL-NDLqMNNSVNLRSITYLVMDEA 378
Cdd:cd18035   93 ASKIIVATPQVIeNDL-LAGRITLDDVSLLIFDEA 126
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
53-113 1.88e-04

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 39.99  E-value: 1.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK---GESEALVRIFGNREMKAKAKAIIETLT 113
Cdd:cd22454    8 VVIPNADVGKVIGKGGETIKRIEALTDTVITFERvngGSPNREVQITGSPDNVAAAKRLIEDTI 71
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
243-396 2.25e-04

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 42.80  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 243 VKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRngpgMLVLTPTRELALQVEAECSKYSYK 322
Cdd:cd17927    1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK----VVFLANKVPLVEQQKEVFRKHFER 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803 323 D-LKSICICGGRNRIGQIEDISKDVDIIIATPGRL-NDLQMNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLD 396
Cdd:cd17927   77 PgYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRYLD 152
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
469-539 3.27e-04

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 40.62  E-value: 3.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803 469 KVIMFVSQKRIADDLSSDFNIQGISVESLHgnSEESDKER---ALQDFESGNIK--ILITTDLVARGLDVNDVTHV 539
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALN--SDYSDRERgdeALILLFFGELKppILVTVDLLTTGVDIPEVDNV 81
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
263-378 5.04e-04

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: 41.87  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 263 IEVAQTGTGKTLSYLMpgFIHVDSQPLSREQRNGPGMLVLTPTRELALQvEAECSKySYKDLKSICICGGRNRIGQIEDI 342
Cdd:cd18034   20 IVVLPTGSGKTLIAVM--LIKEMGELNRKEKNPKKRAVFLVPTVPLVAQ-QAEAIR-SHTDLKVGEYSGEMGVDKWTKER 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 967504803 343 SKDV----DIIIATPGRLNDLQMNNSVNLRSITYLVMDEA 378
Cdd:cd18034   96 WKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
58-110 5.32e-04

third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 38.71  E-value: 5.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803  58 NMVGAVIGHSGSKIKDLQHSTNTKIQIIK------GESEALVRIFGNREMKAKAKAIIE 110
Cdd:cd09031   10 NLVGAILGKGGKTLVEIQELTGARIQISKkgefvpGTRNRKVTITGTPAAVQAAQYLIE 68
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
244-352 5.76e-04

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: 41.25  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 244 KPTPIQSQAWPIILQGI------DLIEVAQTGTGKTLSYLMPGFIHVDsqplsreqrNGPGMLVLTPTRELALQVEAECS 317
Cdd:cd17918   15 SLTKDQAQAIKDIEKDLhspepmDRLLSGDVGSGKTLVALGAALLAYK---------NGKQVAILVPTEILAHQHYEEAR 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 967504803 318 KYsYKDLKSICICGGRNrigqiEDISKDVDIIIAT 352
Cdd:cd17918   86 KF-LPFINVELVTGGTK-----AQILSGISLLVGT 114
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
249-378 5.90e-04

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: 41.03  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 249 QSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREqrngpgmLVLTPTRELALQVEAECSKYSYKDLKSIC 328
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA-------LYLYPTKALAQDQLRSLRELLEQLGLGIR 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 329 I--CGGRNRIGQIEDISKD-VDIIIATPGRLNDLQMNNSVN----LRSITYLVMDEA 378
Cdd:cd17923   78 VatYDGDTPREERRAIIRNpPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA 134
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
57-112 1.11e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 37.97  E-value: 1.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967504803  57 NNMVGAVIGHSGSKIKDLQHSTNTKIQI------IKGESEALVRIFGNREMKAKA-KAIIETL 112
Cdd:cd22437    7 NSSCGLIIGKGGSTIKELREDSNANIKIspkdqlLPGSSERIVTITGSFDQVVKAvALILEKL 69
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
53-110 1.20e-03

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 38.16  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEAL-----------VRIFGNREMKAKAKAIIE 110
Cdd:cd22446   11 ISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNydeddddetveISIEGDAEGVELAKKEIE 79
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
247-378 1.73e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 39.93  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 247 PIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHvdsqplsreQRNGPGM-LVLTPTreLAL---QVEAECSKysyk 322
Cdd:cd18018   15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLL---------RRRGPGLtLVVSPL--IALmkdQVDALPRA---- 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803 323 dLKSICICGGrNRIGQIEDI-----SKDVDIIIATPGRLNdlqmNNSV-----NLRSITYLVMDEA 378
Cdd:cd18018   80 -IKAAALNSS-LTREERRRIleklrAGEVKILYVSPERLV----NESFrellrQTPPISLLVVDEA 139
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
53-86 1.86e-03

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 37.05  E-value: 1.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK 86
Cdd:cd22457    3 ISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAK 36
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
53-115 2.54e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 36.84  E-value: 2.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIK---GESEALVRIFGNREMKAKAKAIIETLTRK 115
Cdd:cd22479    5 YRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPdsgGLPERSVSLTGSPEAVQKAKMMLDDIVSR 70
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
256-434 2.62e-03

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: 39.44  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 256 ILQGIDLIEVAQTGTGKTLSYLMPGFIhvdsqplsreqRNGPGmLVLTPTreLAL---QVEaECSKysyKDLKSICICGG 332
Cdd:cd17920   24 VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVT-LVVSPL--ISLmqdQVD-RLQQ---LGIRAAALNST 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 333 RNRIGQIEDISK----DVDIIIATPGRLNDLQMNNSVN----LRSITYLVMDEA--------DkmldmeFEPQIMKI--L 394
Cdd:cd17920   86 LSPEEKREVLLRikngQYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAhcvsqwghD------FRPDYLRLgrL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 967504803 395 LDVHPDRQTVMISATWPDTVRRLARSYLK-DPMIVYVGNLN 434
Cdd:cd17920  160 RRALPGVPILALTATATPEVREDILKRLGlRNPVIFRASFD 200
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
53-100 2.85e-03

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 36.82  E-value: 2.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQII---KGESEALVRIFGNRE 100
Cdd:cd22439    6 ITIPNDLIGCIIGKGGTKINEIRQLSGATIKIAnseDGSTERSVTITGTPE 56
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
51-112 3.36e-03

type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex subunit 1 (ASCC1) and similar proteins; ASCC1, also called ASC-1 complex subunit p50, or Trip4 complex subunit p50, plays a role in DNA damage repair as component of the ASCC complex. It is part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. ASCC1 may also play a role in the development of neuromuscular junction.


Pssm-ID: 411847 [Multi-domain]  Cd Length: 66  Bit Score: 36.40  E-value: 3.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967504803  51 LCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGESEALVRIFGN-REMKAKAKAIIETL 112
Cdd:cd22419    3 LSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKdRSGVDSARTRIEVL 65
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
231-309 4.40e-03

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: 40.20  E-value: 4.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803 231 PDLLKSITRVGFVKPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREqrngpgmLVLTPTRELA 309
Cdd:COG1205   43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------LYLYPTKALA 114
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
60-84 4.41e-03

second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 36.08  E-value: 4.41e-03
                         10        20
                 ....*....|....*....|....*
gi 967504803  60 VGAVIGHSGSKIKDLQHSTNTKIQI 84
Cdd:cd22433   13 AGCIIGRAGFKIKELREKTGATIKV 37
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
57-84 5.36e-03

second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 36.05  E-value: 5.36e-03
                         10        20
                 ....*....|....*....|....*...
gi 967504803  57 NNMVGAVIGHSGSKIKDLQHSTNTKIQI 84
Cdd:cd22401    8 NNLCGRLIGKDGRNIKKIMEDTNTKITI 35
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
244-396 6.38e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 38.61  E-value: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 244 KPTPIQSQAWPIILQGIDLIEVAQTGTGKTLSYLMPGFIHVDSQPLSREQRNgpgMLVLTPTRELALQVEAECSKYSYKD 323
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGR---VVVLVNKVPLVEQQLEKFFKYFRKG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967504803 324 LKSICICGGRNRIGQIEDISKDVDIIIATPGRL-NDLQ---MNNSVNLRSITYLVMDEADKMLDMEFEPQIMKILLD 396
Cdd:cd18036   79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILiNNLLsgrEEERVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLD 155
KH-I_IGF2BP3_rpt2 cd22495
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
50-122 6.49e-03

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3) and similar proteins; IGF2BP3, also called IGF2 mRNA-binding protein 3 (IMP-3), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 3, or VICKZ family member 3 (VICKZ3), or KH domain-containing protein overexpressed in cancer, or KOC, is primarily found in the nucleolus, where it can bind to the 5' UTR of the insulin-like growth factor II leader 3 mRNA and may repress translation of insulin-like growth factor II during late development. It acts as an RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. IGF2BP3 binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP3 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP2 in an RNA-dependent manner. IGF2BP3 contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411923  Cd Length: 77  Bit Score: 35.79  E-value: 6.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967504803  50 PLCFKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQIIKGES------EALVRIFGNREMKAKAKAiiETLTRKQKSYNSE 122
Cdd:cd22495    1 PLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDltlynpERTITVKGSIETCAKAEE--EIMKKIRESYEND 77
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
53-111 7.11e-03

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411951  Cd Length: 68  Bit Score: 35.64  E-value: 7.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967504803  53 FKIKNNMVGAVIGHSGSKIKDLQHSTNTKIQI---IKGESEALVRIFGNREMKAKAKAIIET 111
Cdd:cd22523    6 FLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIgnqTEGTSERHVTITGSPVSITLAQYLITT 67
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
425-572 8.56e-03

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 37.15  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967504803 425 PMIVYVGNLNLAAVNTVKQNIIVTTEEEKRALTQEFIENMSPndkVIMFVSQKRIADDLSSDfnIQGISVesLHGNSEES 504
Cdd:cd18795    4 PLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKP---VLVFCSSRKECEKTAKD--LAGIAF--HHAGLTRE 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967504803 505 DKERALQDFESGNIKILITT-------DLVARGLDVNDVTHVYNYDFPW-NIEEYVHRVGRIGRAG--KTGTSVTLIT 572
Cdd:cd18795   77 DRELVEELFREGLIKVLVATstlaagvNLPARTVIIKGTQRYDGKGYRElSPLEYLQMIGRAGRPGfdTRGEAIIMTK 154
 
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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