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Conserved domains on  [gi|2217362052|ref|XP_047274939|]
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probable ATP-dependent RNA helicase DDX43 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
145-587 3.71e-158

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


The actual alignment was detected with superfamily member PTZ00110:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 545  Bit Score: 464.25  E-value: 3.71e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 145 IDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQCYpeVMENIKKAGFQKPTP 223
Cdd:PTZ00110   84 INLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPDY--ILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 224 IQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQVEGECCKYSYKG-LRS 302
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELAEQIREQCNKFGASSkIRN 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 303 VCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMT 382
Cdd:PTZ00110  235 TVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMW 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 383 SATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSSTDKVIVFVSRKAVADHLS 460
Cdd:PTZ00110  315 SATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADFLT 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 461 SDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRT 540
Cdd:PTZ00110  395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 541 GVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 587
Cdd:PTZ00110  475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 522
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
69-134 1.20e-27

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: 105.83  E-value: 1.20e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
145-587 3.71e-158

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 464.25  E-value: 3.71e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 145 IDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQCYpeVMENIKKAGFQKPTP 223
Cdd:PTZ00110   84 INLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPDY--ILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 224 IQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQVEGECCKYSYKG-LRS 302
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELAEQIREQCNKFGASSkIRN 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 303 VCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMT 382
Cdd:PTZ00110  235 TVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMW 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 383 SATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSSTDKVIVFVSRKAVADHLS 460
Cdd:PTZ00110  315 SATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADFLT 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 461 SDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRT 540
Cdd:PTZ00110  395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 541 GVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 587
Cdd:PTZ00110  475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
198-603 9.75e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 456.15  E-value: 9.75e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLV 277
Cdd:COG0513     3 SFAD-LGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-----LLQRLDPSRPRAPQALI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 278 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 356
Cdd:COG0513    77 LAPTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 357 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 436
Cdd:COG0513   157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 437 LQSMSsTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 516
Cdd:COG0513   236 LRDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 517 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRvasELINILERANQSIPEELVSMAERFKAHQQKREMERKMERP 596
Cdd:COG0513   315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR---LLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKL 391

                  ....*..
gi 2217362052 597 QGRPKKF 603
Cdd:COG0513   392 KGKKAGR 398
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
209-405 2.45e-141

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: 408.01  E-value: 2.45e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 288
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 368
Cdd:cd17958    81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 369 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVY 405
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
222-393 6.25e-57

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: 188.99  E-value: 6.25e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 222 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpslKGQRNRPGMLVLTPTRELALQVEGECCKY-SYKGL 300
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 301 RSVCVYGGGNRDEQIEELKkGVDIIIATPGRLNDLqMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTV 380
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 2217362052 381 MTSATWPHSVHRL 393
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
213-411 2.41e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 175.37  E-value: 2.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  213 IKKAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGqrnrpgmLVLTPTRELALQVEGE 291
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV-------LVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  292 CCKY-SYKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKI 369
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217362052  370 LLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDL 411
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 ...
69-134 1.20e-27

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: 105.83  E-value: 1.20e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
76-130 1.42e-10

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: 57.29  E-value: 1.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362052  76 SHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDN 130
Cdd:pfam00013   8 SSLVGLIIGKGGSNIKEIREETGAKIQIPPSEsegNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
72-128 1.58e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.45  E-value: 1.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362052   72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVI 128
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITGPPENVEKAAELI 64
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
79-137 1.96e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 47.74  E-value: 1.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIiqEQpESLVKIFGS--KAMQtKAKAVIDNFVKKLEE 137
Cdd:PRK11824  565 IRDVIGPGGKTIREITEETGAKIDI--ED-DGTVKIAATdgEAAE-AAKERIEGITAEPEV 621
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
145-587 3.71e-158

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 464.25  E-value: 3.71e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 145 IDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQCYpeVMENIKKAGFQKPTP 223
Cdd:PTZ00110   84 INLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPDY--ILKSLKNAGFTEPTP 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 224 IQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQVEGECCKYSYKG-LRS 302
Cdd:PTZ00110  156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELAEQIREQCNKFGASSkIRN 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 303 VCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMT 382
Cdd:PTZ00110  235 TVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMW 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 383 SATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSSTDKVIVFVSRKAVADHLS 460
Cdd:PTZ00110  315 SATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRDGDKILIFVETKKGADFLT 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 461 SDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRT 540
Cdd:PTZ00110  395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 541 GVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 587
Cdd:PTZ00110  475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
198-603 9.75e-157

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 456.15  E-value: 9.75e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLV 277
Cdd:COG0513     3 SFAD-LGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-----LLQRLDPSRPRAPQALI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 278 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 356
Cdd:COG0513    77 LAPTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 357 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 436
Cdd:COG0513   157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 437 LQSMSsTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 516
Cdd:COG0513   236 LRDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 517 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRvasELINILERANQSIPEELVSMAERFKAHQQKREMERKMERP 596
Cdd:COG0513   315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR---LLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKL 391

                  ....*..
gi 2217362052 597 QGRPKKF 603
Cdd:COG0513   392 KGKKAGR 398
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
209-405 2.45e-141

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: 408.01  E-value: 2.45e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 288
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 368
Cdd:cd17958    81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 369 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVY 405
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
209-404 1.74e-98

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: 298.20  E-value: 1.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlQPSLKGQRNRPGMLVLTPTRELALQV 288
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL--LPEPKKKGRGPQALVLAPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 367
Cdd:cd00268    79 AEVARKLGkGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 368 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
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 ...
209-404 8.38e-90

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: 276.17  E-value: 8.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQV 288
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLE-RGDGPIVLVLAPTRELAQQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 367
Cdd:cd17966    80 QQEANKFGGSsRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 368 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17966   160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
199-545 3.26e-87

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 277.24  E-value: 3.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 199 FDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKG-QRNRPGMLV 277
Cdd:PRK04837   10 FSD-FALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrKVNQPRALI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 278 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 356
Cdd:PRK04837   89 MAPTRELAVQIHADAEPLAqATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 357 MLDMGFEPQImKILLDVRPD---RQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDLVAvSSVKQNIIVTTEEEKWSHM 433
Cdd:PRK04837  169 MFDLGFIKDI-RWLFRRMPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTG-HRIKEELFYPSNEEKMRLL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 434 QTFLQSmSSTDKVIVFVSRK----AVADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDV 509
Cdd:PRK04837  247 QTLIEE-EWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2217362052 510 HDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 545
Cdd:PRK04837  322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSIS 357
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
207-545 1.54e-86

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 276.69  E-value: 1.54e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVL-QPSLKGQRNRPGmLVLTPTRELA 285
Cdd:PRK10590   10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrQPHAKGRRPVRA-LILTPTRELA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 286 LQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 364
Cdd:PRK10590   89 AQIGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIH 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 365 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlVAVSSVKQNIIVTTEEEKwSHMQTFLQSMSSTD 444
Cdd:PRK10590  169 DIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRK-RELLSQMIGKGNWQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 445 KVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNI 524
Cdd:PRK10590  247 QVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                         330       340
                  ....*....|....*....|.
gi 2217362052 525 EEYVHRIGRTGRAGRTGVSIT 545
Cdd:PRK10590  327 EDYVHRIGRTGRAAATGEALS 347
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
169-551 3.85e-84

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 271.02  E-value: 3.85e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 169 ADSWRKENFNITWDDLKDGekrpipnptctFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGK 248
Cdd:PRK01297   70 ASLWKLEDFVVEPQEGKTR-----------FHD-FNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 249 TLCYLMpGFIHLVLQPSLKGQRNR--PGMLVLTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELK-KGVDI 324
Cdd:PRK01297  138 TAAFLI-SIINQLLQTPPPKERYMgePRALIIAPTRELVVQIAKDAAALTkYTGLNVMTFVGGMDFDKQLKQLEaRFCDI 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 325 IIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRP--DRQTVMTSATWPHSVHRLAQSYLKEPM 402
Cdd:PRK01297  217 LVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPA 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 403 IVYVGTLDlVAVSSVKQNIIVTTEEEKWSHMQTFLQSmSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDR 482
Cdd:PRK01297  297 IVEIEPEN-VASDTVEQHVYAVAGSDKYKLLYNLVTQ-NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKR 374
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052 483 EKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRND 551
Cdd:PRK01297  375 IKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
202-575 9.89e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 270.28  E-value: 9.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 202 AFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQR-NRPGMLVLTP 280
Cdd:PRK04537   13 SFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKpEDPRALILAP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 281 TRELALQVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKML 358
Cdd:PRK04537   93 TRELAIQIHKDAVKFgADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADRMF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 359 DMGFEPQIMKIL--LDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 436
Cdd:PRK04537  173 DLGFIKDIRFLLrrMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET-ETITAARVRQRIYFPADEEKQTLLLGL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 437 LqSMSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 516
Cdd:PRK04537  252 L-SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052 517 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRndwRVASELINILERANQSIPEELVS 575
Cdd:PRK04537  331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLPDIEAYIEQKIPVEPVT 386
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
198-554 1.25e-82

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 265.65  E-value: 1.25e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPslkgqRNRPG--- 274
Cdd:PRK11192    2 TFSE-LELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP-----RRKSGppr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 275 MLVLTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFvNLKNITYLVLD 352
Cdd:PRK11192   76 ILILTPTRELAMQVADQARELAkHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQyIKEENF-DCRAVETLILD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 353 EADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHS-VHRLAQSYLKEPMivyvgTLDLVAVSSVKQNI-----IVTTE 426
Cdd:PRK11192  155 EADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPV-----EVEAEPSRRERKKIhqwyyRADDL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 427 EEKWSHMQTFLQSMSSTdKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRG 506
Cdd:PRK11192  230 EHKTALLCHLLKQPEVT-RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 507 LDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRV 554
Cdd:PRK11192  309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
209-402 8.88e-82

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: 256.15  E-value: 8.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrPGMLVLTPTRELALQV 288
Cdd:cd17953    23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEG-PIGLIMAPTRELALQI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSN---FVNLKNITYLVLDEADKMLDMGFEP 364
Cdd:cd17953   102 YVECKKFSKAlGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANngrVTNLRRVTYVVLDEADRMFDMGFEP 181
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217362052 365 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPM 402
Cdd:cd17953   182 QIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
207-595 3.51e-81

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 262.81  E-value: 3.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPsLKGQRNRPGMLVLTPTRELAL 286
Cdd:PRK11776   13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLG-----LLQK-LDVKRFRVQALVLCPTRELAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGEcckysykgLR------------SVCvyGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA 354
Cdd:PRK11776   87 QVAKE--------IRrlarfipnikvlTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 355 DKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlvAVSSVKQNIIVTTEEEKWSHMQ 434
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDERLPALQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 435 TFLQSM--SSTdkvIVFVSRK----AVADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLD 508
Cdd:PRK11776  235 RLLLHHqpESC---VVFCNTKkecqEVADALNAQ----GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 509 VHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITtltrndwrvaselinileranqsipeeLVSMAERFKAHQQKRE 588
Cdd:PRK11776  308 IKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALS---------------------------LVAPEEMQRANAIEDY 360

                  ....*..
gi 2217362052 589 MERKMER 595
Cdd:PRK11776  361 LGRKLNW 367
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
198-408 1.57e-79

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: 250.10  E-value: 1.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDAFQCyPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQ--PSLKGQRNR--- 272
Cdd:cd17967     1 SFEEAGLR-ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLP-IISKLLEdgPPSVGRGRRkay 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 273 PGMLVLTPTRELALQVEGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVL 351
Cdd:cd17967    79 PSALILAPTRELAIQIYEEARKFSYRsGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052 352 DEADKMLDMGFEPQIMKIL----LDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGT 408
Cdd:cd17967   159 DEADRMLDMGFEPQIRKIVehpdMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
193-407 6.80e-77

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: 244.15  E-value: 6.80e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 193 PNPTCTFDDAfqCYPE-VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRN 271
Cdd:cd18049    20 PKPVLNFYEA--NFPAnVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE-RGD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 272 RPGMLVLTPTRELALQVEGECCKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLV 350
Cdd:cd18049    97 GPICLVLAPTRELAQQVQQVAAEYGRACrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLV 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052 351 LDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 407
Cdd:cd18049   177 LDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
192-592 4.16e-76

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 251.25  E-value: 4.16e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 192 IPNPTCTFDdafQC--YPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVL-QPSLKG 268
Cdd:PLN00206  116 VPPPILSFS---SCglPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPS 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 269 QRNRPGMLVLTPTRELALQVEgECCKYSYKGL--RSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNI 346
Cdd:PLN00206  193 EQRNPLAMVLTPTRELCVQVE-DQAKVLGKGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNV 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 347 TYLVLDEADKMLDMGFEPQIMKILLDVrPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlVAVSSVKQNIIVTTE 426
Cdd:PLN00206  272 SVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPN-RPNKAVKQLAIWVET 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 427 EEKWSHMQTFLQSMSS-TDKVIVFVSRKAVADHLSSDL-ILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLAS 504
Cdd:PLN00206  350 KQKKQKLFDILKSKQHfKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLG 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 505 RGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELINILERANQSIPEELVSmaERFKAHQ 584
Cdd:PLN00206  430 RGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN--SRYLGSG 507

                  ....*...
gi 2217362052 585 QKREMERK 592
Cdd:PLN00206  508 RKRKKKRR 515
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
208-588 5.21e-73

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 245.91  E-value: 5.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 208 EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHlVLQPSLKGqrnrPGMLVLTPTRELALQ 287
Cdd:PRK11634   16 PILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP-LLH-NLDPELKA----PQILVLAPTRELAVQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 288 VEGECCKYS--YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 365
Cdd:PRK11634   90 VAEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 366 IMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTFLQSmSSTDK 445
Cdd:PRK11634  170 VETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLEA-EDFDA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 446 VIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIE 525
Cdd:PRK11634  248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217362052 526 EYVHRIGRTGRAGRTGVSITTLTRNDWRVaseLINILERANQSIPE------ELVSM--AERFKAH-QQKRE 588
Cdd:PRK11634  328 SYVHRIGRTGRAGRAGRALLFVENRERRL---LRNIERTMKLTIPEvelpnaELLGKrrLEKFAAKvQQQLE 396
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
209-404 9.39e-73

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: 231.92  E-value: 9.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrPGMLVLTPTRELALQV 288
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEG-PIAVIVAPTRELAQQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 367
Cdd:cd17952    80 YLEAKKFGkAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 368 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17952   160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
146-407 2.22e-72

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: 233.75  E-value: 2.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 146 DLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEkrpIPNPTCTFDDAfqCYPE-VMENIKKAGFQKPTPI 224
Cdd:cd18050    18 ELPKFEKNFYVEHPEVARMTQYDVEELRRKK-EIT---IRGVG---CPKPVFAFHQA--NFPQyVMDVLLDQNFKEPTPI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 225 QSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQVEGECCKYSYKG-LRSV 303
Cdd:cd18050    89 QCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLE-RGDGPICLVLAPTRELAQQVQQVADDYGKSSrLKST 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 304 CVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMTS 383
Cdd:cd18050   168 CIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWS 247
                         250       260
                  ....*....|....*....|....
gi 2217362052 384 ATWPHSVHRLAQSYLKEPMIVYVG 407
Cdd:cd18050   248 ATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
209-405 1.02e-70

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: 227.20  E-value: 1.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSL--KGQRNRPGMLVLTPTRELAL 286
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLdeETKDDGPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 365
Cdd:cd17945    81 QIEEETQKFaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 366 IMKIL--LDV---RPD---------------RQTVMTSATWPHSVHRLAQSYLKEPMIVY 405
Cdd:cd17945   161 VTKILdaMPVsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
192-400 6.18e-69

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: 224.08  E-value: 6.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 192 IPNPTCTFDDAfQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMP---GFIHLVLQPSLKG 268
Cdd:cd18052    38 PPPAILTFEEA-NLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMKEGLTASSFS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 269 QRNRPGMLVLTPTRELALQVEGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNIT 347
Cdd:cd18052   117 EVQEPQALIVAPTRELANQIFLEARKFSYGtCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLK 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052 348 YLVLDEADKMLDMGFEPQIMKILLDV----RPDRQTVMTSATWPHSVHRLAQSYLKE 400
Cdd:cd18052   197 YLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
PTZ00424 PTZ00424
helicase 45; Provisional
197-578 8.20e-64

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 215.46  E-value: 8.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 197 CTFDDAFQCYP------EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFihLVLQPSLkgqr 270
Cdd:PTZ00424   21 SNYDEIVDSFDalklneDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL--QLIDYDL---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 271 NRPGMLVLTPTRELALQVE------GECCKYSYKGlrsvCVYGGGNRDEqIEELKKGVDIIIATPGRLNDLQMSNFVNLK 344
Cdd:PTZ00424   95 NACQALILAPTRELAQQIQkvvlalGDYLKVRCHA----CVGGTVVRDD-INKLKAGVHMVVGTPGRVYDMIDKRHLRVD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 345 NITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQ-NIIV 423
Cdd:PTZ00424  170 DLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK-DELTLEGIRQfYVAV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 424 TTEEEKWSHMQTFLQSMSSTDKVIVFVSRKAVaDHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLA 503
Cdd:PTZ00424  249 EKEEWKFDTLCDLYETLTITQAIIYCNTRRKV-DYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217362052 504 SRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDwrvASELINILERANQSIPEELVSMAE 578
Cdd:PTZ00424  328 ARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDD---IEQLKEIERHYNTQIEEMPMEVAD 399
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
192-407 7.14e-59

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: 197.18  E-value: 7.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 192 IPNPTCTFDDAfQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHL------VLQPS 265
Cdd:cd18051    16 CPPHIETFSDL-DLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 266 LKGQRNR----PGMLVLTPTRELALQVEGECCKYSYKGLRSVCV-YGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNF 340
Cdd:cd18051    95 ESGYYGRrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVvYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052 341 VNLKNITYLVLDEADKMLDMGFEPQIMKILL-DVRP---DRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 407
Cdd:cd18051   175 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
417-545 2.29e-57

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: 188.87  E-value: 2.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 417 VKQNIIVTTEEEKWSHMQTFLQSMSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRI 496
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217362052 497 LIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 545
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAIT 129
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
222-393 6.25e-57

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: 188.99  E-value: 6.25e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 222 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpslKGQRNRPGMLVLTPTRELALQVEGECCKY-SYKGL 300
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 301 RSVCVYGGGNRDEQIEELKkGVDIIIATPGRLNDLqMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTV 380
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 2217362052 381 MTSATWPHSVHRL 393
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
203-404 7.51e-54

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: 182.12  E-value: 7.51e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 203 FQCY---PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrpgmLVLT 279
Cdd:cd17959     3 FQSMglsPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARA----LILS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 280 PTRELALQ---VEGECCKYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 356
Cdd:cd17959    79 PTRELALQtlkVTKELGKFT--DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 357 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17959   157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
198-401 1.93e-52

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: 178.28  E-value: 1.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDAFQCyPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQpSLKGQRNRPGMLV 277
Cdd:cd17954     1 TFKELGVC-EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP-----ILQ-ALLENPQRFFALV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 278 LTPTRELALQVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEAD 355
Cdd:cd17954    74 LAPTRELAQQISEQFEALgSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEAD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217362052 356 KMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 401
Cdd:cd17954   154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
209-407 3.73e-52

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: 177.40  E-value: 3.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRnrpgMLVLTPTRELALQV 288
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLR----ALILAPTRELASQI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGECCKYSY-KGLRsVCVYGGGNRD--EQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 365
Cdd:cd17957    77 YRELLKLSKgTGLR-IVLLSKSLEAkaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217362052 366 IMKILLDVR-PDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 407
Cdd:cd17957   156 TDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
207-400 4.65e-52

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: 177.78  E-value: 4.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQ-GIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRPGMLVLTPTRELA 285
Cdd:cd17964     3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKP-AGRRSGVSALIISPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 286 LQVEGECCK--YSYKGLRSVCVYGGGNRDEQIEELKK-GVDIIIATPGRLNDLQMSNFV--NLKNITYLVLDEADKMLDM 360
Cdd:cd17964    82 LQIAAEAKKllQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDM 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217362052 361 GFEPQIMKILLDVRP----DRQTVMTSATWPHSVHRLAQSYLKE 400
Cdd:cd17964   162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEXDc smart00487
DEAD-like helicases superfamily;
213-411 2.41e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 175.37  E-value: 2.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  213 IKKAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGqrnrpgmLVLTPTRELALQVEGE 291
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV-------LVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  292 CCKY-SYKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKI 369
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217362052  370 LLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDL 411
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
209-404 1.96e-49

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: 170.60  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQ----PSLKGQRnrPGMLVLTPTREL 284
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFIKGEG--PYGLIVCPSREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 285 ALQVEGECCKYS-------YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKM 357
Cdd:cd17951    79 ARQTHEVIEYYCkalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217362052 358 LDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17951   159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
210-407 6.10e-49

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: 169.08  E-value: 6.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 210 MENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGfIHLVLQPSLKgQRNRPGMLVLTPTRELALQVE 289
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPA-IELLYKLKFK-PRNGTGVIIISPTRELALQIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 290 G---ECCKYSYKGLrsVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 365
Cdd:cd17942    80 GvakELLKYHSQTF--GIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217362052 366 IMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIvYVG 407
Cdd:cd17942   158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPL-YVG 198
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
212-404 1.46e-48

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: 167.73  E-value: 1.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 212 NIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkGQRNRPGMLVLTPTRELALQVEGE 291
Cdd:cd17962     4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL------TEHRNPSALILTPTRELAVQIEDQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 292 CcKYSYKGL---RSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 368
Cdd:cd17962    78 A-KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217362052 369 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17962   157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
214-404 1.16e-47

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: 165.84  E-value: 1.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 214 KKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNR-PGMLVLTPTRELALQVEgEC 292
Cdd:cd17949     7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLP-IIQRLLSLEPRVDRSDgTLALVLVPTRELALQIY-EV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 293 CKysyKGLRSV------CVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 365
Cdd:cd17949    85 LE---KLLKPFhwivpgYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKD 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217362052 366 IMKIL--LDVRPD-----------RQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17949   162 ITKILelLDDKRSkaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
217-401 1.34e-46

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: 162.42  E-value: 1.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 217 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRpgMLVLTPTRELALQVEG---ECC 293
Cdd:cd17947     9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPK-KKAATR--VLVLVPTRELAMQCFSvlqQLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 294 KYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 372
Cdd:cd17947    86 QFT--DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDhLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
                         170       180
                  ....*....|....*....|....*....
gi 2217362052 373 VRPDRQTVMTSATWPHSVHRLAQSYLKEP 401
Cdd:cd17947   164 CPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
207-401 2.76e-46

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: 161.70  E-value: 2.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQ---PSLKGQRnrpgMLVLTPTRE 283
Cdd:cd17940     8 RELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP-----ILEkidPKKDVIQ----ALILVPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 284 LALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGF 362
Cdd:cd17940    79 LALQTSQVCKELGkHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217362052 363 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 401
Cdd:cd17940   159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
209-401 3.21e-45

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: 158.89  E-value: 3.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 288
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP-VLEILLKRKANLKKGQVGALIISPTRELATQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 EGEC---CKYSYKGLRSVCVYGGGNRDEQIEELK-KGVDIIIATPGRLNDL--QMSNFVNLKNITYLVLDEADKMLDMGF 362
Cdd:cd17960    80 YEVLqsfLEHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGF 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217362052 363 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 401
Cdd:cd17960   160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
213-406 1.13e-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: 157.45  E-value: 1.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 213 IKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkgqRNR------PGMLVLTPTRELAL 286
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY--------RERwtpedgLGALIISPTRELAM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGECCKYSYKGLRSVCVYGGGnRDEQIEELK-KGVDIIIATPGRLndLQ-MSNFVNL--KNITYLVLDEADKMLDMGF 362
Cdd:cd17941    77 QIFEVLRKVGKYHSFSAGLIIGG-KDVKEEKERiNRMNILVCTPGRL--LQhMDETPGFdtSNLQMLVLDEADRILDMGF 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217362052 363 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYV 406
Cdd:cd17941   154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
209-404 5.17e-40

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: 144.33  E-value: 5.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELALQV 288
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLV-----FVVIALE-SLDLERRHPQVLILAPTREIAVQI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 289 E---GECCKYsYKGLRsVCVY-GGGNRDEQIEELkKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 364
Cdd:cd17943    75 HdvfKKIGKK-LEGLK-CEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217362052 365 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17943   152 DVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
211-402 1.66e-39

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 143.52  E-value: 1.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 211 ENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQ-----PSlkgqrnrpGM--LVLTPTRE 283
Cdd:cd17955    12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-----ILQrlsedPY--------GIfaLVLTPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 284 LALQ------VEGECCkysykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSN---FVNLKNITYLVLDEA 354
Cdd:cd17955    79 LAYQiaeqfrALGAPL-----GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217362052 355 DKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPM 402
Cdd:cd17955   154 DRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
217-404 2.31e-39

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: 142.85  E-value: 2.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 217 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELALQVEgECCKY- 295
Cdd:cd17939    16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTAT-----FSIGALQ-RIDTTVRETQALVLAPTRELAQQIQ-KVVKAl 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 296 -SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVR 374
Cdd:cd17939    89 gDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLP 168
                         170       180       190
                  ....*....|....*....|....*....|
gi 2217362052 375 PDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17939   169 PETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
209-385 6.97e-39

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: 142.76  E-value: 6.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLCYLMP---GFIHLVLQPSLKGQRNRPGMLVLTPTREL 284
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPileRLLSQKSSNGVGGKQKPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 285 ALQVEG---ECCKYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDL-QMSN--FVNLKNITYLVLDEADKML 358
Cdd:cd17946    81 AVQVKDhlkAIAKYT--NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiQEGNehLANLKSLRFLVLDEADRML 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217362052 359 DMG-FEP--QIMKILLDVRP----DRQTVMTSAT 385
Cdd:cd17946   159 EKGhFAEleKILELLNKDRAgkkrKRQTFVFSAT 192
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
210-399 1.65e-37

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: 138.06  E-value: 1.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 210 MENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGF--IHLVLQPSLKGQRnrPGMLVLTPTRELALQ 287
Cdd:cd17944     2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPRKRGRA--PKVLVLAPTRELANQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 288 VEGECCKYSYKgLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 367
Cdd:cd17944    80 VTKDFKDITRK-LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 368 KIL-----LDVRPDRQTVMTSATWPHSVHRLAQSYLK 399
Cdd:cd17944   159 EILsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
207-404 9.39e-37

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: 135.78  E-value: 9.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGID--LIGVAQTGTGKTLCYLMpGFIHLVlQPSLKgqrnRPGMLVLTPTREL 284
Cdd:cd17963     3 PELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVL-AMLSRV-DPTLK----SPQALCLAPTREL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 285 ALQVEGECCKY-SYKGLRSVCVYGGG--NRDEQIEElkkgvDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDM- 360
Cdd:cd17963    77 ARQIGEVVEKMgKFTGVKVALAVPGNdvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTq 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217362052 361 GFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17963   152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
213-404 5.56e-36

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: 133.86  E-value: 5.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 213 IKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNR-PGMLVLTPTRELALQVEG- 290
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP-IIQKILKAKAESGEEQgTRALILVPTRELAQQVSKv 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 291 --ECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 367
Cdd:cd17961    88 leQLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLK 167
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217362052 368 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd17961   168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
207-406 3.24e-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: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELAL 286
Cdd:cd17950    11 PELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAV-----FVLSTLQ-QLEPVDGQVSVLVICHTRELAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGECCKYS--YKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKML-DMGF 362
Cdd:cd17950    85 QISNEYERFSkyMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDM 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217362052 363 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYV 406
Cdd:cd17950   165 RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
209-390 1.22e-33

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: 128.25  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSL--KGQRNRPGMLVLTPTRELAL 286
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQRLLRYKLlaEGPFNAPRGLVITPSRELAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGECCKYS-YKGLRSVCVyGGGN-----RDEQIEElkkgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDM 360
Cdd:cd17948    80 QIGSVAQSLTeGLGLKVKVI-TGGRtkrqiRNPHFEE----VDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217362052 361 GFEPQIMKIL----LDVRPDR---------QTVMTSATWPHSV 390
Cdd:cd17948   155 SFNEKLSHFLrrfpLASRRSEntdgldpgtQLVLVSATMPSGV 197
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
201-401 1.28e-33

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: 127.18  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 201 DAFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQ---PSLKGqrnrPGMLV 277
Cdd:cd18046     2 DDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTAT-----FSISILQqidTSLKA----TQALV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 278 LTPTRELALQVE------GEcckysYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVL 351
Cdd:cd18046    73 LAPTRELAQQIQkvvmalGD-----YMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217362052 352 DEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 401
Cdd:cd18046   148 DEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
428-538 1.81e-32

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 120.78  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 428 EKWSHMQTFLQSmSSTDKVIVFVSRKavaDHLSSDLIL--GNISVESLHGDREQRDREKALENFKTGKVRILIATDLASR 505
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSQTK---KTLEAELLLekEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217362052 506 GLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAG 538
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
207-404 7.89e-32

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: 122.04  E-value: 7.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQpslkgqrnrpgmLVLTPTRELAL 286
Cdd:cd17938     8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQIVVA------------LILEPSRELAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 QVEGECCKYSY----KGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGF 362
Cdd:cd17938    75 QTYNCIENFKKyldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGN 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217362052 363 EPQIMKIL-----LDVRPDR-QTVMTSATWpHS--VHRLAQSYLKEPMIV 404
Cdd:cd17938   155 LETINRIYnripkITSDGKRlQVIVCSATL-HSfeVKKLADKIMHFPTWV 203
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
208-404 9.43e-31

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: 119.11  E-value: 9.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 208 EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKT----LCYLMpgfihlVLQPSLKgqrnRPGMLVLTPTRE 283
Cdd:cd18045     9 DLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTatfsISVLQ------CLDIQVR----ETQALILSPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 284 LALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGF 362
Cdd:cd18045    79 LAVQIQKVLLALGdYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217362052 363 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd18045   159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
209-386 3.26e-28

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: 112.73  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 209 VMENIKKAGFQKPTPIQSQAWPIVLQGI---------DLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLVLT 279
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLP-----IVQALSKRVVPRLRALIVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 280 PTRELALQVEGECCKYSYKGLRSVCVYGGGN--RDEQIE-------ELKKGVDIIIATPGRLND-LQMSNFVNLKNITYL 349
Cdd:cd17956    76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKsfKKEQKLllvdtsgRYLSRVDILVATPGRLVDhLNSTPGFTLKHLRFL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217362052 350 VLDEADKMLDMGFE---PQIMKILLDVRPDRQTVMTSATW 386
Cdd:cd17956   156 VIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDANL 195
HELICc smart00490
helicase superfamily c-terminal domain;
457-538 3.27e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 107.68  E-value: 3.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  457 DHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGR 536
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2217362052  537 AG 538
Cdd:smart00490  81 AG 82
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
69-134 1.20e-27

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: 105.83  E-value: 1.20e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
201-389 2.45e-22

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: 96.68  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 201 DAFQCYPEVMENIKKA---------GFQKPTPIQSQAWPIVLQG-----------------IDLIGvAQTGTGKTLCYLM 254
Cdd:cd17965     2 DQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepkleVFLLA-AETGSGKTLAYLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 255 PGFIHL---------VLQPSLKGQRN--RPGMLVLTPTRELALQVeGECCK----YSYKGLRSVCVYGGGNRDEQIEELK 319
Cdd:cd17965    81 PLLDYLkrqeqepfeEAEEEYESAKDtgRPRSVILVPTHELVEQV-YSVLKklshTVKLGIKTFSSGFGPSYQRLQLAFK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 320 KGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHS 389
Cdd:cd17965   160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
241-533 5.77e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 90.47  E-value: 5.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 241 VAQTGTGKTLCylmpgFIHLVLQpSLKGQRnrpgMLVLTPTRELALQVEGECCKYSYKGLRsvcvyGGGNRDEqieelkk 320
Cdd:COG1061   106 VAPTGTGKTVL-----ALALAAE-LLRGKR----VLVLVPRRELLEQWAEELRRFLGDPLA-----GGGKKDS------- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 321 GVDIIIATPGRL-NDLQMSNFVNlkNITYLVLDEA--------DKMLDMgFEPqimKILLDV-----RPDRQTvMTSATW 386
Cdd:COG1061   164 DAPITVATYQSLaRRAHLDELGD--RFGLVIIDEAhhagapsyRRILEA-FPA---AYRLGLtatpfRSDGRE-ILLFLF 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 387 PHSVHR------LAQSYLKEPMIVYVGT------LDLVAVSSVKQNIIVTTEEEKWSHMQTFLQSMSSTDKVIVFVSRKA 454
Cdd:COG1061   237 DGIVYEyslkeaIEDGYLAPPEYYGIRVdltderAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVD 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 455 VADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYnfdFPRNIE---EYVHRI 531
Cdd:COG1061   317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGsprEFIQRL 393

                  ..
gi 2217362052 532 GR 533
Cdd:COG1061   394 GR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
208-404 1.50e-18

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: 85.07  E-value: 1.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 208 EVMENIKKAGFQKPTPIQSQAWPIVLQGI--DLIGVAQTGTGKTLCYLmpgfihLVLQPSLKGQRNRPGMLVLTPTRELA 285
Cdd:cd18048    28 ELLRGIYAMGFNRPSKIQENALPMMLADPpqNLIAQSQSGTGKTAAFV------LAMLSRVDALKLYPQCLCLSPTFELA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 286 LQ----VE--GECCK-----YSYKGLRSvcvyGGGNRDEQieelkkgvDIIIATPGRLNDLQMS-NFVNLKNITYLVLDE 353
Cdd:cd18048   102 LQtgkvVEemGKFCVgiqviYAIRGNRP----GKGTDIEA--------QIVIGTPGTVLDWCFKlRLIDVTNISVFVLDE 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217362052 354 ADKMLDM-GFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd18048   170 ADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
241-385 1.25e-16

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: 77.06  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 241 VAQTGTGKTLCYLMPGFIHLVLQpslkgqrnRPGMLVLTPTRELALQVEGECCKYSYKGLRsVCVYGGGNRDEQIEELKK 320
Cdd:cd00046     7 TAPTGSGKTLAALLAALLLLLKK--------GKKVLVLVPTKALALQTAERLRELFGPGIR-VAVLVGGSSAEEREKNKL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052 321 G-VDIIIATPGRL-NDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD--VRPDRQTVMTSAT 385
Cdd:cd00046    78 GdADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
232-589 1.29e-16

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 82.88  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 232 VLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTreLAL---QVEG--EcckysyKGLRSVCV 305
Cdd:COG0514    29 VLAGRDALVVMPTGGGKSLCYQLPALL-------------LPGLtLVVSPL--IALmkdQVDAlrA------AGIRAAFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 306 YGGGNRDEQ---IEELKKG-VDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA--------DkmldmgFEPQIMKI--LL 371
Cdd:COG0514    88 NSSLSAEERrevLRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD------FRPDYRRLgeLR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 372 DVRPDRQTVMTSATWPHSVHR--LAQSYLKEPMiVYVGTLDlvavssvKQNI----IVTTEEEKWSHMQTFLQSMSStDK 445
Cdd:COG0514   162 ERLPNVPVLALTATATPRVRAdiAEQLGLEDPR-VFVGSFD-------RPNLrlevVPKPPDDKLAQLLDFLKEHPG-GS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 446 VIVFV-SRKAV---ADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATdlaSR---GLDVHDVTHVYNF 518
Cdd:COG0514   233 GIVYClSRKKVeelAEWLREA----GIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT---IAfgmGIDKPDVRFVIHY 305
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052 519 DFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELInileraNQSIPEELVSMAERfkahQQKREM 589
Cdd:COG0514   306 DLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI------EQSPPDEERKRVER----AKLDAM 366
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
198-404 3.44e-15

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: 74.76  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 198 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQG--IDLIGVAQTGTGKTLCYLMPGFIHlvLQPSLKGQRnrpgM 275
Cdd:cd18047     2 SFEE-LRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYPQ----C 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 276 LVLTPTRELALQVeGECCKYSYKGLRSVCVYGG--GNRDEQIEELKKgvDIIIATPGRLNDLQMS-NFVNLKNITYLVLD 352
Cdd:cd18047    75 LCLSPTYELALQT-GKVIEQMGKFYPELKLAYAvrGNKLERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217362052 353 EADKML-DMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 404
Cdd:cd18047   152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
217-541 1.20e-13

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 73.98  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 217 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTRELAL-QVEgeccK 294
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV-------------LDGLtLVVSPLISLMKdQVD----Q 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 295 YSYKGLRSVCVYGGGNRDEQIE---ELKKG-VDIIIATPGRLndlQMSNFV-NLK--NITYLVLDEADKMLDMG--FEP- 364
Cdd:PRK11057   85 LLANGVAAACLNSTQTREQQLEvmaGCRTGqIKLLYIAPERL---MMDNFLeHLAhwNPALLAVDEAHCISQWGhdFRPe 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 365 -----QIMKILLDVRPDRQTVMTSATWPHSVHRLAQsyLKEPMIvYVGTLDlvavssvKQNIIVTTEEE--KWSHMQTFL 437
Cdd:PRK11057  162 yaalgQLRQRFPTLPFMALTATADDTTRQDIVRLLG--LNDPLI-QISSFD-------RPNIRYTLVEKfkPLDQLMRYV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 438 QSMSSTDKVIVFVSRKAVADhLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYN 517
Cdd:PRK11057  232 QEQRGKSGIIYCNSRAKVED-TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVH 310
                         330       340
                  ....*....|....*....|....
gi 2217362052 518 FDFPRNIEEYVHrigRTGRAGRTG 541
Cdd:PRK11057  311 FDIPRNIESYYQ---ETGRAGRDG 331
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
447-537 3.04e-12

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: 64.15  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 447 IVFVSRKAVA--------------DHLSSDLILG-NISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHD 511
Cdd:cd18802    29 IIFVERRATAvvlsrllkehpstlAFIRCGFLIGrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                          90       100
                  ....*....|....*....|....*.
gi 2217362052 512 VTHVYNFDFPRNIEEYVHRIGRtGRA 537
Cdd:cd18802   109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
441-532 1.86e-11

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: 61.72  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 441 SSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGK--VRILIATDLASRGLDVHDVTHVYNF 518
Cdd:cd18793    25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILY 104
                          90       100
                  ....*....|....*....|
gi 2217362052 519 DFPRN--IEEY----VHRIG 532
Cdd:cd18793   105 DPWWNpaVEEQaidrAHRIG 124
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
76-130 1.42e-10

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: 57.29  E-value: 1.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362052  76 SHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDN 130
Cdd:pfam00013   8 SSLVGLIIGKGGSNIKEIREETGAKIQIPPSEsegNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
78-133 3.10e-10

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: 56.42  E-value: 3.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVIDNFVK 133
Cdd:cd02394    12 FHGHIIGKGGANIKRIREESGVSIRIPDDEANSdEIRIEGSPEGVKKAKAEILELVD 68
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
447-545 1.27e-09

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


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 56.45  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 447 IVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEE 526
Cdd:cd18794    34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
                          90
                  ....*....|....*....
gi 2217362052 527 YVHRIGRTGRAGRTGVSIT 545
Cdd:cd18794   114 YYQESGRAGRDGLPSECIL 132
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
207-575 1.58e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 60.68  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLCYLMpGFIHLVLQpSLKGqrnrpgmLVLTPTRELA 285
Cdd:COG1204     9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAEL-AILKALLN-GGKA-------LYIVPLRALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 286 LQVEGECCK-YSYKGLRSVCVYGggNRDEQIEELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEAdKMLDmgfEP 364
Cdd:COG1204    80 SEKYREFKRdFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID---DE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 365 Q-------IMKILLDVRPDRQTVMTSATWPhSVHRLAQsylkepmivyvgTLDLVAVSS-----------VKQNIIVTTE 426
Cdd:COG1204   153 SrgptlevLLARLRRLNPEAQIVALSATIG-NAEEIAE------------WLDAELVKSdwrpvplnegvLYDGVLRFDD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 427 EEKWSHMQTF---LQSMSSTDKVIVFVSR--------KAVADHLSSDLILGNIS----------------------VESL 473
Cdd:COG1204   220 GSRRSKDPTLalaLDLLEEGGQVLVFVSSrrdaeslaKKLADELKRRLTPEEREeleelaeellevseethtneklADCL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 474 -------HGDREQRDREKALENFKTGKVRILIATD-------LASRGLDVHDVTHVYNFDFPrnIEEYVHRIGRTGRAGR 539
Cdd:COG1204   300 ekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGY 377
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2217362052 540 --TGVSIttLTRNDWRVASELINILERANqsiPEELVS 575
Cdd:COG1204   378 dpYGEAI--LVAKSSDEADELFERYILGE---PEPIRS 410
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
496-548 1.65e-09

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: 54.63  E-value: 1.65e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217362052 496 ILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLT 548
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
444-549 2.61e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.13  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 444 DKVIVFVSRKAVADHLSSDLILGNISVESLHG--DRE------QRDREKALENFKTGKVRILIATDLASRGLDVHDVTHV 515
Cdd:COG1111   354 SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLV 433
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217362052 516 YNFD-FPRNIeEYVHRIGRTGR--AGRTGVSITTLTR 549
Cdd:COG1111   434 IFYEpVPSEI-RSIQRKGRTGRkrEGRVVVLIAKGTR 469
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
207-545 2.64e-09

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 60.23  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 207 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRpgMLVLTPTRELAL 286
Cdd:COG1205    43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLP-----VLEALLEDPGAT--ALYLYPTKALAR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 -QVEgECCKYSYKGLR--SVCVYGGGNRDEQIEELKKGVDIIIATPGRLNdLQM-------SNFvnLKNITYLVLDEA-- 354
Cdd:COG1205   116 dQLR-RLRELAEALGLgvRVATYDGDTPPEERRWIREHPDIVLTNPDMLH-YGLlphhtrwARF--FRNLRYVVIDEAht 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 355 -------------DKML----DMGFEPQImkilldvrpdrqtVMTSATWPHSVhRLAQSYLKEPMIVyV-------GTLD 410
Cdd:COG1205   192 yrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIGNPA-EHAERLTGRPVTV-VdedgsprGERT 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 411 LVAVSSVkqniIVTTEEEKWSHMQT---FLQSMSSTDKVIVFV-SRKAV---ADHLSSDLI--LGNISVESLHGDREQRD 481
Cdd:COG1205   257 FVLWNPP----LVDDGIRRSALAEAarlLADLVREGLRTLVFTrSRRGAellARYARRALRepDLADRVAAYRAGYLPEE 332
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217362052 482 ReKALEN-FKTGKVRILIAT-------DLAsrGLDVhdvthVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 545
Cdd:COG1205   333 R-REIERgLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
72-129 3.75e-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: 3.75e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES---LVKIFGSKAMQTKAKAVID 129
Cdd:cd00105     3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSgerVVTITGTPEAVEKAKELIE 63
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
429-534 4.27e-09

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 59.47  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 429 KWSHMQTFLQS-MSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGK--VRILIATDLASR 505
Cdd:COG0553   534 KLEALLELLEElLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217362052 506 GLDVHDVTHVYNFDFPRN--IEEY----VHRIGRT 534
Cdd:COG0553   614 GLNLTAADHVIHYDLWWNpaVEEQaidrAHRIGQT 648
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
79-136 8.80e-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: 52.09  E-value: 8.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIiqeQPESLVKIFG-SKAMQTKAKAVIDNFVKKLE 136
Cdd:cd02393    15 IGDVIGPGGKTIRAIIEETGAKIDI---EDDGTVTIFAtDKESAEAAKAMIEDIVAEPE 70
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
211-410 3.70e-08

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: 53.69  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 211 ENIKKAGFQKPTPIQSQAwpI--VLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTreLAL- 286
Cdd:cd17920     3 ILKEVFGYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALL-------------LDGVtLVVSPL--ISLm 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 287 --QVEgECCKysyKGLRSVCVYGGGNRDEQ---IEELKKG-VDIIIATPGRLNDLQMSNFVN----LKNITYLVLDEADK 356
Cdd:cd17920    66 qdQVD-RLQQ---LGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHC 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052 357 MLDMG--FEPQIMKI--LLDVRPDRQTVMTSATWPHSVHRLAQSYLK-EPMIVYVGTLD 410
Cdd:cd17920   142 VSQWGhdFRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRASFD 200
KH smart00322
K homology RNA-binding domain;
72-128 1.58e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.45  E-value: 1.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362052   72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVI 128
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITGPPENVEKAAELI 64
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
78-132 1.49e-06

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: 45.71  E-value: 1.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQE---QPESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22396    11 MVGLIIGRGGEQINRLQAESGAKIQIAPDsggLPERPCTLTGTPDAIETAKRLIDQIV 68
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
79-124 2.00e-06

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: 45.32  E-value: 2.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQ----EQPESLVKIFGSKAMQTKA 124
Cdd:cd22402    12 VGAIIGTKGSHIRYIKRFSGASIKIAPadspDAPERKVTITGPPEAQWKA 61
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
217-390 2.90e-06

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: 48.41  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 217 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgqrnrpgmLVLTPTreLAL---QVEGecc 293
Cdd:cd18018     9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLT--------LVVSPL--IALmkdQVDA--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 294 kySYKGLRSVCvYGGGNRDEQ----IEELKKG-VDIIIATPGRLNDLQMSNFV-NLKNITYLVLDEADKMLDMG--FEP- 364
Cdd:cd18018    76 --LPRAIKAAA-LNSSLTREErrriLEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWShnFRPd 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217362052 365 -----QIMKILLDVRPdrqTVMTSATWPHSV 390
Cdd:cd18018   153 ylrlcRVLRELLGAPP---VLALTATATKRV 180
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
78-128 3.02e-06

eighth 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 eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 44.89  E-value: 3.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVI 128
Cdd:cd22411    10 FHKNIIGKGGATIKKIREETNTRIDLPEENSDSdVITITGKKEDVEKARERI 61
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
222-354 3.56e-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: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 222 TPIQSQAW-PIVLQGIDLIGVAQTGTGKTLCYLmpgfihLVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKySYKGL 300
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAE------LAILRALATSGGK--AVYIAPTRALVNQKEADLRE-RFGPL 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052 301 RSVCVYGGGNRDEQIEELKKGvDIIIATPGRLnDLQMSNF--VNLKNITYLVLDEA 354
Cdd:cd17921    74 GKNVGLLTGDPSVNKLLLAEA-DILVATPEKL-DLLLRNGgeRLIQDVRLVVVDEA 127
PRK13766 PRK13766
Hef nuclease; Provisional
445-549 3.94e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.87  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 445 KVIVFV-SR---KAVADHLSSDlilgNISVESLHG--DRE------QRDREKALENFKTGKVRILIATDLASRGLDVHDV 512
Cdd:PRK13766  367 RIIVFTqYRdtaEKIVDLLEKE----GIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSV 442
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217362052 513 THVYnFDFP-----RNIEeyvhRIGRTGR--AGRTGVSITTLTR 549
Cdd:PRK13766  443 DLVI-FYEPvpseiRSIQ----RKGRTGRqeEGRVVVLIAKGTR 481
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
443-539 4.25e-06

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 46.86  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 443 TDKVIVFVSRKAVADHLSSDLILgnisvESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHV----YNF 518
Cdd:cd18789    49 GDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAiqisGHG 123
                          90       100
                  ....*....|....*....|.
gi 2217362052 519 DFPRnieEYVHRIGRTGRAGR 539
Cdd:cd18789   124 GSRR---QEAQRLGRILRPKK 141
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
78-128 5.56e-06

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: 44.13  E-value: 5.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQII---QEQP---ESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22437     9 SCGLIIGKGGSTIKELREDSNANIKISpkdQLLPgssERIVTITGSFDQVVKAVALI 65
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
439-541 7.21e-06

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 46.19  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 439 SMSSTDKVIVFV----SRKAVADHLSSD-------LILGNISVESLHGdREQRDREKALENFKTGKVRILIATDLASRGL 507
Cdd:cd18801    26 QEGSDTRVIIFSefrdSAEEIVNFLSKIrpgiratRFIGQASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGL 104
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217362052 508 DVHDVTHVYNFDFPRNIEEYVHRIGRTGRaGRTG 541
Cdd:cd18801   105 DIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
232-385 7.53e-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: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 232 VLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpsLKGQRnrpgMLVLTPTRELALQVEGECCKYSYKGLRsvCVYGGGNR 311
Cdd:cd18028    14 LLKGENLLISIPTASGKTLIAEMAMVNTL-----LEGGK----ALYLVPLRALASEKYEEFKKLEEIGLK--VGISTGDY 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052 312 DEQIEELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ---IMKILLDVRPDRQTVMTSAT 385
Cdd:cd18028    83 DEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTlesIVARLRRLNPNTQIIGLSAT 158
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
406-536 1.06e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 45.72  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 406 VGTLDLVAVSSVkQNIIVTTEEEKWSHM-QTFLQSMSSTDKVIVFV-SRKA---VADHLSSdlILGNISVESL----HG- 475
Cdd:cd18796     1 KKKLDIKVILPV-APEIFPWAGESGADAyAEVIFLLERHKSTLVFTnTRSQaerLAQRLRE--LCPDRVPPDFialhHGs 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052 476 -DREQRDR-EKALenfKTGKVRILIAT---DLasrGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGR 536
Cdd:cd18796    78 lSRELREEvEAAL---KRGDLKVVVATsslEL---GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
79-110 1.06e-05

third 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 third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 1.06e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES 110
Cdd:cd22398    11 VGVVIGKGGEMIKKIQNETGARVQFKPDDGNS 42
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
239-354 1.48e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.11  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 239 IGVAQTGTGKTL--CYLMPGFIHLVLQPSLKGQRnrpgMLVLTPTRELALQVegecCKY--SYKGLRSVCVYGGGNRDEQ 314
Cdd:cd18034    20 IVVLPTGSGKTLiaVMLIKEMGELNRKEKNPKKR----AVFLVPTVPLVAQQ----AEAirSHTDLKVGEYSGEMGVDKW 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217362052 315 I-----EELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA 354
Cdd:cd18034    92 TkerwkEELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
79-137 1.96e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 47.74  E-value: 1.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIiqEQpESLVKIFGS--KAMQtKAKAVIDNFVKKLEE 137
Cdd:PRK11824  565 IRDVIGPGGKTIREITEETGAKIDI--ED-DGTVKIAATdgEAAE-AAKERIEGITAEPEV 621
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
220-372 2.07e-05

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: 45.89  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 220 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMpgfihlVLQPSLKGQRNRPG--MLVLTPTRELALQVEGECCKYSY 297
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVL------ICEHHLKKFPAGRKgkVVFLANKVPLVEQQKEVFRKHFE 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052 298 KGLRSVCVYGGGNRDE-QIEELKKGVDIIIATPGRL-NDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 372
Cdd:cd17927    76 RPGYKVTGLSGDTSENvSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRYLD 152
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
77-132 3.32e-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: 41.85  E-value: 3.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052  77 HFVGAVIGRGGSKIKNIQSTTNTTIQII---QEQPESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22462     8 HAVGSVIGRGGSNINQIREISGAKVEVLkpdSATGERIVLISGTPDQARHAQNLIEAFI 66
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
218-285 8.33e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.86  E-value: 8.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052 218 FQKPTPIQSQAWPIVLQGID-LIgVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELA 285
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLYISPLKALA 89
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
79-134 9.18e-05

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: 41.08  E-value: 9.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22479    12 VGLIIGRGGEQINKIQQDSGCKVQISPDSgglPERSVSLTGSPEAVQKAKMMLDDIVSR 70
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
225-354 1.24e-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: 43.34  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 225 QSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkgQRNRPGMLVLTPTRELALQVEGECCKYSYKGLRSVC 304
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-------RDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217362052 305 V--YGGgnrDEQIEE----LKKGVDIIIATPGRLN-------DLQMSNFVNLKnitYLVLDEA 354
Cdd:cd17923    78 VatYDG---DTPREErraiIRNPPRILLTNPDMLHyallphhDRWARFLRNLR---YVVLDEA 134
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
349-539 2.74e-04

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 43.57  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 349 LVLDEADKMLD--MGFEPQIMKILLDVrpDRQTVMTSATWPHSVHRLAQSYLkepMIVYVGTLDLVAVSSVKQNIIVTTE 426
Cdd:cd09639   127 LIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEKIG---YVEENEPLDLKPNERAPFIKIESDK 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 427 EEKWSHMQTFLQSMSSTDKVIVFVSRKAVADHLSSDLILGNISVES--LHGDREQRDREKA----LENFKTGKVRILIAT 500
Cdd:cd09639   202 VGEISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKDRAKKeaelLLEFKKSEKFVIVAT 281
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217362052 501 DLASRGLDVhdvthvyNFDF----PRNIEEYVHRIGRTGRAGR 539
Cdd:cd09639   282 QVIEASLDI-------SVDVmiteLAPIDSLIQRLGRLHRYGE 317
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
69-117 3.04e-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: 39.18  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ----PESLVKIFGS 117
Cdd:cd22400     1 PLRILVPSEFVGAIIGKGGATIRQITQQTGARIDIHRKEnagaAEKAITIYGT 53
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
78-134 3.93e-04

fourth 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 fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 39.17  E-value: 3.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22449    14 YVPHIIGKKGANINKLREEYGVKIDFEDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
72-118 4.04e-04

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: 39.14  E-value: 4.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217362052  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSK 118
Cdd:cd22439     6 ITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEdgsTERSVTITGTP 55
KH-I_IGF2BP3_rpt2 cd22495
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
69-142 4.59e-04

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: 39.25  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQI--IQE----QPESLVKIFGSKAMQTKAKAVIdnfVKKLEENYNSE 142
Cdd:cd22495     1 PLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITIspLQDltlyNPERTITVKGSIETCAKAEEEI---MKKIRESYEND 77
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
214-358 4.68e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 41.54  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 214 KKAGFqKPTPIQsQAWPI-VLQGIDLIGVAQTGTGKTLCYLMpgfIHLVLqpSLKGQRnrpgMLVLTPTRELALQVEGEC 292
Cdd:cd17924    12 KKTGF-PPWGAQ-RTWAKrLLRGKSFAIIAPTGVGKTTFGLA---TSLYL--ASKGKR----SYLIFPTKSLVKQAYERL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217362052 293 CKYSYKGLRSV--CVYGGGNRDEQIEELKKGV-----DIIIATPGRLNDlqmsNFVNLKNITY--LVLDEADKML 358
Cdd:cd17924    81 SKYAEKAGVEVkiLVYHSRLKKKEKEELLEKIekgdfDILVTTNQFLSK----NFDLLSNKKFdfVFVDDVDAVL 151
KH-I_IGF2BP1_rpt2 cd22493
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
66-142 5.39e-04

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. It 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: 411921  Cd Length: 97  Bit Score: 39.66  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052  66 EELPLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ------PESLVKIFGSKAMQTKAKAVIdnfVKKLEENY 139
Cdd:cd22493     3 DEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISPLQdltlynPERTITVKGSIEACCRAEQEI---MKKVREAY 79

                  ...
gi 2217362052 140 NSE 142
Cdd:cd22493    80 END 82
PRK05580 PRK05580
primosome assembly protein PriA; Validated
483-541 7.90e-04

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 42.45  E-value: 7.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217362052 483 EKALENFKTGKVRILIATDLASRGLDVHDVTHV---------YNFDFpRNIEE----YVHRIGRTGRAGRTG 541
Cdd:PRK05580  470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTLVgvldadlglFSPDF-RASERtfqlLTQVAGRAGRAEKPG 540
KH-I_FUBP1_rpt1 cd22478
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
79-134 1.24e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; 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. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411906 [Multi-domain]  Cd Length: 75  Bit Score: 37.70  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22478    15 VGFIIGRGGEQISRIQQESGCKIQIAPDSgglPERSCMLTGTPESVQSAKRLLDQIVEK 73
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
220-372 1.34e-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: 40.54  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 220 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRPGMLVltPTRELALQVEGECCKYSYKG 299
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS-AGEKGRVVVLV--NKVPLVEQQLEKFFKYFRKG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052 300 LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRL-NDLQ---MSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 372
Cdd:cd18036    79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILiNNLLsgrEEERVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLD 155
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
79-117 1.43e-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: 37.62  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQE-QPES---LVKIFGS 117
Cdd:cd22433    13 AGCIIGRAGFKIKELREKTGATIKVYSEcCPRStdrVVQIGGK 55
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
79-128 1.52e-03

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 37.70  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217362052  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQE-----QPESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22428    16 VGLIIGRQGATIKQIQKETGARIDFKDEgsggeLPERVLLIQGNPVQAQRAEEAI 70
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
241-354 1.52e-03

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: 39.81  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 241 VAQTGTGKTLCYLMpgfihlVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKYSYKGLRSVCVYGGGNRDEQIEELKK 320
Cdd:cd18035    22 VLPTGLGKTIIAIL------VAADRLTKKGGK--VLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPEERAERWDA 93
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217362052 321 GvDIIIATPGRL-NDLqMSNFVNLKNITYLVLDEA 354
Cdd:cd18035    94 S-KIIVATPQVIeNDL-LAGRITLDDVSLLIFDEA 126
KH-I_HNRNPK_rpt1 cd22432
first type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
80-114 1.54e-03

first 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 first one.


Pssm-ID: 411860 [Multi-domain]  Cd Length: 64  Bit Score: 37.16  E-value: 1.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217362052  80 GAVIGRGGSKIKNIQSTTNTTIQIIQEQ-PESLVKI 114
Cdd:cd22432    14 GAIIGKGGENIKRLRTEYNASVSVPDSSgPERILTI 49
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
70-132 1.55e-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: 37.17  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217362052  70 LCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQ-TKAKAVIDNFV 132
Cdd:cd22419     3 LSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGvDSARTRIEVLV 66
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
77-105 1.75e-03

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: 37.17  E-value: 1.75e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217362052  77 HFVGAVIGRGGSKIKNIQSTTNTTIQIIQ 105
Cdd:cd09031    10 NLVGAILGKGGKTLVEIQELTGARIQISK 38
KH-I_KHDC1_like cd22440
type I K homology (KH) RNA-binding domain found in KHDC1-like family; The KHDC1-like family ...
69-131 1.88e-03

type I K homology (KH) RNA-binding domain found in KHDC1-like family; The KHDC1-like family corresponds to a group of structurally related proteins characterized by an atypical RNA-binding KH domain. They are unique to eutherian mammals and specifically expressed in oocytes and/or embryonic stem cells. Family members include KH homology domain-containing protein 1 (KHDC1), KHDC1-like protein (KHDC1L), KHDC3-like protein (KHDC3L, also called ES cell-associated transcript 1 protein or ECAT1), developmental pluripotency-associated 5 protein (DPPA5, also called embryonal stem cell-specific gene 1 protein or ESG-1), Oocyte-expressed protein (OOEP, also called KH homology domain-containing protein 2 or KHDC2, or Oocyte- and embryo-specific protein 19 or OEP19). KHDC3L is essential for human oocyte maturation and pre-implantation development of the resulting embryos. DPPA5 is involved in the maintenance of embryonic stem (ES) cell pluripotency. OOEP plays an essential role for zygotes to progress beyond the first embryonic cell divisions.


Pssm-ID: 411868  Cd Length: 68  Bit Score: 37.28  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217362052  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKI--FGSKAMQTKAKAVIDNF 131
Cdd:cd22440     4 PSVFHVEARLLEKIFGPDGTLIPHLEQESHTLIHVDRWDPEGKAEItiFGPPRYRQRAKWMLQCL 68
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
76-103 2.64e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. 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. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 36.83  E-value: 2.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 2217362052  76 SHFVGAVIGRGGSKIKNIQSTTNTTIQI 103
Cdd:cd22460     8 SSQAGSLIGKGGAIIKQIREESGASVRI 35
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
72-128 2.68e-03

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 36.73  E-value: 2.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217362052  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIqIIQEQPES----LVKIFGSKAMQTKAKAVI 128
Cdd:cd22395     4 FEVPSELVGRLIGKQGRNVKQLKQKSGAKI-YIKPHPYTqnfqICSIEGTQQQIDKALKLI 63
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
82-137 3.23e-03

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 36.82  E-value: 3.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052  82 VIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVIDNFVKKLEE 137
Cdd:cd22416    16 IIGQKGADVRKMMDEFDVNISIPPAELQSdIIKITGPPANVERAKAALLERVKELEA 72
KH-I_FUBP2_rpt3 cd22485
third type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
77-132 3.53e-03

third 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 third one.


Pssm-ID: 411913  Cd Length: 68  Bit Score: 36.48  E-value: 3.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217362052  77 HFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22485    10 HSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDgtgPEKIAHIMGPPDRCEHAARIINDLL 68
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
72-106 4.72e-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: 35.90  E-value: 4.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217362052  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQE 106
Cdd:cd22457     3 ISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKA 37
KH-I_FUBP2_rpt4 cd22488
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
70-129 5.46e-03

fourth 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 fourth one.


Pssm-ID: 411916  Cd Length: 69  Bit Score: 35.85  E-value: 5.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052  70 LCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES------LVKIFGSKAMQTKAKAVID 129
Cdd:cd22488     2 MTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNgdpnfkLFIIRGSPQQIDHAKQLIE 67
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
77-132 7.09e-03

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: 35.77  E-value: 7.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217362052  77 HFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22424    13 RVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVERAREEIEAHI 68
ResIII pfam04851
Type III restriction enzyme, res subunit;
241-354 7.40e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217362052 241 VAQTGTGKTLCYLmpgfiHLVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKYSYKGLRSVCVYGGGNRDEQieelKK 320
Cdd:pfam04851  29 VMATGSGKTLTAA-----KLIARLFKKGPIKK--VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDES----VD 97
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217362052 321 GVDIIIATPGRLN--DLQMSNFVNLKNITYLVLDEA 354
Cdd:pfam04851  98 DNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEA 133
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
80-117 7.65e-03

second 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 second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 35.32  E-value: 7.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217362052  80 GAVIGRGGSKIKNIQSTTNTTIQIIQEQ-PES---LVKIFGS 117
Cdd:cd02396    14 GSLIGKGGSKIKEIRESTGASVQVASEMlPNSterAVTISGS 55
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
80-128 9.37e-03

second 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 second one.


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 35.29  E-value: 9.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217362052  80 GAVIGRGGSKIKNIQSTTNTTIQIIQEQ-----PESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22436    13 GMIIGKGGATIKAIMEQSGARVQISQKPesinlQERVVTVTGEPEANRKAVSLI 66
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
78-128 9.51e-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: 35.28  E-value: 9.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217362052  78 FVGAVIGRGGSKIKNIQSTTNTTIQI--IQE----QPESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22401    10 LCGRLIGKDGRNIKKIMEDTNTKITIssLQDltsyNPERTITIKGSLEAMSEAESLI 66
 
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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