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Conserved domains on  [gi|222352149|ref|NP_061135|]
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probable ATP-dependent RNA helicase DDX43 [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 ...
171-631 1.06e-157

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: 464.63  E-value: 1.06e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 171 IDWDQIreeglkwqktkwaDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQC 249
Cdd:PTZ00110  79 IDWKSI-------------NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 250 YpeVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELA 329
Cdd:PTZ00110 140 Y--ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELA 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:PTZ00110 217 EQIREQCNKFGASSkIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSS 486
Cdd:PTZ00110 297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRD 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 487 TDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPR 566
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149 567 NIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 631
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 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 1.40e-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: 105.44  E-value: 1.40e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22430    1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
171-631 1.06e-157

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 464.63  E-value: 1.06e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 171 IDWDQIreeglkwqktkwaDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQC 249
Cdd:PTZ00110  79 IDWKSI-------------NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 250 YpeVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELA 329
Cdd:PTZ00110 140 Y--ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELA 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:PTZ00110 217 EQIREQCNKFGASSkIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSS 486
Cdd:PTZ00110 297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRD 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 487 TDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPR 566
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149 567 NIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 631
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
242-647 2.15e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 456.53  E-value: 2.15e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLV 321
Cdd:COG0513    3 SFAD-LGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-----LLQRLDPSRPRAPQALI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 322 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 400
Cdd:COG0513   77 LAPTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 401 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 480
Cdd:COG0513  157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 481 LQSMSsTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 560
Cdd:COG0513  236 LRDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 561 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRvasELINILERANQSIPEELVSMAERFKAHQQKREMERKMERP 640
Cdd:COG0513  315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR---LLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKL 391

                 ....*..
gi 222352149 641 QGRPKKF 647
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 ...
253-449 6.30e-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: 408.39  E-value: 6.30e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 332
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 412
Cdd:cd17958   81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 413 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVY 449
Cdd:cd17958  161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
266-437 6.58e-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: 189.76  E-value: 6.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  266 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpslKGQRNRPGMLVLTPTRELALQVEGECCKY-SYKGL 344
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  345 RSVCVYGGGNRDEQIEELKkGVDIIIATPGRLNDLqMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTV 424
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 222352149  425 MTSATWPHSVHRL 437
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
257-455 1.79e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.53  E-value: 1.79e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149   257 IKKAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGqrnrpgmLVLTPTRELALQVEGE 335
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV-------LVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149   336 CCKY-SYKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKI 413
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 222352149   414 LLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDL 455
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 1.40e-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: 105.44  E-value: 1.40e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149  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 1.19e-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: 1.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 222352149   76 SHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSKAMQTKAKAVIDN 130
Cdd:pfam00013   8 SSLVGLIIGKGGSNIKEIREETGAKIQIPPSEsegNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
72-128 1.37e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.83  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 222352149    72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVI 128
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITGPPENVEKAAELI 64
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
79-137 1.98e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 47.74  E-value: 1.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149  79 VGAVIGRGGSKIKNIQSTTNTTIQIiqEQpESLVKIFGS--KAMQtKAKAVIDNFVKKLEE 137
Cdd:PRK11824 565 IRDVIGPGGKTIREITEETGAKIDI--ED-DGTVKIAATdgEAAE-AAKERIEGITAEPEV 621
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
171-631 1.06e-157

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 464.63  E-value: 1.06e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 171 IDWDQIreeglkwqktkwaDLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEKrpIPNPTCTFDD-AFQC 249
Cdd:PTZ00110  79 IDWKSI-------------NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EIT---IIAGEN--VPKPVVSFEYtSFPD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 250 YpeVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELA 329
Cdd:PTZ00110 140 Y--ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDGPIVLVLAPTRELA 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:PTZ00110 217 EQIREQCNKFGASSkIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKE-PMIVYVGTLDLVAVSSVKQNIIVTTEEEKWSHMQTFLQS-MSS 486
Cdd:PTZ00110 297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRD 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 487 TDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPR 566
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149 567 NIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELINILERANQSIPEELVSMA-ERFKAHQQKR 631
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSnERSNGTERRR 522
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
242-647 2.15e-156

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 456.53  E-value: 2.15e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLV 321
Cdd:COG0513    3 SFAD-LGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP-----LLQRLDPSRPRAPQALI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 322 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 400
Cdd:COG0513   77 LAPTRELALQVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 401 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 480
Cdd:COG0513  157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 481 LQSMSsTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 560
Cdd:COG0513  236 LRDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 561 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRvasELINILERANQSIPEELVSMAERFKAHQQKREMERKMERP 640
Cdd:COG0513  315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR---LLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKL 391

                 ....*..
gi 222352149 641 QGRPKKF 647
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 ...
253-449 6.30e-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: 408.39  E-value: 6.30e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 332
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 412
Cdd:cd17958   81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 413 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVY 449
Cdd:cd17958  161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
253-448 2.99e-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: 298.97  E-value: 2.99e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlQPSLKGQRNRPGMLVLTPTRELALQV 332
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL--LPEPKKKGRGPQALVLAPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 411
Cdd:cd00268   79 AEVARKLGkGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 412 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
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 ...
253-448 2.74e-89

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: 275.79  E-value: 2.74e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQV 332
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLE-RGDGPIVLVLAPTRELAQQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 411
Cdd:cd17966   80 QQEANKFGGSsRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 412 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
243-589 7.87e-87

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 277.62  E-value: 7.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 243 FDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKG-QRNRPGMLV 321
Cdd:PRK04837  10 FSD-FALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrKVNQPRALI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 322 LTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 400
Cdd:PRK04837  89 MAPTRELAVQIHADAEPLAqATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 401 MLDMGFEPQImKILLDVRPD---RQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDLVAvSSVKQNIIVTTEEEKWSHM 477
Cdd:PRK04837 169 MFDLGFIKDI-RWLFRRMPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTG-HRIKEELFYPSNEEKMRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 478 QTFLQSmSSTDKVIVFVSRK----AVADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDV 553
Cdd:PRK04837 247 QTLIEE-EWPDRAIIFANTKhrceEIWGHLAAD----GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 222352149 554 HDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 589
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSIS 357
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
251-589 4.04e-86

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 277.07  E-value: 4.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVL-QPSLKGQRNRPGmLVLTPTRELA 329
Cdd:PRK10590  10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrQPHAKGRRPVRA-LILTPTRELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:PRK10590  89 AQIGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlVAVSSVKQNIIVTTEEEKwSHMQTFLQSMSSTD 488
Cdd:PRK10590 169 DIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRK-RELLSQMIGKGNWQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 489 KVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNI 568
Cdd:PRK10590 247 QVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                        330       340
                 ....*....|....*....|.
gi 222352149 569 EEYVHRIGRTGRAGRTGVSIT 589
Cdd:PRK10590 327 EDYVHRIGRTGRAAATGEALS 347
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
213-595 1.44e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 271.02  E-value: 1.44e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 213 ADSWRKENFNITWDDLKDGekrpipnptctFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGK 292
Cdd:PRK01297  70 ASLWKLEDFVVEPQEGKTR-----------FHD-FNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 293 TLCYLMpGFIHLVLQPSLKGQRNR--PGMLVLTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELK-KGVDI 368
Cdd:PRK01297 138 TAAFLI-SIINQLLQTPPPKERYMgePRALIIAPTRELVVQIAKDAAALTkYTGLNVMTFVGGMDFDKQLKQLEaRFCDI 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 369 IIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRP--DRQTVMTSATWPHSVHRLAQSYLKEPM 446
Cdd:PRK01297 217 LVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPA 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 447 IVYVGTLDlVAVSSVKQNIIVTTEEEKWSHMQTFLQSmSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDR 526
Cdd:PRK01297 297 IVEIEPEN-VASDTVEQHVYAVAGSDKYKLLYNLVTQ-NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKR 374
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149 527 EKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRND 595
Cdd:PRK01297 375 IKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
246-619 1.26e-82

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 271.44  E-value: 1.26e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 246 AFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQR-NRPGMLVLTP 324
Cdd:PRK04537  13 SFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKpEDPRALILAP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 325 TRELALQVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKML 402
Cdd:PRK04537  93 TRELAIQIHKDAVKFgADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADRMF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 403 DMGFEPQIMKIL--LDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTF 480
Cdd:PRK04537 173 DLGFIKDIRFLLrrMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET-ETITAARVRQRIYFPADEEKQTLLLGL 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 481 LqSMSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVY 560
Cdd:PRK04537 252 L-SRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149 561 NFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRndwRVASELINILERANQSIPEELVS 619
Cdd:PRK04537 331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLPDIEAYIEQKIPVEPVT 386
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
242-598 3.26e-82

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 266.04  E-value: 3.26e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPslkgqRNRPG--- 318
Cdd:PRK11192   2 TFSE-LELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP-----RRKSGppr 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 319 MLVLTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFvNLKNITYLVLD 396
Cdd:PRK11192  76 ILILTPTRELAMQVADQARELAkHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQyIKEENF-DCRAVETLILD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 397 EADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHS-VHRLAQSYLKEPMivyvgTLDLVAVSSVKQNI-----IVTTE 470
Cdd:PRK11192 155 EADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPV-----EVEAEPSRRERKKIhqwyyRADDL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 471 EEKWSHMQTFLQSMSSTdKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRG 550
Cdd:PRK11192 230 EHKTALLCHLLKQPEVT-RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 222352149 551 LDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRV 598
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) ...
253-446 1.22e-81

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: 256.92  E-value: 1.22e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrPGMLVLTPTRELALQV 332
Cdd:cd17953   23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEG-PIGLIMAPTRELALQI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSN---FVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:cd17953  102 YVECKKFSKAlGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANngrVTNLRRVTYVVLDEADRMFDMGFEP 181
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPM 446
Cdd:cd17953  182 QIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
251-639 7.44e-81

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 263.20  E-value: 7.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPsLKGQRNRPGMLVLTPTRELAL 330
Cdd:PRK11776  13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLG-----LLQK-LDVKRFRVQALVLCPTRELAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGEcckysykgLR------------SVCvyGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA 398
Cdd:PRK11776  87 QVAKE--------IRrlarfipnikvlTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 399 DKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlvAVSSVKQNIIVTTEEEKWSHMQ 478
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDERLPALQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 479 TFLQSM--SSTdkvIVFVSRK----AVADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLD 552
Cdd:PRK11776 235 RLLLHHqpESC---VVFCNTKkecqEVADALNAQ----GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 553 VHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITtltrndwrvaselinileranqsipeeLVSMAERFKAHQQKRE 632
Cdd:PRK11776 308 IKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALS---------------------------LVAPEEMQRANAIEDY 360

                 ....*..
gi 222352149 633 MERKMER 639
Cdd:PRK11776 361 LGRKLNW 367
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
242-452 2.49e-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: 250.87  E-value: 2.49e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDAFQCyPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQ--PSLKGQRNR--- 316
Cdd:cd17967    1 SFEEAGLR-ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLP-IISKLLEdgPPSVGRGRRkay 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 317 PGMLVLTPTRELALQVEGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVL 395
Cdd:cd17967   79 PSALILAPTRELAIQIYEEARKFSYRsGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149 396 DEADKMLDMGFEPQIMKIL----LDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGT 452
Cdd:cd17967  159 DEADRMLDMGFEPQIRKIVehpdMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
237-451 1.82e-76

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: 1.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 237 PNPTCTFDDAfqCYPE-VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRN 315
Cdd:cd18049   20 PKPVLNFYEA--NFPAnVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE-RGD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 316 RPGMLVLTPTRELALQVEGECCKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLV 394
Cdd:cd18049   97 GPICLVLAPTRELAQQVQQVAAEYGRACrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLV 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149 395 LDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 451
Cdd:cd18049  177 LDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
236-636 5.95e-76

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 252.02  E-value: 5.95e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 236 IPNPTCTFDdafQC--YPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVL-QPSLKG 312
Cdd:PLN00206 116 VPPPILSFS---SCglPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPS 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 313 QRNRPGMLVLTPTRELALQVEgECCKYSYKGL--RSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNI 390
Cdd:PLN00206 193 EQRNPLAMVLTPTRELCVQVE-DQAKVLGKGLpfKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 391 TYLVLDEADKMLDMGFEPQIMKILLDVrPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDlVAVSSVKQNIIVTTE 470
Cdd:PLN00206 272 SVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPN-RPNKAVKQLAIWVET 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 471 EEKWSHMQTFLQSMSS-TDKVIVFVSRKAVADHLSSDL-ILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLAS 548
Cdd:PLN00206 350 KQKKQKLFDILKSKQHfKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLG 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 549 RGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELINILERANQSIPEELVSmaERFKAHQ 628
Cdd:PLN00206 430 RGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN--SRYLGSG 507

                 ....*...
gi 222352149 629 QKREMERK 636
Cdd:PLN00206 508 RKRKKKRR 515
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
180-451 1.22e-73

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: 237.99  E-value: 1.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 180 GLKWQKTKW--ADLPPIKKNFYKESTATSAMSKVEADSWRKENfNITwddLKDGEkrpIPNPTCTFDDAfqCYPE-VMEN 256
Cdd:cd18050    6 GERLRKKKWdlSELPKFEKNFYVEHPEVARMTQYDVEELRRKK-EIT---IRGVG---CPKPVFAFHQA--NFPQyVMDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 257 IKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgQRNRPGMLVLTPTRELALQVEGEC 336
Cdd:cd18050   77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLE-RGDGPICLVLAPTRELAQQVQQVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 337 CKYSYKG-LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILL 415
Cdd:cd18050  156 DDYGKSSrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 222352149 416 DVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 451
Cdd:cd18050  236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
252-632 1.02e-72

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 246.30  E-value: 1.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 252 EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHlVLQPSLKGqrnrPGMLVLTPTRELALQ 331
Cdd:PRK11634  16 PILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP-LLH-NLDPELKA----PQILVLAPTRELAVQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 332 VEGECCKYS--YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 409
Cdd:PRK11634  90 VAEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 410 IMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQNIIVTTEEEKWSHMQTFLQSmSSTDK 489
Cdd:PRK11634 170 VETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLEA-EDFDA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 490 VIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIE 569
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222352149 570 EYVHRIGRTGRAGRTGVSITTLTRNDWRVaseLINILERANQSIPE------ELVSM--AERFKAH-QQKRE 632
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRL---LRNIERTMKLTIPEvelpnaELLGKrrLEKFAAKvQQQLE 396
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
253-448 1.67e-72

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: 232.31  E-value: 1.67e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrPGMLVLTPTRELALQV 332
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEG-PIAVIVAPTRELAQQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 411
Cdd:cd17952   80 YLEAKKFGkAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 412 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
253-449 9.73e-71

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: 228.36  E-value: 9.73e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSL--KGQRNRPGMLVLTPTRELAL 330
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLdeETKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 409
Cdd:cd17945   81 QIEEETQKFaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 410 IMKIL--LDV---RPD---------------RQTVMTSATWPHSVHRLAQSYLKEPMIVY 449
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 ...
236-444 1.46e-68

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: 1.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 236 IPNPTCTFDDAfQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMP---GFIHLVLQPSLKG 312
Cdd:cd18052   38 PPPAILTFEEA-NLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMKEGLTASSFS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 313 QRNRPGMLVLTPTRELALQVEGECCKYSYK-GLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNIT 391
Cdd:cd18052  117 EVQEPQALIVAPTRELANQIFLEARKFSYGtCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLK 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149 392 YLVLDEADKMLDMGFEPQIMKILLDV----RPDRQTVMTSATWPHSVHRLAQSYLKE 444
Cdd:cd18052  197 YLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
PTZ00424 PTZ00424
helicase 45; Provisional
241-622 1.18e-63

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 215.85  E-value: 1.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 241 CTFDDAFQCYP------EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFihLVLQPSLkgqr 314
Cdd:PTZ00424  21 SNYDEIVDSFDalklneDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL--QLIDYDL---- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 315 NRPGMLVLTPTRELALQVE------GECCKYSYKGlrsvCVYGGGNRDEqIEELKKGVDIIIATPGRLNDLQMSNFVNLK 388
Cdd:PTZ00424  95 NACQALILAPTRELAQQIQkvvlalGDYLKVRCHA----CVGGTVVRDD-INKLKAGVHMVVGTPGRVYDMIDKRHLRVD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 389 NITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTlDLVAVSSVKQ-NIIV 467
Cdd:PTZ00424 170 DLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK-DELTLEGIRQfYVAV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 468 TTEEEKWSHMQTFLQSMSSTDKVIVFVSRKAVaDHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLA 547
Cdd:PTZ00424 249 EKEEWKFDTLCDLYETLTITQAIIYCNTRRKV-DYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLL 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222352149 548 SRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDwrvASELINILERANQSIPEELVSMAE 622
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 ...
236-451 1.33e-58

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: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 236 IPNPTCTFDDAfQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHL------VLQPS 309
Cdd:cd18051   16 CPPHIETFSDL-DLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 310 LKGQRNR----PGMLVLTPTRELALQVEGECCKYSYKGLRSVCV-YGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNF 384
Cdd:cd18051   95 ESGYYGRrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVvYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149 385 VNLKNITYLVLDEADKMLDMGFEPQIMKILL-DVRP---DRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 451
Cdd:cd18051  175 IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
461-589 2.48e-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: 189.64  E-value: 2.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 461 VKQNIIVTTEEEKWSHMQTFLQSMSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRI 540
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 222352149 541 LIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 589
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAIT 129
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
266-437 6.58e-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: 189.76  E-value: 6.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  266 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpslKGQRNRPGMLVLTPTRELALQVEGECCKY-SYKGL 344
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL------DKLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  345 RSVCVYGGGNRDEQIEELKkGVDIIIATPGRLNDLqMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTV 424
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 222352149  425 MTSATWPHSVHRL 437
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
247-448 1.47e-53

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: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 247 FQCY---PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNrpgmLVLT 323
Cdd:cd17959    3 FQSMglsPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARA----LILS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 324 PTRELALQ---VEGECCKYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADK 400
Cdd:cd17959   79 PTRELALQtlkVTKELGKFT--DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 222352149 401 MLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
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 ...
242-445 3.69e-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: 3.69e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDAFQCyPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQpSLKGQRNRPGMLV 321
Cdd:cd17954    1 TFKELGVC-EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALP-----ILQ-ALLENPQRFFALV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 322 LTPTRELALQVEGECCKY-SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEAD 399
Cdd:cd17954   74 LAPTRELAQQISEQFEALgSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEAD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 222352149 400 KMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 445
Cdd:cd17954  154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
253-451 4.15e-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: 178.17  E-value: 4.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRnrpgMLVLTPTRELALQV 332
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLR----ALILAPTRELASQI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGECCKYSY-KGLRsVCVYGGGNRD--EQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 409
Cdd:cd17957   77 YRELLKLSKgTGLR-IVLLSKSLEAkaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 222352149 410 IMKILLDVR-PDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVG 451
Cdd:cd17957  156 TDEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
251-444 6.30e-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: 178.16  E-value: 6.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQ-GIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRPGMLVLTPTRELA 329
Cdd:cd17964    3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKP-AGRRSGVSALIISPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCK--YSYKGLRSVCVYGGGNRDEQIEELKK-GVDIIIATPGRLNDLQMSNFV--NLKNITYLVLDEADKMLDM 404
Cdd:cd17964   82 LQIAAEAKKllQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDM 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 222352149 405 GFEPQIMKILLDVRP----DRQTVMTSATWPHSVHRLAQSYLKE 444
Cdd:cd17964  162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEXDc smart00487
DEAD-like helicases superfamily;
257-455 1.79e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 176.53  E-value: 1.79e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149   257 IKKAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKGqrnrpgmLVLTPTRELALQVEGE 335
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRV-------LVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149   336 CCKY-SYKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKI 413
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 222352149   414 LLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYVGTLDL 455
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
253-448 1.66e-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: 171.37  E-value: 1.66e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQ----PSLKGQRnrPGMLVLTPTREL 328
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFIKGEG--PYGLIVCPSREL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 329 ALQVEGECCKYS-------YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKM 401
Cdd:cd17951   79 ARQTHEVIEYYCkalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 222352149 402 LDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
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 ...
254-451 4.34e-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: 169.85  E-value: 4.34e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 254 MENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGfIHLVLQPSLKgQRNRPGMLVLTPTRELALQVE 333
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPA-IELLYKLKFK-PRNGTGVIIISPTRELALQIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 334 G---ECCKYSYKGLRsvCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 409
Cdd:cd17942   80 GvakELLKYHSQTFG--IVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 222352149 410 IMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIvYVG 451
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 ...
256-448 1.20e-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: 168.50  E-value: 1.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 256 NIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkGQRNRPGMLVLTPTRELALQVEGE 335
Cdd:cd17962    4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL------TEHRNPSALILTPTRELAVQIEDQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 336 CcKYSYKGL---RSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMK 412
Cdd:cd17962   78 A-KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 222352149 413 ILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17962  157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
258-448 1.23e-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: 166.61  E-value: 1.23e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 258 KKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNR-PGMLVLTPTRELALQVEgEC 336
Cdd:cd17949    7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLP-IIQRLLSLEPRVDRSDgTLALVLVPTRELALQIY-EV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 337 CKysyKGLRSV------CVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQ 409
Cdd:cd17949   85 LE---KLLKPFhwivpgYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222352149 410 IMKIL--LDVRPD-----------RQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17949  162 ITKILelLDDKRSkaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
261-445 1.94e-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: 162.81  E-value: 1.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 261 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRpgMLVLTPTRELALQVEG---ECC 337
Cdd:cd17947    9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPK-KKAATR--VLVLVPTRELAMQCFSvlqQLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 338 KYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 416
Cdd:cd17947   86 QFT--DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDhLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
                        170       180
                 ....*....|....*....|....*....
gi 222352149 417 VRPDRQTVMTSATWPHSVHRLAQSYLKEP 445
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 ...
243-445 2.66e-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: 162.47  E-value: 2.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 243 FDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQ---PSLKGQRnrpgM 319
Cdd:cd17940    1 FED-YGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP-----ILEkidPKKDVIQ----A 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 320 LVLTPTRELALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA 398
Cdd:cd17940   71 LILVPTRELALQTSQVCKELGkHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 222352149 399 DKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 445
Cdd:cd17940  151 DKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
253-445 3.22e-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: 159.66  E-value: 3.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNRPGMLVLTPTRELALQV 332
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIP-VLEILLKRKANLKKGQVGALIISPTRELATQI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 EGEC---CKYSYKGLRSVCVYGGGNRDEQIEELK-KGVDIIIATPGRLNDL--QMSNFVNLKNITYLVLDEADKMLDMGF 406
Cdd:cd17960   80 YEVLqsfLEHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGF 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 222352149 407 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 445
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 ...
257-450 1.85e-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: 1.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 257 IKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkgqRNR------PGMLVLTPTRELAL 330
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY--------RERwtpedgLGALIISPTRELAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGECCKYSYKGLRSVCVYGGGnRDEQIEELK-KGVDIIIATPGRLndLQ-MSNFVNL--KNITYLVLDEADKMLDMGF 406
Cdd:cd17941   77 QIFEVLRKVGKYHSFSAGLIIGG-KDVKEEKERiNRMNILVCTPGRL--LQhMDETPGFdtSNLQMLVLDEADRILDMGF 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 222352149 407 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYV 450
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, ...
253-448 4.56e-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: 145.10  E-value: 4.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELALQV 332
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLV-----FVVIALE-SLDLERRHPQVLILAPTREIAVQI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 333 E---GECCKYsYKGLRsVCVY-GGGNRDEQIEELkKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEP 408
Cdd:cd17943   75 HdvfKKIGKK-LEGLK-CEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQK 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 222352149 409 QIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17943  152 DVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
261-448 2.25e-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: 143.62  E-value: 2.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 261 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELALQVEgECCKY- 339
Cdd:cd17939   16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTAT-----FSIGALQ-RIDTTVRETQALVLAPTRELAQQIQ-KVVKAl 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 340 -SYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVR 418
Cdd:cd17939   89 gDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLP 168
                        170       180       190
                 ....*....|....*....|....*....|
gi 222352149 419 PDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd17939  169 PETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
255-446 2.44e-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: 2.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 255 ENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQ-----PSlkgqrnrpGM--LVLTPTRE 327
Cdd:cd17955   12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-----ILQrlsedPY--------GIfaLVLTPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 328 LALQ------VEGECCkysykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSN---FVNLKNITYLVLDEA 398
Cdd:cd17955   79 LAYQiaeqfrALGAPL-----GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 222352149 399 DKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPM 446
Cdd:cd17955  154 DRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
253-429 7.15e-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: 143.15  E-value: 7.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLCYLMP---GFIHLVLQPSLKGQRNRPGMLVLTPTREL 328
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPileRLLSQKSSNGVGGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 329 ALQVEG---ECCKYSykGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDL-QMSN--FVNLKNITYLVLDEADKML 402
Cdd:cd17946   81 AVQVKDhlkAIAKYT--NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiQEGNehLANLKSLRFLVLDEADRML 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 222352149 403 DMG-FEP--QIMKILLDVRP----DRQTVMTSAT 429
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 ...
254-443 2.62e-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: 137.67  E-value: 2.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 254 MENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGF--IHLVLQPSLKGQRnrPGMLVLTPTRELALQ 331
Cdd:cd17944    2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPRKRGRA--PKVLVLAPTRELANQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 332 VEGECCKYSYKgLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 411
Cdd:cd17944   80 VTKDFKDITRK-LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 412 KIL-----LDVRPDRQTVMTSATWPHSVHRLAQSYLK 443
Cdd:cd17944  159 EILsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
251-448 7.98e-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: 136.17  E-value: 7.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGID--LIGVAQTGTGKTLCYLMpGFIHLVlQPSLKgqrnRPGMLVLTPTREL 328
Cdd:cd17963    3 PELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVL-AMLSRV-DPTLK----SPQALCLAPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 329 ALQVEGECCKY-SYKGLRSVCVYGGG--NRDEQIEElkkgvDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDM- 404
Cdd:cd17963   77 ARQIGEVVEKMgKFTGVKVALAVPGNdvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTq 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 222352149 405 GFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
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 ...
257-448 7.59e-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: 7.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 257 IKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSLKGQRNR-PGMLVLTPTRELALQVEG- 334
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP-IIQKILKAKAESGEEQgTRALILVPTRELAQQVSKv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 335 --ECCKYSYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLND-LQMSNFVNLKNITYLVLDEADKMLDMGFEPQIM 411
Cdd:cd17961   88 leQLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLK 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 222352149 412 KILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
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 ...
251-450 3.94e-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: 132.08  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQpSLKGQRNRPGMLVLTPTRELAL 330
Cdd:cd17950   11 PELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAV-----FVLSTLQ-QLEPVDGQVSVLVICHTRELAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGECCKYS--YKGLRSVCVYGGGNRDEQIEELKKGV-DIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKML-DMGF 406
Cdd:cd17950   85 QISNEYERFSkyMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDM 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 222352149 407 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIVYV 450
Cdd:cd17950  165 RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
245-445 1.14e-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: 127.56  E-value: 1.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 245 DAFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCylmpgFIHLVLQ---PSLKGqrnrPGMLV 321
Cdd:cd18046    2 DDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTAT-----FSISILQqidTSLKA----TQALV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 322 LTPTRELALQVE------GEcckysYKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVL 395
Cdd:cd18046   73 LAPTRELAQQIQkvvmalGD-----YMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVL 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 222352149 396 DEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEP 445
Cdd:cd18046  148 DEADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
253-434 1.41e-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: 1.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQPSL--KGQRNRPGMLVLTPTRELAL 330
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQRLLRYKLlaEGPFNAPRGLVITPSRELAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGECCKYS-YKGLRSVCVyGGGN-----RDEQIEElkkgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDM 404
Cdd:cd17948   80 QIGSVAQSLTeGLGLKVKVI-TGGRtkrqiRNPHFEE----VDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 222352149 405 GFEPQIMKIL----LDVRPDR---------QTVMTSATWPHSV 434
Cdd:cd17948  155 SFNEKLSHFLrrfpLASRRSEntdgldpgtQLVLVSATMPSGV 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
472-582 1.45e-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: 121.16  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  472 EKWSHMQTFLQSmSSTDKVIVFVSRKavaDHLSSDLIL--GNISVESLHGDREQRDREKALENFKTGKVRILIATDLASR 549
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSQTK---KTLEAELLLekEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 222352149  550 GLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAG 582
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 ...
251-448 9.86e-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: 9.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgFIHLVLQpslkgqrnrpgmLVLTPTRELAL 330
Cdd:cd17938    8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQIVVA------------LILEPSRELAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 QVEGECCKYSY----KGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGF 406
Cdd:cd17938   75 QTYNCIENFKKyldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGN 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 222352149 407 EPQIMKIL-----LDVRPDR-QTVMTSATWpHS--VHRLAQSYLKEPMIV 448
Cdd:cd17938  155 LETINRIYnripkITSDGKRlQVIVCSATL-HSfeVKKLADKIMHFPTWV 203
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
252-448 7.07e-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: 119.88  E-value: 7.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 252 EVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKT----LCYLMpgfihlVLQPSLKgqrnRPGMLVLTPTRE 327
Cdd:cd18045    9 DLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTatfsISVLQ------CLDIQVR----ETQALILSPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 328 LALQVEGECCKYS-YKGLRSVCVYGGGNRDEQIEELKKGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGF 406
Cdd:cd18045   79 LAVQIQKVLLALGdYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 222352149 407 EPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
HELICc smart00490
helicase superfamily c-terminal domain;
501-582 2.83e-28

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 108.07  E-value: 2.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149   501 DHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGR 580
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 222352149   581 AG 582
Cdd:smart00490  81 AG 82
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
253-430 3.78e-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: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 253 VMENIKKAGFQKPTPIQSQAWPIVLQGI---------DLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRPGMLVLT 323
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLP-----IVQALSKRVVPRLRALIVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 324 PTRELALQVEGECCKYSYKGLRSVCVYGGGN--RDEQIE-------ELKKGVDIIIATPGRLND-LQMSNFVNLKNITYL 393
Cdd:cd17956   76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKsfKKEQKLllvdtsgRYLSRVDILVATPGRLVDhLNSTPGFTLKHLRFL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 222352149 394 VLDEADKMLDMGFE---PQIMKILLDVRPDRQTVMTSATW 430
Cdd:cd17956  156 VIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDANL 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 1.40e-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: 105.44  E-value: 1.40e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149  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 ...
245-433 2.08e-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: 97.06  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 245 DAFQCYPEVMENIKKA---------GFQKPTPIQSQAWPIVLQG-----------------IDLIGvAQTGTGKTLCYLM 298
Cdd:cd17965    2 DQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepkleVFLLA-AETGSGKTLAYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 299 PGFIHL---------VLQPSLKGQRN--RPGMLVLTPTRELALQVeGECCK----YSYKGLRSVCVYGGGNRDEQIEELK 363
Cdd:cd17965   81 PLLDYLkrqeqepfeEAEEEYESAKDtgRPRSVILVPTHELVEQV-YSVLKklshTVKLGIKTFSSGFGPSYQRLQLAFK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 364 KGVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTVMTSATWPHS 433
Cdd:cd17965  160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
285-577 5.78e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 90.85  E-value: 5.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 285 VAQTGTGKTLCylmpgFIHLVLQpSLKGQRnrpgMLVLTPTRELALQVEGECCKYSYKGLRsvcvyGGGNRDEqieelkk 364
Cdd:COG1061  106 VAPTGTGKTVL-----ALALAAE-LLRGKR----VLVLVPRRELLEQWAEELRRFLGDPLA-----GGGKKDS------- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 365 GVDIIIATPGRL-NDLQMSNFVNlkNITYLVLDEA--------DKMLDMgFEPqimKILLDV-----RPDRQTvMTSATW 430
Cdd:COG1061  164 DAPITVATYQSLaRRAHLDELGD--RFGLVIIDEAhhagapsyRRILEA-FPA---AYRLGLtatpfRSDGRE-ILLFLF 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 431 PHSVHR------LAQSYLKEPMIVYVGT------LDLVAVSSVKQNIIVTTEEEKWSHMQTFLQSMSSTDKVIVFVSRKA 498
Cdd:COG1061  237 DGIVYEyslkeaIEDGYLAPPEYYGIRVdltderAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVD 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 499 VADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYnfdFPRNIE---EYVHRI 575
Cdd:COG1061  317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGsprEFIQRL 393

                 ..
gi 222352149 576 GR 577
Cdd:COG1061  394 GR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
252-448 1.65e-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: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 252 EVMENIKKAGFQKPTPIQSQAWPIVLQGI--DLIGVAQTGTGKTLCYLmpgfihLVLQPSLKGQRNRPGMLVLTPTRELA 329
Cdd:cd18048   28 ELLRGIYAMGFNRPSKIQENALPMMLADPpqNLIAQSQSGTGKTAAFV------LAMLSRVDALKLYPQCLCLSPTFELA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQ----VE--GECCK-----YSYKGLRSvcvyGGGNRDEQieelkkgvDIIIATPGRLNDLQMS-NFVNLKNITYLVLDE 397
Cdd:cd18048  102 LQtgkvVEemGKFCVgiqviYAIRGNRP----GKGTDIEA--------QIVIGTPGTVLDWCFKlRLIDVTNISVFVLDE 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222352149 398 ADKMLDM-GFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd18048  170 ADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
285-429 1.36e-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: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 285 VAQTGTGKTLCYLMPGFIHLVLQpslkgqrnRPGMLVLTPTRELALQVEGECCKYSYKGLRsVCVYGGGNRDEQIEELKK 364
Cdd:cd00046    7 TAPTGSGKTLAALLAALLLLLKK--------GKKVLVLVPTKALALQTAERLRELFGPGIR-VAVLVGGSSAEEREKNKL 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149 365 G-VDIIIATPGRL-NDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD--VRPDRQTVMTSAT 429
Cdd:cd00046   78 GdADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
276-633 1.49e-16

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 82.88  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 276 VLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTreLAL---QVEG--EcckysyKGLRSVCV 349
Cdd:COG0514   29 VLAGRDALVVMPTGGGKSLCYQLPALL-------------LPGLtLVVSPL--IALmkdQVDAlrA------AGIRAAFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 350 YGGGNRDEQ---IEELKKG-VDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA--------DkmldmgFEPQIMKI--LL 415
Cdd:COG0514   88 NSSLSAEERrevLRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD------FRPDYRRLgeLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 416 DVRPDRQTVMTSATWPHSVHR--LAQSYLKEPMiVYVGTLDlvavssvKQNI----IVTTEEEKWSHMQTFLQSMSStDK 489
Cdd:COG0514  162 ERLPNVPVLALTATATPRVRAdiAEQLGLEDPR-VFVGSFD-------RPNLrlevVPKPPDDKLAQLLDFLKEHPG-GS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 490 VIVFV-SRKAV---ADHLSSDlilgNISVESLHGDREQRDREKALENFKTGKVRILIATdlaSR---GLDVHDVTHVYNF 562
Cdd:COG0514  233 GIVYClSRKKVeelAEWLREA----GIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT---IAfgmGIDKPDVRFVIHY 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149 563 DFPRNIEEYVHRIGRTGRAGRTGVSITTLTRNDWRVASELInileraNQSIPEELVSMAERfkahQQKREM 633
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 ...
242-448 3.80e-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: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 242 TFDDaFQCYPEVMENIKKAGFQKPTPIQSQAWPIVLQG--IDLIGVAQTGTGKTLCYLMPGFIHlvLQPSLKGQRnrpgM 319
Cdd:cd18047    2 SFEE-LRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQ--VEPANKYPQ----C 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 320 LVLTPTRELALQVeGECCKYSYKGLRSVCVYGG--GNRDEQIEELKKgvDIIIATPGRLNDLQMS-NFVNLKNITYLVLD 396
Cdd:cd18047   75 LCLSPTYELALQT-GKVIEQMGKFYPELKLAYAvrGNKLERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222352149 397 EADKML-DMGFEPQIMKILLDVRPDRQTVMTSATWPHSVHRLAQSYLKEPMIV 448
Cdd:cd18047  152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
261-585 1.01e-13

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 74.36  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 261 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTRELAL-QVEgeccK 338
Cdd:PRK11057  22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV-------------LDGLtLVVSPLISLMKdQVD----Q 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 339 YSYKGLRSVCVYGGGNRDEQIE---ELKKG-VDIIIATPGRLndlQMSNFV-NLK--NITYLVLDEADKMLDMG--FEP- 408
Cdd:PRK11057  85 LLANGVAAACLNSTQTREQQLEvmaGCRTGqIKLLYIAPERL---MMDNFLeHLAhwNPALLAVDEAHCISQWGhdFRPe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 -----QIMKILLDVRPDRQTVMTSATWPHSVHRLAQsyLKEPMIvYVGTLDlvavssvKQNIIVTTEEE--KWSHMQTFL 481
Cdd:PRK11057 162 yaalgQLRQRFPTLPFMALTATADDTTRQDIVRLLG--LNDPLI-QISSFD-------RPNIRYTLVEKfkPLDQLMRYV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 482 QSMSSTDKVIVFVSRKAVADhLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYN 561
Cdd:PRK11057 232 QEQRGKSGIIYCNSRAKVED-TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVH 310
                        330       340
                 ....*....|....*....|....
gi 222352149 562 FDFPRNIEEYVHrigRTGRAGRTG 585
Cdd:PRK11057 311 FDIPRNIESYYQ---ETGRAGRDG 331
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
491-581 2.20e-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: 64.92  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 491 IVFVSRKAVA--------------DHLSSDLILG-NISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHD 555
Cdd:cd18802   29 IIFVERRATAvvlsrllkehpstlAFIRCGFLIGrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                         90       100
                 ....*....|....*....|....*.
gi 222352149 556 VTHVYNFDFPRNIEEYVHRIGRtGRA 581
Cdd:cd18802  109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
485-576 1.93e-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: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 485 SSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGK--VRILIATDLASRGLDVHDVTHVYNF 562
Cdd:cd18793   25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILY 104
                         90       100
                 ....*....|....*....|
gi 222352149 563 DFPRN--IEEY----VHRIG 576
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 1.19e-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: 1.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 222352149   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 2.77e-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: 2.77e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149  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 ...
491-589 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: 56.83  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 491 IVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHVYNFDFPRNIEE 570
Cdd:cd18794   34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
                         90
                 ....*....|....*....
gi 222352149 571 YVHRIGRTGRAGRTGVSIT 589
Cdd:cd18794  114 YYQESGRAGRDGLPSECIL 132
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
540-592 1.37e-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: 55.02  E-value: 1.37e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222352149 540 ILIATDLASRGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGRAGRTGVSITTLT 592
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
251-619 1.41e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 61.06  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLCYLMpGFIHLVLQpSLKGqrnrpgmLVLTPTRELA 329
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAEL-AILKALLN-GGKA-------LYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 330 LQVEGECCK-YSYKGLRSVCVYGggNRDEQIEELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEAdKMLDmgfEP 408
Cdd:COG1204   80 SEKYREFKRdFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID---DE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 409 Q-------IMKILLDVRPDRQTVMTSATWPhSVHRLAQsylkepmivyvgTLDLVAVSS-----------VKQNIIVTTE 470
Cdd:COG1204  153 SrgptlevLLARLRRLNPEAQIVALSATIG-NAEEIAE------------WLDAELVKSdwrpvplnegvLYDGVLRFDD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 471 EEKWSHMQTF---LQSMSSTDKVIVFVSR--------KAVADHLSSDLILGNIS----------------------VESL 517
Cdd:COG1204  220 GSRRSKDPTLalaLDLLEEGGQVLVFVSSrrdaeslaKKLADELKRRLTPEEREeleelaeellevseethtneklADCL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 518 -------HGDREQRDREKALENFKTGKVRILIATD-------LASRGLDVHDVTHVYNFDFPrnIEEYVHRIGRTGRAGR 583
Cdd:COG1204  300 ekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGY 377
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 222352149 584 --TGVSIttLTRNDWRVASELINILERANqsiPEELVS 619
Cdd:COG1204  378 dpYGEAI--LVAKSSDEADELFERYILGE---PEPIRS 410
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
488-593 2.46e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.51  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 488 DKVIVFVSRKAVADHLSSDLILGNISVESLHG--DRE------QRDREKALENFKTGKVRILIATDLASRGLDVHDVTHV 559
Cdd:COG1111  354 SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLV 433
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 222352149 560 YNFD-FPRNIeEYVHRIGRTGR--AGRTGVSITTLTR 593
Cdd:COG1111  434 IFYEpVPSEI-RSIQRKGRTGRkrEGRVVVLIAKGTR 469
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
251-589 2.96e-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: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 251 PEVMENIKKAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPgfihlVLQPSLKGQRNRpgMLVLTPTRELAL 330
Cdd:COG1205   43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLP-----VLEALLEDPGAT--ALYLYPTKALAR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 -QVEgECCKYSYKGLR--SVCVYGGGNRDEQIEELKKGVDIIIATPGRLNdLQM-------SNFvnLKNITYLVLDEA-- 398
Cdd:COG1205  116 dQLR-RLRELAEALGLgvRVATYDGDTPPEERRWIREHPDIVLTNPDMLH-YGLlphhtrwARF--FRNLRYVVIDEAht 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 399 -------------DKML----DMGFEPQImkilldvrpdrqtVMTSATWPHSVhRLAQSYLKEPMIVyV-------GTLD 454
Cdd:COG1205  192 yrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIGNPA-EHAERLTGRPVTV-VdedgsprGERT 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 455 LVAVSSVkqniIVTTEEEKWSHMQT---FLQSMSSTDKVIVFV-SRKAV---ADHLSSDLI--LGNISVESLHGDREQRD 525
Cdd:COG1205  257 FVLWNPP----LVDDGIRRSALAEAarlLADLVREGLRTLVFTrSRRGAellARYARRALRepDLADRVAAYRAGYLPEE 332
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222352149 526 ReKALEN-FKTGKVRILIAT-------DLAsrGLDVhdvthVYNFDFPRNIEEYVHRIGRTGRAGRTGVSIT 589
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 3.28e-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: 53.46  E-value: 3.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES---LVKIFGSKAMQTKAKAVID 129
Cdd:cd00105    3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSgerVVTITGTPEAVEKAKELIE 63
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
473-578 5.26e-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: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 473 KWSHMQTFLQS-MSSTDKVIVFVSRKAVADHLSSDLILGNISVESLHGDREQRDREKALENFKTGK--VRILIATDLASR 549
Cdd:COG0553  534 KLEALLELLEElLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 222352149 550 GLDVHDVTHVYNFDFPRN--IEEY----VHRIGRT 578
Cdd:COG0553  614 GLNLTAADHVIHYDLWWNpaVEEQaidrAHRIGQT 648
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
79-136 9.56e-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: 9.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149  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 ...
255-454 3.74e-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: 54.08  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 255 ENIKKAGFQKPTPIQSQAwpI--VLQGIDLIGVAQTGTGKTLCYLMPGFIhlvlqpslkgqrnRPGM-LVLTPTreLAL- 330
Cdd:cd17920    3 ILKEVFGYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALL-------------LDGVtLVVSPL--ISLm 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 331 --QVEgECCKysyKGLRSVCVYGGGNRDEQ---IEELKKG-VDIIIATPGRLNDLQMSNFVN----LKNITYLVLDEADK 400
Cdd:cd17920   66 qdQVD-RLQQ---LGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHC 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149 401 MLDMG--FEPQIMKI--LLDVRPDRQTVMTSATWPHSVHRLAQSYLK-EPMIVYVGTLD 454
Cdd:cd17920  142 VSQWGhdFRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRASFD 200
KH smart00322
K homology RNA-binding domain;
72-128 1.37e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.83  E-value: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 222352149    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 1.48e-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: 46.09  E-value: 1.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222352149  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 1.97e-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: 45.70  E-value: 1.97e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 222352149  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) ...
261-434 2.99e-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: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 261 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSLKgqrnrpgmLVLTPTreLAL---QVEGecc 337
Cdd:cd18018    9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGLT--------LVVSPL--IALmkdQVDA--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 338 kySYKGLRSVCvYGGGNRDEQ----IEELKKG-VDIIIATPGRLNDLQMSNFV-NLKNITYLVLDEADKMLDMG--FEP- 408
Cdd:cd18018   76 --LPRAIKAAA-LNSSLTREErrriLEKLRAGeVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWShnFRPd 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 222352149 409 -----QIMKILLDVRPdrqTVMTSATWPHSV 434
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 3.09e-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: 3.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222352149  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES-LVKIFGSKAMQTKAKAVI 128
Cdd:cd22411   10 FHKNIIGKGGATIKKIREETNTRIDLPEENSDSdVITITGKKEDVEKARERI 61
PRK13766 PRK13766
Hef nuclease; Provisional
489-593 3.58e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 50.26  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 489 KVIVFV-SR---KAVADHLSSDlilgNISVESLHG--DRE------QRDREKALENFKTGKVRILIATDLASRGLDVHDV 556
Cdd:PRK13766 367 RIIVFTqYRdtaEKIVDLLEKE----GIKAVRFVGqaSKDgdkgmsQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSV 442
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 222352149 557 THVYnFDFP-----RNIEeyvhRIGRTGR--AGRTGVSITTLTR 593
Cdd:PRK13766 443 DLVI-FYEPvpseiRSIQ----RKGRTGRqeEGRVVVLIAKGTR 481
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
266-398 3.87e-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: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 266 TPIQSQAW-PIVLQGIDLIGVAQTGTGKTLCYLmpgfihLVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKySYKGL 344
Cdd:cd17921    3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAE------LAILRALATSGGK--AVYIAPTRALVNQKEADLRE-RFGPL 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149 345 RSVCVYGGGNRDEQIEELKKGvDIIIATPGRLnDLQMSNF--VNLKNITYLVLDEA 398
Cdd:cd17921   74 GKNVGLLTGDPSVNKLLLAEA-DILVATPEKL-DLLLRNGgeRLIQDVRLVVVDEA 127
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
487-583 4.27e-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: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 487 TDKVIVFVSRKAVADHLSSDLILgnisvESLHGDREQRDREKALENFKTGKVRILIATDLASRGLDVHDVTHV----YNF 562
Cdd:cd18789   49 GDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAiqisGHG 123
                         90       100
                 ....*....|....*....|.
gi 222352149 563 DFPRnieEYVHRIGRTGRAGR 583
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 4.92e-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: 44.52  E-value: 4.92e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149  78 FVGAVIGRGGSKIKNIQSTTNTTIQI---IQEQP---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 ...
483-585 6.39e-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: 6.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 483 SMSSTDKVIVFV----SRKAVADHLSSD-------LILGNISVESLHGdREQRDREKALENFKTGKVRILIATDLASRGL 551
Cdd:cd18801   26 QEGSDTRVIIFSefrdSAEEIVNFLSKIrpgiratRFIGQASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGL 104
                         90       100       110
                 ....*....|....*....|....*....|....
gi 222352149 552 DVHDVTHVYNFDFPRNIEEYVHRIGRTGRaGRTG 585
Cdd:cd18801  105 DIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
450-580 8.04e-06

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: 46.10  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 450 VGTLDLVAVSSVkQNIIVTTEEEKWSHM-QTFLQSMSSTDKVIVFV-SRKA---VADHLSSdlILGNISVESL----HG- 519
Cdd:cd18796    1 KKKLDIKVILPV-APEIFPWAGESGADAyAEVIFLLERHKSTLVFTnTRSQaerLAQRLRE--LCPDRVPPDFialhHGs 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149 520 -DREQRDR-EKALenfKTGKVRILIAT---DLasrGLDVHDVTHVYNFDFPRNIEEYVHRIGRTGR 580
Cdd:cd18796   78 lSRELREEvEAAL---KRGDLKVVVATsslEL---GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
276-429 8.19e-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: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 276 VLQGIDLIGVAQTGTGKTLCYLMPGFIHLvlqpsLKGQRnrpgMLVLTPTRELALQVEGECCKYSYKGLRsvCVYGGGNR 355
Cdd:cd18028   14 LLKGENLLISIPTASGKTLIAEMAMVNTL-----LEGGK----ALYLVPLRALASEKYEEFKKLEEIGLK--VGISTGDY 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149 356 DEQIEELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQ---IMKILLDVRPDRQTVMTSAT 429
Cdd:cd18028   83 DEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTlesIVARLRRLNPNTQIIGLSAT 158
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
79-110 1.18e-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: 1.18e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 222352149  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES 110
Cdd:cd22398   11 VGVVIGKGGEMIKKIQNETGARVQFKPDDGNS 42
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
283-398 1.28e-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: 46.49  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 283 IGVAQTGTGKTL--CYLMPGFIHLVLQPSLKGQRnrpgMLVLTPTRELALQVegecCKY--SYKGLRSVCVYGGGNRDEQ 358
Cdd:cd18034   20 IVVLPTGSGKTLiaVMLIKEMGELNRKEKNPKKR----AVFLVPTVPLVAQQ----AEAirSHTDLKVGEYSGEMGVDKW 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 222352149 359 I-----EELKKgVDIIIATPGRLNDLQMSNFVNLKNITYLVLDEA 398
Cdd:cd18034   92 TkerwkEELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
79-137 1.98e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 47.74  E-value: 1.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149  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 ...
264-416 2.12e-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: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 264 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMpgfihlVLQPSLKGQRNRPG--MLVLTPTRELALQVEGECCKYSY 341
Cdd:cd17927    2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVL------ICEHHLKKFPAGRKgkVVFLANKVPLVEQQKEVFRKHFE 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149 342 KGLRSVCVYGGGNRDE-QIEELKKGVDIIIATPGRL-NDLQMSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 416
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 2.99e-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: 42.24  E-value: 2.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149  77 HFVGAVIGRGGSKIKNIQSTTNTTIQII---QEQPESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22462    8 HAVGSVIGRGGSNINQIREISGAKVEVLkpdSATGERIVLISGTPDQARHAQNLIEAFI 66
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
262-329 8.96e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.86  E-value: 8.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149 262 FQKPTPIQSQAWPIVLQGID-LIgVAQTGTGKTLCYLMPGFIHLVLQPSLKGQRNRPGMLVLTPTRELA 329
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 1.08e-04

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: 40.69  E-value: 1.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149  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 ...
269-398 1.35e-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: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 269 QSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVlqpslkgQRNRPGMLVLTPTRELALQVEGECCKYSYKGLRSVC 348
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-------RDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIR 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222352149 349 V--YGGgnrDEQIEE----LKKGVDIIIATPGRLN-------DLQMSNFVNLKnitYLVLDEA 398
Cdd:cd17923   78 VatYDG---DTPREErraiIRNPPRILLTNPDMLHyallphhDRWARFLRNLR---YVVLDEA 134
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
393-583 2.48e-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: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 393 LVLDEADKMLD--MGFEPQIMKILLDVrpDRQTVMTSATWPHSVHRLAQSYLkepMIVYVGTLDLVAVSSVKQNIIVTTE 470
Cdd:cd09639  127 LIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEKIG---YVEENEPLDLKPNERAPFIKIESDK 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 471 EEKWSHMQTFLQSMSSTDKVIVFVS--RKAVAdhlSSDLILGNISVES---LHGDREQRDREKA----LENFKTGKVRIL 541
Cdd:cd09639  202 VGEISSLERLLEFIKKGGSVAIIVNtvDRAQE---FYQQLKEKGPEEEimlIHSRFTEKDRAKKeaelLLEFKKSEKFVI 278
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 222352149 542 IATDLASRGLDVhdvthvyNFDF----PRNIEEYVHRIGRTGRAGR 583
Cdd:cd09639  279 VATQVIEASLDI-------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 2.76e-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: 39.56  E-value: 2.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222352149  69 PLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ----PESLVKIFGS 117
Cdd:cd22400    1 PLRILVPSEFVGAIIGKGGATIRQITQQTGARIDIHRKEnagaAEKAITIYGT 53
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
72-118 3.82e-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: 3.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 222352149  72 FALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ---PESLVKIFGSK 118
Cdd:cd22439    6 ITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEdgsTERSVTITGTP 55
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
78-134 4.32e-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: 4.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149  78 FVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFVKK 134
Cdd:cd22449   14 YVPHIIGKKGANINKLREEYGVKIDFEDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_IGF2BP3_rpt2 cd22495
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
69-142 4.70e-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: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  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 ...
258-402 4.91e-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: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 258 KKAGFqKPTPIQsQAWPI-VLQGIDLIGVAQTGTGKTLCYLMpgfIHLVLqpSLKGQRnrpgMLVLTPTRELALQVEGEC 336
Cdd:cd17924   12 KKTGF-PPWGAQ-RTWAKrLLRGKSFAIIAPTGVGKTTFGLA---TSLYL--ASKGKR----SYLIFPTKSLVKQAYERL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222352149 337 CKYSYKGLRSV--CVYGGGNRDEQIEELKKGV-----DIIIATPGRLNDlqmsNFVNLKNITY--LVLDEADKML 402
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 5.53e-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: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  66 EELPLCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQ------PESLVKIFGSKAMQTKAKAVIdnfVKKLEENY 139
Cdd:cd22493    3 DEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISPLQdltlynPERTITVKGSIEACCRAEQEI---MKKVREAY 79

                 ...
gi 222352149 140 NSE 142
Cdd:cd22493   80 END 82
PRK05580 PRK05580
primosome assembly protein PriA; Validated
527-585 8.69e-04

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 42.45  E-value: 8.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222352149 527 EKALENFKTGKVRILIATDLASRGLDVHDVTHV---------YNFDFpRNIEE----YVHRIGRTGRAGRTG 585
Cdd:PRK05580 470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTLVgvldadlglFSPDF-RASERtfqlLTQVAGRAGRAEKPG 540
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
79-117 1.27e-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: 1.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 222352149  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQE-QPES---LVKIFGS 117
Cdd:cd22433   13 AGCIIGRAGFKIKELREKTGATIKVYSEcCPRStdrVVQIGGK 55
KH-I_FUBP1_rpt1 cd22478
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
79-134 1.35e-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: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149  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 ...
264-416 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 264 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLCYLMPGFIHLVLQPSlKGQRNRPGMLVltPTRELALQVEGECCKYSYKG 343
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRS-AGEKGRVVVLV--NKVPLVEQQLEKFFKYFRKG 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149 344 LRSVCVYGGGNRDEQIEELKKGVDIIIATPGRL-NDLQ---MSNFVNLKNITYLVLDEADKMLDMGFEPQIMKILLD 416
Cdd:cd18036   79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILiNNLLsgrEEERVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLD 155
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
285-398 1.41e-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: 40.19  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149 285 VAQTGTGKTLCYLMpgfihlVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKYSYKGLRSVCVYGGGNRDEQIEELKK 364
Cdd:cd18035   22 VLPTGLGKTIIAIL------VAADRLTKKGGK--VLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPEERAERWDA 93
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 222352149 365 GvDIIIATPGRL-NDLqMSNFVNLKNITYLVLDEA 398
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 1.45e-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: 37.55  E-value: 1.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 222352149  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 1.47e-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: 37.56  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222352149  70 LCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQ-TKAKAVIDNFV 132
Cdd:cd22419    3 LSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGvDSARTRIEVLV 66
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
79-128 1.54e-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: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 222352149  79 VGAVIGRGGSKIKNIQSTTNTTIQIIQE-----QPESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22428   16 VGLIIGRQGATIKQIQKETGARIDFKDEgsggeLPERVLLIQGNPVQAQRAEEAI 70
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
77-105 1.71e-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: 37.56  E-value: 1.71e-03
                         10        20
                 ....*....|....*....|....*....
gi 222352149  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 1.81e-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: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222352149  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 2.55e-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: 2.55e-03
                         10        20
                 ....*....|....*....|....*...
gi 222352149  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 2.59e-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: 2.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222352149  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 2.98e-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: 2.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149  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 3.87e-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: 3.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222352149  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 4.60e-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: 4.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 222352149  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 5.82e-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: 5.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149  70 LCFALKSHFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPES------LVKIFGSKAMQTKAKAVID 129
Cdd:cd22488    2 MTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQPPPNgdpnfkLFIIRGSPQQIDHAKQLIE 67
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
80-117 6.19e-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: 35.71  E-value: 6.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 222352149  80 GAVIGRGGSKIKNIQSTTNTTIQIIQEQ-PES---LVKIFGS 117
Cdd:cd02396   14 GSLIGKGGSKIKEIRESTGASVQVASEMlPNSterAVTISGS 55
ResIII pfam04851
Type III restriction enzyme, res subunit;
285-398 6.97e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222352149  285 VAQTGTGKTLCYLmpgfiHLVLQPSLKGQRNRpgMLVLTPTRELALQVEGECCKYSYKGLRSVCVYGGGNRDEQieelKK 364
Cdd:pfam04851  29 VMATGSGKTLTAA-----KLIARLFKKGPIKK--VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDES----VD 97
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 222352149  365 GVDIIIATPGRLN--DLQMSNFVNLKNITYLVLDEA 398
Cdd:pfam04851  98 DNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEA 133
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 6.99e-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: 6.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222352149  77 HFVGAVIGRGGSKIKNIQSTTNTTIQIIQEQPESLVKIFGSKAMQTKAKAVIDNFV 132
Cdd:cd22424   13 RVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVERAREEIEAHI 68
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
78-128 8.32e-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: 35.66  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222352149  78 FVGAVIGRGGSKIKNIQSTTNTTIQI--IQE----QPESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22401   10 LCGRLIGKDGRNIKKIMEDTNTKITIssLQDltsyNPERTITIKGSLEAMSEAESLI 66
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
80-128 9.31e-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: 9.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222352149  80 GAVIGRGGSKIKNIQSTTNTTIQIIQEQ-----PESLVKIFGSKAMQTKAKAVI 128
Cdd:cd22436   13 GMIIGKGGATIKAIMEQSGARVQISQKPesinlQERVVTVTGEPEANRKAVSLI 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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