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Conserved domains on  [gi|1907194079|ref|XP_036010385|]
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probable ATP-dependent RNA helicase DDX43 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
249-580 3.11e-145

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 425.72  E-value: 3.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFihldsQPLAREQRNGPGMLVLTPTRELAL 328
Cdd:COG0513    11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:COG0513    86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTlDLVAVSTVKQNIIITTEEEKRTHIQTFLENMSPkDK 487
Cdd:COG0513   166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 488 VIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIE 567
Cdd:COG0513   244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                         330
                  ....*....|...
gi 1907194079 568 EYVHRVGRTGRAG 580
Cdd:COG0513   324 DYVHRIGRTGRAG 336
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
68-133 3.35e-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: 104.29  E-value: 3.35e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  68 PLCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
249-580 3.11e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 425.72  E-value: 3.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFihldsQPLAREQRNGPGMLVLTPTRELAL 328
Cdd:COG0513    11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:COG0513    86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTlDLVAVSTVKQNIIITTEEEKRTHIQTFLENMSPkDK 487
Cdd:COG0513   166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 488 VIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIE 567
Cdd:COG0513   244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                         330
                  ....*....|...
gi 1907194079 568 EYVHRVGRTGRAG 580
Cdd:COG0513   324 DYVHRIGRTGRAG 336
PTZ00110 PTZ00110
helicase; Provisional
169-580 1.51e-142

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 423.42  E-value: 1.51e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 169 IDWDQIredalkwekkkwaDLPPIKKNFYIESATTSSMSQVQIDNWRKENfNITCDdlkdgEKRPIPNPICKFEdaFQSY 248
Cdd:PTZ00110   79 IDWKSI-------------NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EITII-----AGENVPKPVVSFE--YTSF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PE-VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQrNGPGMLVLTPTRELA 327
Cdd:PTZ00110  138 PDyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG-DGPIVLVLAPTRELA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 328 LQVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEP 406
Cdd:PTZ00110  217 EQIREQCNKFGaSSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 407 QIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKE-PMIVYVGTLDLVAVSTVKQNIIITTEEEKRTHIQTFLEN-MSP 484
Cdd:PTZ00110  297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRD 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 485 KDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPR 564
Cdd:PTZ00110  377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                         410
                  ....*....|....*.
gi 1907194079 565 NIEEYVHRVGRTGRAG 580
Cdd:PTZ00110  457 QIEDYVHRIGRTGRAG 472
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
251-447 2.69e-137

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: 396.83  E-value: 2.69e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYSYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMK 410
Cdd:cd17958    81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194079 411 ILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVY 447
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
264-435 4.52e-55

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: 183.60  E-value: 4.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 264 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDsqplarEQRNGPGMLVLTPTRELALQVEAECSKY-SYGDL 342
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD------KLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 343 KSVCVYGGGDRDGQIQDVsKGVDIIIATPGRLNDLqMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTI 422
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 1907194079 423 MTSATWPYAVRRL 435
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
255-453 2.15e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 175.37  E-value: 2.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  255 IKRAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLSYLMPGFIHLDSQPlareqrnGPGMLVLTPTRELALQVEAE 333
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGK-------GGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  334 CSKY-SYGDLKSVCVYGGGDRDGQIQDVSKGV-DIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKI 411
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907194079  412 LLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDL 453
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 ...
68-133 3.35e-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: 104.29  E-value: 3.35e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  68 PLCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
73-129 1.20e-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: 1.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEA---EIKIFGNKAMQTKAKTVIDN 129
Cdd:pfam00013   6 VPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGnerIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
73-131 5.66e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 5.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079   73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVI-KGNPEAEIKIFGNKAMQTKAKTVIDNVV 131
Cdd:smart00322   9 IPADKVGLIIGKGGSTIKKIEEETGVKIDIPgPGSEERVVEITGPPENVEKAAELILEIL 68
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
69-133 7.52e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 7.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  69 LCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVikgNPEAEIKIFG-NKAMQTKAKTVIDNVVKK 133
Cdd:PRK11824  556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDI---EDDGTVKIAAtDGEAAEAAKERIEGITAE 618
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
249-580 3.11e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 425.72  E-value: 3.11e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFihldsQPLAREQRNGPGMLVLTPTRELAL 328
Cdd:COG0513    11 PPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL-----QRLDPSRPRAPQALILAPTRELAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:COG0513    86 QVAEELRKLAkYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIED 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTlDLVAVSTVKQNIIITTEEEKRTHIQTFLENMSPkDK 487
Cdd:COG0513   166 IERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAP-ENATAETIEQRYYLVDKRDKLELLRRLLRDEDP-ER 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 488 VIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIE 567
Cdd:COG0513   244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPE 323
                         330
                  ....*....|...
gi 1907194079 568 EYVHRVGRTGRAG 580
Cdd:COG0513   324 DYVHRIGRTGRAG 336
PTZ00110 PTZ00110
helicase; Provisional
169-580 1.51e-142

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 423.42  E-value: 1.51e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 169 IDWDQIredalkwekkkwaDLPPIKKNFYIESATTSSMSQVQIDNWRKENfNITCDdlkdgEKRPIPNPICKFEdaFQSY 248
Cdd:PTZ00110   79 IDWKSI-------------NLVPFEKNFYKEHPEVSALSSKEVDEIRKEK-EITII-----AGENVPKPVVSFE--YTSF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PE-VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQrNGPGMLVLTPTRELA 327
Cdd:PTZ00110  138 PDyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG-DGPIVLVLAPTRELA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 328 LQVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEP 406
Cdd:PTZ00110  217 EQIREQCNKFGaSSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 407 QIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKE-PMIVYVGTLDLVAVSTVKQNIIITTEEEKRTHIQTFLEN-MSP 484
Cdd:PTZ00110  297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRiMRD 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 485 KDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPR 564
Cdd:PTZ00110  377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
                         410
                  ....*....|....*.
gi 1907194079 565 NIEEYVHRVGRTGRAG 580
Cdd:PTZ00110  457 QIEDYVHRIGRTGRAG 472
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
251-447 2.69e-137

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: 396.83  E-value: 2.69e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYSYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMK 410
Cdd:cd17958    81 EAECSKYSYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194079 411 ILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVY 447
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
251-446 8.99e-96

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: 290.50  E-value: 8.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlaREQRNGPGMLVLTPTRELALQV 330
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYSYG-DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIM 409
Cdd:cd00268    79 AEVARKLGKGtGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194079 410 KILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
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 ...
251-446 1.37e-94

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: 287.73  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLaREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPP-LERGDGPIVLVLAPTRELAQQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYSYG-DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIM 409
Cdd:cd17966    80 QQEANKFGGSsRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194079 410 KILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17966   160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
249-579 8.29e-85

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 271.68  E-value: 8.29e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNGPGMLVLTPTRELAL 328
Cdd:PRK10590   10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTRELAA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:PRK10590   90 QIGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDlVAVSTVKQNIIITTEEEKRtHIQTFLENMSPKDK 487
Cdd:PRK10590  170 IRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKR-ELLSQMIGKGNWQQ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 488 VIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIE 567
Cdd:PRK10590  248 VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327
                         330
                  ....*....|..
gi 1907194079 568 EYVHRVGRTGRA 579
Cdd:PRK10590  328 DYVHRIGRTGRA 339
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
235-449 4.64e-84

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: 261.87  E-value: 4.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 235 PNPICKFEDAfqSYPE-VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLArEQRN 313
Cdd:cd18049    20 PKPVLNFYEA--NFPAnVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL-ERGD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 314 GPGMLVLTPTRELALQVEAECSKYSYG-DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLV 392
Cdd:cd18049    97 GPICLVLAPTRELAQQVQQVAAEYGRAcRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLV 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079 393 LDEADKMLDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVG 449
Cdd:cd18049   177 LDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
240-580 2.01e-83

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 266.84  E-value: 2.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 240 KFEDaFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLARE-QRNGPGML 318
Cdd:PRK04837    9 KFSD-FALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrKVNQPRAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 319 VLTPTRELALQV--EAECSKYSYGdLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEA 396
Cdd:PRK04837   88 IMAPTRELAVQIhaDAEPLAQATG-LKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 397 DKMLDMGFEPQImKILLDVRPD---RQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDLVAVStVKQNIIITTEEEKRT 473
Cdd:PRK04837  167 DRMFDLGFIKDI-RWLFRRMPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHR-IKEELFYPSNEEKMR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 474 HIQTFLENMSPkDKVIVFVSRK----AVADHLSSDlilRHiSVESLHGNREQSDREKALENFKTGKVRILIATDLASRGL 549
Cdd:PRK04837  245 LLQTLIEEEWP-DRAIIFANTKhrceEIWGHLAAD---GH-RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1907194079 550 DVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PRK04837  320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAG 350
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
180-449 6.23e-80

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: 252.62  E-value: 6.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 180 KWEKKKW--ADLPPIKKNFYIESATTSSMSQVQIDNWRKENfNITCDDLKdgekrpIPNPICKFEDAfqSYPE-VMENIK 256
Cdd:cd18050     8 RLRKKKWdlSELPKFEKNFYVEHPEVARMTQYDVEELRRKK-EITIRGVG------CPKPVFAFHQA--NFPQyVMDVLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 257 RAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLArEQRNGPGMLVLTPTRELALQVEAECSK 336
Cdd:cd18050    79 DQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYL-ERGDGPICLVLAPTRELAQQVQQVADD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 337 YSYGD-LKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDV 415
Cdd:cd18050   158 YGKSSrLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 237
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907194079 416 RPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVG 449
Cdd:cd18050   238 RPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
234-444 1.03e-79

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: 250.37  E-value: 1.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 234 IPNPICKFEDAFQSYPeVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQrN 313
Cdd:cd17953     7 CPKPIQKWSQCGLSEK-VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPG-E 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 314 GPGMLVLTPTRELALQVEAECSKYSYG-DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNN--FVNLKSVT 389
Cdd:cd17953    85 GPIGLIMAPTRELALQIYVECKKFSKAlGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDiLTANNgrVTNLRRVT 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079 390 YLVLDEADKMLDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPM 444
Cdd:cd17953   165 YVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
211-580 1.47e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 258.30  E-value: 1.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 211 IDNWRKENFNITCDDLKDGekrpipnpickFEDaFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGK 290
Cdd:PRK01297   70 ASLWKLEDFVVEPQEGKTR-----------FHD-FNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 291 TLSYLMPGFIHLDSQPLAREQRNG-PGMLVLTPTRELALQVE---AECSKYSygDLKSVCVYGGGDRDGQIQDV-SKGVD 365
Cdd:PRK01297  138 TAAFLISIINQLLQTPPPKERYMGePRALIIAPTRELVVQIAkdaAALTKYT--GLNVMTFVGGMDFDKQLKQLeARFCD 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 366 IIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDVRP--DRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:PRK01297  216 ILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDP 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 444 MIVYVGTLDlVAVSTVKQNIIITTEEEKRTHIQTFLeNMSPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSD 523
Cdd:PRK01297  296 AIVEIEPEN-VASDTVEQHVYAVAGSDKYKLLYNLV-TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHK 373
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079 524 REKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PRK01297  374 RIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
241-580 9.64e-78

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 252.56  E-value: 9.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 241 FEDaFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlaREQRNGPGMLVL 320
Cdd:PRK11192    3 FSE-LELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP--RRKSGPPRILIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 321 TPTRELALQVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNNFvNLKSVTYLVLDEADK 398
Cdd:PRK11192   80 TPTRELAMQVADQARELAkHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQyIKEENF-DCRAVETLILDEADR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 399 MLDMGFEPQIMKILLDVRPDRQTIMTSATWP-YAVRRLAQSYLKEPMivyvgtlDLVAVSTVKQNIIIT-------TEEE 470
Cdd:PRK11192  159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPV-------EVEAEPSRRERKKIHqwyyradDLEH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 471 KRTHIQTFLENMSPKdKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLD 550
Cdd:PRK11192  232 KTALLCHLLKQPEVT-RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
                         330       340       350
                  ....*....|....*....|....*....|
gi 1907194079 551 VHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PRK11192  311 IDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
249-450 4.58e-77

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: 243.16  E-value: 4.58e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMP--GFIHLDSQPLAREQRNG--PGMLVLTPTR 324
Cdd:cd17967     9 ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPiiSKLLEDGPPSVGRGRRKayPSALILAPTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 325 ELALQVEAECSKYSYGD-LKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMG 403
Cdd:cd17967    89 ELAIQIYEEARKFSYRSgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194079 404 FEPQIMKIL----LDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGT 450
Cdd:cd17967   169 FEPQIRKIVehpdMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
244-580 7.67e-75

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 248.71  E-value: 7.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 244 AFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQP-LAREQRNGPGMLVLTP 322
Cdd:PRK04537   13 SFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaLADRKPEDPRALILAP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 323 TRELALQVEAECSKYSyGDL--KSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNNFVNLKSVTYLVLDEADKM 399
Cdd:PRK04537   93 TRELAIQIHKDAVKFG-ADLglRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADRM 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 400 LDMGFEPQIMKIL--LDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTlDLVAVSTVKQNIIITTEEEKRTHIQT 477
Cdd:PRK04537  172 FDLGFIKDIRFLLrrMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET-ETITAARVRQRIYFPADEEKQTLLLG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 478 FLENmSPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHV 557
Cdd:PRK04537  251 LLSR-SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
                         330       340
                  ....*....|....*....|...
gi 1907194079 558 YNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PRK04537  330 YNYDLPFDAEDYVHRIGRTARLG 352
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
249-580 1.61e-73

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 242.01  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQplareqRNGPGMLVLTPTRELAL 328
Cdd:PRK11776   13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVK------RFRVQALVLCPTRELAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYSYG--DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEP 406
Cdd:PRK11776   87 QVAKEIRRLARFipNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 407 QIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDlvAVSTVKQNIIITTEEEKRTHIQTFLENMSPkD 486
Cdd:PRK11776  167 AIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDERLPALQRLLLHHQP-E 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 487 KVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNI 566
Cdd:PRK11776  244 SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDP 323
                         330
                  ....*....|....
gi 1907194079 567 EEYVHRVGRTGRAG 580
Cdd:PRK11776  324 EVHVHRIGRTGRAG 337
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
251-447 2.43e-70

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


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 225.66  E-value: 2.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQP--LAREQRNGPGMLVLTPTRELAL 328
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPplDEETKDDGPYALILAPTRELAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKY-SYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:cd17945    81 QIEEETQKFaKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKIL--LDV---RPD---------------RQTIMTSATWPYAVRRLAQSYLKEPMIVY 447
Cdd:cd17945   161 VTKILdaMPVsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
251-446 2.32e-69

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: 222.29  E-value: 2.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlAREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQR-ELEKGEGPIAVIVAPTRELAQQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYS--YGdLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQI 408
Cdd:cd17952    80 YLEAKKFGkaYN-LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907194079 409 MKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17952   159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
234-442 1.51e-67

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: 219.84  E-value: 1.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 234 IPNPICKFEDAfQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRN 313
Cdd:cd18052    38 PPPAILTFEEA-NLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 314 G---PGMLVLTPTRELALQVEAECSKYSYGD-LKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVT 389
Cdd:cd18052   117 EvqePQALIVAPTRELANQIFLEARKFSYGTcIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLK 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079 390 YLVLDEADKMLDMGFEPQIMKILLDV----RPDRQTIMTSATWPYAVRRLAQSYLKE 442
Cdd:cd18052   197 YLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
250-580 5.60e-67

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 229.35  E-value: 5.60e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 250 EVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAreqrngPGMLVLTPTRELALQ 329
Cdd:PRK11634   16 PILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKA------PQILVLAPTRELAVQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 330 VEAECSKYS--YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:PRK11634   90 VAEAMTDFSkhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTldlvAVST---VKQNIIITTEEEKRTHIQTFLEnMSP 484
Cdd:PRK11634  170 VETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS----SVTTrpdISQSYWTVWGMRKNEALVRFLE-AED 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 485 KDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPR 564
Cdd:PRK11634  245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
                         330
                  ....*....|....*.
gi 1907194079 565 NIEEYVHRVGRTGRAG 580
Cdd:PRK11634  325 DSESYVHRIGRTGRAG 340
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
234-580 2.92e-66

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 224.67  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 234 IPNPICKFEDAfQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDS-QPLAREQR 312
Cdd:PLN00206  116 VPPPILSFSSC-GLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPSEQ 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 313 NGPGMLVLTPTRELALQVEAECSKYSYG-DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYL 391
Cdd:PLN00206  195 RNPLAMVLTPTRELCVQVEDQAKVLGKGlPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 392 VLDEADKMLDMGFEPQIMKILLDVrPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDLVAVStVKQNIIITTEEEK 471
Cdd:PLN00206  275 VLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKA-VKQLAIWVETKQK 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 472 RTHIQTFLENMSP-KDKVIVFVSRKAVADHLSSDL-ILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGL 549
Cdd:PLN00206  353 KQKLFDILKSKQHfKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGV 432
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1907194079 550 DVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PLN00206  433 DLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
234-449 1.96e-57

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: 192.95  E-value: 1.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 234 IPNPICKFEDAfqSYPE-VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQ----PLA 308
Cdd:cd18051    16 CPPHIETFSDL--DLGEiIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeSLP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 309 REQRNG------PGMLVLTPTRELALQVEAECSKYSYGDLKSVCV-YGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNN 381
Cdd:cd18051    94 SESGYYgrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVvYGGADIGQQMRDLERGCHLLVATPGRLVDMLERG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194079 382 FVNLKSVTYLVLDEADKMLDMGFEPQIMKILL-DVRP---DRQTIMTSATWPYAVRRLAQSYLKEPMIVYVG 449
Cdd:cd18051   174 KIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqDTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
264-435 4.52e-55

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: 183.60  E-value: 4.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 264 TPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDsqplarEQRNGPGMLVLTPTRELALQVEAECSKY-SYGDL 342
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD------KLDNGPQALVLAPTRELAEQIYEELKKLgKGLGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 343 KSVCVYGGGDRDGQIQDVsKGVDIIIATPGRLNDLqMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTI 422
Cdd:pfam00270  75 KVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
                         170
                  ....*....|...
gi 1907194079 423 MTSATWPYAVRRL 435
Cdd:pfam00270 153 LLSATLPRNLEDL 165
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
245-446 5.39e-55

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: 184.82  E-value: 5.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 245 FQSY---PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSqplaREQRNGPGMLVLT 321
Cdd:cd17959     3 FQSMglsPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA----HSPTVGARALILS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 322 PTRELALQ---VEAECSKYSygDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADK 398
Cdd:cd17959    79 PTRELALQtlkVTKELGKFT--DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907194079 399 MLDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17959   157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
251-449 6.75e-54

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: 181.63  E-value: 6.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLdsqpLAREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL----GKPRKKKGLRALILAPTRELASQI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECSKYSYGDLKSVCVYGGGDRDGQIQDV--SKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQI 408
Cdd:cd17957    77 YRELLKLSKGTGLRIVLLSKSLEAKAKDGPksITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907194079 409 MKILLDVR-PDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVG 449
Cdd:cd17957   157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
459-580 3.86e-53

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: 177.31  E-value: 3.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 459 VKQNIIITTEEEKRTHIQTFLENMSPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRI 538
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907194079 539 LIATDLASRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAG 122
PTZ00424 PTZ00424
helicase 45; Provisional
243-580 4.16e-53

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 186.19  E-value: 4.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 243 DAFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREqrngpgMLVLTP 322
Cdd:PTZ00424   31 DALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQ------ALILAP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 323 TRELALQVEAecSKYSYGDLKSV----CVYGGGDRDgQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADK 398
Cdd:PTZ00424  105 TRELAQQIQK--VVLALGDYLKVrchaCVGGTVVRD-DINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 399 MLDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDLVAVSTVKQNIIITTEEEKRTHIQTF 478
Cdd:PTZ00424  182 MLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 479 LENMSPKDKVIVFVSRKAVaDHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVY 558
Cdd:PTZ00424  262 YETLTITQAIIYCNTRRKV-DYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
                         330       340
                  ....*....|....*....|..
gi 1907194079 559 NYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PTZ00424  341 NYDLPASPENYIHRIGRSGRFG 362
DEXDc smart00487
DEAD-like helicases superfamily;
255-453 2.15e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 175.37  E-value: 2.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  255 IKRAGFQKPTPIQSQAWPIVLQGI-DLIGVAQTGTGKTLSYLMPGFIHLDSQPlareqrnGPGMLVLTPTRELALQVEAE 333
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGK-------GGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  334 CSKY-SYGDLKSVCVYGGGDRDGQIQDVSKGV-DIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKI 411
Cdd:smart00487  74 LKKLgPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907194079  412 LLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYVGTLDL 453
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL 195
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
249-443 2.61e-51

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: 175.20  E-value: 2.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHL--DSQPLAreqrngpgMLVLTPTREL 326
Cdd:cd17954     9 EELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALleNPQRFF--------ALVLAPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 327 ALQVEAECSKY--SYGdLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNNFVNLKSVTYLVLDEADKMLDMG 403
Cdd:cd17954    81 AQQISEQFEALgsSIG-LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907194079 404 FEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:cd17954   160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
249-442 1.10e-50

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: 173.54  E-value: 1.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQ-GIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlAREQRNGPGMLVLTPTRELA 327
Cdd:cd17964     3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTK-PAGRRSGVSALIISPTRELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 328 LQVEAECSKYSYG--DLKSVCVYGGGDRDGQIQDVSK-GVDIIIATPGRLNDLQMNNFV--NLKSVTYLVLDEADKMLDM 402
Cdd:cd17964    82 LQIAAEAKKLLQGlrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDM 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907194079 403 GFEPQIMKILLDVRP----DRQTIMTSATWPYAVRRLAQSYLKE 442
Cdd:cd17964   162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
251-446 5.45e-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: 169.06  E-value: 5.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIH-LDSQ-PLAREQRNGPGMLVLTPTRELAL 328
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFaLEQEkKLPFIKGEGPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYS-------YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLD 401
Cdd:cd17951    81 QTHEVIEYYCkalqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907194079 402 MGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
241-443 1.78e-48

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: 167.47  E-value: 1.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 241 FEDaFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREqrngpgMLVL 320
Cdd:cd17940     1 FED-YGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ------ALIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 321 TPTRELALQVEAECSKYS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKM 399
Cdd:cd17940    74 VPTRELALQTSQVCKELGkHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKL 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907194079 400 LDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:cd17940   154 LSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
254-446 1.39e-47

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: 164.64  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 254 NIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHldsqplAREQRNGPGMLVLTPTRELALQVEAE 333
Cdd:cd17962     4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR------CLTEHRNPSALILTPTRELAVQIEDQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 334 CSKYSYG--DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKI 411
Cdd:cd17962    78 AKELMKGlpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDI 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907194079 412 LLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17962   158 LENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
259-446 7.60e-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: 163.53  E-value: 7.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 259 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlAREQRN-GPGMLVLTPTRELALQVEAECSKY 337
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLE-PRVDRSdGTLALVLVPTRELALQIYEVLEKL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 338 sygdLKSV------CVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMK 410
Cdd:cd17949    89 ----LKPFhwivpgYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907194079 411 IL--LDVRPD-----------RQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17949   165 ILelLDDKRSkaggekskpsrRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
259-443 7.93e-45

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: 157.42  E-value: 7.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 259 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFihldsQPLAREQRNGPG--MLVLTPTRELALQVEAECSK 336
Cdd:cd17947     9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL-----ERLLYRPKKKAAtrVLVLVPTRELAMQCFSVLQQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 337 YS-YGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNF-VNLKSVTYLVLDEADKMLDMGFEPQIMKILLD 414
Cdd:cd17947    84 LAqFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
                         170       180
                  ....*....|....*....|....*....
gi 1907194079 415 VRPDRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:cd17947   164 CPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
252-449 1.39e-44

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: 156.75  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 252 MENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPG--FIHldsqPLAREQRNGPGMLVLTPTRELALQ 329
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLY----KLKFKPRNGTGVIIISPTRELALQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 330 ---VEAECSKY---SYGdlksvCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQ-MNNFV--NLKSvtyLVLDEADKM 399
Cdd:cd17942    78 iygVAKELLKYhsqTFG-----IVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQnTKGFLykNLQC---LIIDEADRI 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907194079 400 LDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIvYVG 449
Cdd:cd17942   150 LEIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPL-YVG 198
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
255-448 5.22e-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: 155.14  E-value: 5.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 255 IKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREqrNGPGMLVLTPTRELALQV-EAE 333
Cdd:cd17941     5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPE--DGLGALIISPTRELAMQIfEVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 334 CSKYSYGDLKSVCVYGGGDRDGQIQDVSkGVDIIIATPGRLndLQ-MNNFVNLKS--VTYLVLDEADKMLDMGFEPQIMK 410
Cdd:cd17941    83 RKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRL--LQhMDETPGFDTsnLQMLVLDEADRILDMGFKETLDA 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907194079 411 ILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYV 448
Cdd:cd17941   160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
251-443 1.26e-42

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: 151.57  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLdSQPLAREQRNGPGMLVLTPTRELALQV 330
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIL-LKRKANLKKGQVGALIISPTRELATQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 EAECS---KYSYGDLKSVCVYGGGDRDGQIQDVS-KGVDIIIATPGRLNDL--QMNNFVNLKSVTYLVLDEADKMLDMGF 404
Cdd:cd17960    80 YEVLQsflEHHLPKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGF 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907194079 405 EPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:cd17960   160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
253-444 1.47e-39

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


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 143.52  E-value: 1.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 253 ENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPgfIhldsqpLAREQRNGPGM--LVLTPTRELALQV 330
Cdd:cd17955    12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP--I------LQRLSEDPYGIfaLVLTPTRELAYQI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 eAEcSKYSYG---DLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNN---FVNLKSVTYLVLDEADKMLDMGF 404
Cdd:cd17955    84 -AE-QFRALGaplGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEADRLLTGSF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907194079 405 EPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPM 444
Cdd:cd17955   162 EDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
251-427 2.17e-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: 143.92  E-value: 2.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLSYLMP---GFIHLDSQPLAREQRNGPGMLVLTPTREL 326
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPileRLLSQKSSNGVGGKQKPLRALILTPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 327 ALQV----EAECskySYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDL-QMNN--FVNLKSVTYLVLDEADKM 399
Cdd:cd17946    81 AVQVkdhlKAIA---KYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiQEGNehLANLKSLRFLVLDEADRM 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907194079 400 LDMG-FEP--QIMKILLDVRP----DRQTIMTSAT 427
Cdd:cd17946   158 LEKGhFAEleKILELLNKDRAgkkrKRQTFVFSAT 192
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
252-441 1.33e-38

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: 140.75  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 252 MENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGF--IHLDSQPLAREQrnGPGMLVLTPTRELALQ 329
Cdd:cd17944     2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQPRKRGR--APKVLVLAPTRELANQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 330 VEAECSKYSYgDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIM 409
Cdd:cd17944    80 VTKDFKDITR-KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194079 410 KIL-----LDVRPDRQTIMTSATWPYAVRRLAQSYLK 441
Cdd:cd17944   159 EILsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
251-446 1.54e-38

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: 140.09  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYlmpGFIHLDSqpLAREQRnGPGMLVLTPTRELALQV 330
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVF---VVIALES--LDLERR-HPQVLILAPTREIAVQI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 331 eAECSKY---SYGDLKsVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ 407
Cdd:cd17943    75 -HDVFKKigkKLEGLK-CEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907194079 408 IMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17943   153 VNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
255-446 2.96e-35

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 131.55  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 255 IKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNGPGMLVLTPTRELALQVEAEC 334
Cdd:cd17961     9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 335 SK---YSYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLND-LQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMK 410
Cdd:cd17961    89 EQltaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLKS 168
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907194079 411 ILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17961   169 LLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
251-435 5.97e-35

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 131.72  E-value: 5.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPgFIH--LDSQPLAREQRNGPGMLVLTPTRELAL 328
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQrlLRYKLLAEGPFNAPRGLVITPSRELAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYSYG-DLKSVCVyGGGDRDGQIQDVSKG-VDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEP 406
Cdd:cd17948    80 QIGSVAQSLTEGlGLKVKVI-TGGRTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907194079 407 QIMKIL----LDVRPDR---------QTIMTSATWPYAVRRL 435
Cdd:cd17948   159 KLSHFLrrfpLASRRSEntdgldpgtQLVLVSATMPSGVGEV 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
249-446 1.56e-34

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: 129.23  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGID--LIGVAQTGTGKTLSYLMPGFIHLDsqplarEQRNGPGMLVLTPTREL 326
Cdd:cd17963     3 PELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRVD------PTLKSPQALCLAPTREL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 327 ALQVEAECSKY-SYGDLKSVCVYGGGDRDGqiqdvSKGVD--IIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDM- 402
Cdd:cd17963    77 ARQIGEVVEKMgKFTGVKVALAVPGNDVPR-----GKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTq 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907194079 403 GFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17963   152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
245-448 5.75e-33

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: 125.54  E-value: 5.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 245 FQSY---PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlareqrNGPGMLVLT 321
Cdd:cd17950     4 FRDFllkPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVSVLVIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 322 PTRELALQVEAE---CSKYsYGDLKSVCVYGGGDRDGQIQDVSKGV-DIIIATPGRLNDLQMNNFVNLKSVTYLVLDEAD 397
Cdd:cd17950    78 HTRELAFQISNEyerFSKY-MPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907194079 398 KML-DMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIVYV 448
Cdd:cd17950   157 KMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
259-446 1.99e-32

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: 123.59  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 259 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSylmpgFIHLDSQPLAREQRNgPGMLVLTPTRELALQVEAECSKY- 337
Cdd:cd17939    16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTAT-----FSIGALQRIDTTVRE-TQALVLAPTRELAQQIQKVVKALg 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 338 SYGDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDVRP 417
Cdd:cd17939    90 DYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPP 169
                         170       180
                  ....*....|....*....|....*....
gi 1907194079 418 DRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd17939   170 ETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
470-580 9.13e-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: 118.47  E-value: 9.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 470 EKRTHIQTFLENmSPKDKVIVFVSRKavaDHLSSDLILR--HISVESLHGNREQSDREKALENFKTGKVRILIATDLASR 547
Cdd:pfam00271   1 EKLEALLELLKK-ERGGKVLIFSQTK---KTLEAELLLEkeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907194079 548 GLDVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
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 ...
249-446 3.18e-30

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 117.42  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPgFIHLDSQplareqrngpgmLVLTPTRELAL 328
Cdd:cd17938     8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQIVVA------------LILEPSRELAE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKYSY----GDLKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGF 404
Cdd:cd17938    75 QTYNCIENFKKyldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGN 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907194079 405 EPQIMKIL-----LDVRPDR-QTIMTSATW-PYAVRRLAQSYLKEPMIV 446
Cdd:cd17938   155 LETINRIYnripkITSDGKRlQVIVCSATLhSFEVKKLADKIMHFPTWV 203
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
243-443 1.50e-29

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 115.62  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 243 DAFQSYPEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQplareqRNGPGMLVLTP 322
Cdd:cd18046     2 DDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS------LKATQALVLAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 323 TRELALQVEAECSkySYGDLKSV----CVYGGGDRDgQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADK 398
Cdd:cd18046    76 TRELAQQIQKVVM--ALGDYMGIkchaCIGGTSVRD-DAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907194079 399 MLDMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEP 443
Cdd:cd18046   153 MLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
HELICc smart00490
helicase superfamily c-terminal domain;
499-580 1.28e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 106.14  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  499 DHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGR 578
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1907194079  579 AG 580
Cdd:smart00490  81 AG 82
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
68-133 3.35e-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: 104.29  E-value: 3.35e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  68 PLCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22430     1 PLCFKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVKIFGSDEAQQKAKELIDELVGR 66
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
251-435 4.00e-27

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 109.64  E-value: 4.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 251 VMENIKRAGFQKPTPIQSQAWPIVLQGI---------DLIGVAQTGTGKTLSYLMPgFIHLDSQPLAREQRngpgMLVLT 321
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLP-IVQALSKRVVPRLR----ALIVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 322 PTRELALQVEAECSKYSYG-DLKSVCVygGGDRD----------GQIQDVSKGVDIIIATPGRLND-LQMNNFVNLKSVT 389
Cdd:cd17956    76 PTKELVQQVYKVFESLCKGtGLKVVSL--SGQKSfkkeqklllvDTSGRYLSRVDILVATPGRLVDhLNSTPGFTLKHLR 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907194079 390 YLVLDEADKMLDMGFE---PQIMKILLDVRPDRQTIMTSA----TWPYAVRRL 435
Cdd:cd17956   154 FLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDAnlleRSVRPLQKL 206
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
250-446 9.74e-27

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: 107.55  E-value: 9.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 250 EVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDsqPLAREqrngPGMLVLTPTRELALQ 329
Cdd:cd18045     9 DLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD--IQVRE----TQALILSPTRELAVQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 330 VEAECskYSYGDLKSVCVY---GGGDRDGQIQDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEP 406
Cdd:cd18045    83 IQKVL--LALGDYMNVQCHaciGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907194079 407 QIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd18045   161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
243-429 1.24e-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: 97.45  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 243 DAFQSYPEVMENIKRA---------GFQKPTPIQSQAWPIVLQG-----------------IDLIGvAQTGTGKTLSYLM 296
Cdd:cd17965     2 DQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepkleVFLLA-AETGSGKTLAYLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 297 PGFIHL----------DSQPLAREQRNG-PGMLVLTPTRELALQVEA------ECSKYSYGDLKSvcvyGGGDRDGQIQD 359
Cdd:cd17965    81 PLLDYLkrqeqepfeeAEEEYESAKDTGrPRSVILVPTHELVEQVYSvlkklsHTVKLGIKTFSS----GFGPSYQRLQL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194079 360 VSKG-VDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLDVRPDRQTIMTSATWP 429
Cdd:cd17965   157 AFKGrIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
283-575 2.95e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 94.32  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 283 VAQTGTGKTLSYLMpgfihldsqpLAREQRNGPGMLVLTPTRELALQVEAECSKYSYGDLksvcvYGGGDRDgqiqdvsK 362
Cdd:COG1061   106 VAPTGTGKTVLALA----------LAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPL-----AGGGKKD-------S 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 363 GVDIIIATPGRL-NDLQMNNFVNlkSVTYLVLDEA--------DKMLDMgFEPqimKILLDV-----RPDRQTIMT---- 424
Cdd:COG1061   164 DAPITVATYQSLaRRAHLDELGD--RFGLVIIDEAhhagapsyRRILEA-FPA---AYRLGLtatpfRSDGREILLflfd 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 425 ----SATWPYAvrrLAQSYLKEPMIVYVGT------LDLVAVSTVKQNIIITTEEEKRTHIQTFLENMSPKDKVIVFVSR 494
Cdd:COG1061   238 givyEYSLKEA---IEDGYLAPPEYYGIRVdltderAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSS 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 495 KAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVYnydFPRNIE---EYVH 571
Cdd:COG1061   315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGsprEFIQ 391

                  ....
gi 1907194079 572 RVGR 575
Cdd:COG1061   392 RLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
250-446 2.51e-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: 84.30  E-value: 2.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 250 EVMENIKRAGFQKPTPIQSQAWPIVLQG--IDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAreqrngPGMLVLTPTRELA 327
Cdd:cd18048    28 ELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY------PQCLCLSPTFELA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 328 LQ---VEAECSKYSYGdlKSVCVYGGGDRDGQIQDVSKgvDIIIATPGRLNDLQMN-NFVNLKSVTYLVLDEADKMLDM- 402
Cdd:cd18048   102 LQtgkVVEEMGKFCVG--IQVIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMINVq 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907194079 403 GFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd18048   178 GHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
283-427 1.88e-15

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: 73.59  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 283 VAQTGTGKTLSYLMPGFIHLDSQplareqrnGPGMLVLTPTRELALQVEAECSKYSYGDLKsVCVYGGGDRDGQIQDVSK 362
Cdd:cd00046     7 TAPTGSGKTLAALLAALLLLLKK--------GKKVLVLVPTKALALQTAERLRELFGPGIR-VAVLVGGSSAEEREKNKL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079 363 G-VDIIIATPGRL-NDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLD--VRPDRQTIMTSAT 427
Cdd:cd00046    78 GdADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
249-446 2.26e-14

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: 72.06  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQG--IDLIGVAQTGTGKTLSYLMPGFIHLDsqPLAREQRngpgMLVLTPTREL 326
Cdd:cd18047    10 PQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANKYPQ----CLCLSPTYEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 327 ALQ---VEAECSKYSYGDLKSVCVYGGG-DRDGQIQDvskgvDIIIATPGRLNDLQMN-NFVNLKSVTYLVLDEADKML- 400
Cdd:cd18047    84 ALQtgkVIEQMGKFYPELKLAYAVRGNKlERGQKISE-----QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907194079 401 DMGFEPQIMKILLDVRPDRQTIMTSATWPYAVRRLAQSYLKEPMIV 446
Cdd:cd18047   159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
274-580 2.71e-13

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 72.48  E-value: 2.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 274 VLQGIDLIGVAQTGTGKTLSYLMPGfihldsqpLAREqrnGPGmLVLTPTreLAL---QVEAecskysygdLKS-----V 345
Cdd:COG0514    29 VLAGRDALVVMPTGGGKSLCYQLPA--------LLLP---GLT-LVVSPL--IALmkdQVDA---------LRAagiraA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 346 CVYGGGDRDGQ---IQDVSKG-VDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEA--------DkmldmgFEPQIMKI-- 411
Cdd:COG0514    86 FLNSSLSAEERrevLRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghD------FRPDYRRLge 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 412 LLDVRPDRQTIMTSATWPYAVRR--LAQSYLKEPMiVYVGTLDlvavstvKQNI----IITTEEEKRTHIQTFLENMSPK 485
Cdd:COG0514   160 LRERLPNVPVLALTATATPRVRAdiAEQLGLEDPR-VFVGSFD-------RPNLrlevVPKPPDDKLAQLLDFLKEHPGG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 486 DKVIVFVSRKAVaDHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATdlaSR---GLDVHDITHVYNYDF 562
Cdd:COG0514   232 SGIVYCLSRKKV-EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT---IAfgmGIDKPDVRFVIHYDL 307
                         330
                  ....*....|....*...
gi 1907194079 563 PRNIEEYVHRVGRTGRAG 580
Cdd:COG0514   308 PKSIEAYYQEIGRAGRDG 325
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
259-580 6.08e-13

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 71.67  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 259 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIhldsqplareqRNGPgMLVLTPTREL---------ALQ 329
Cdd:PRK11057   22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV-----------LDGL-TLVVSPLISLmkdqvdqllANG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 330 VEAECSKYSYGDLKSVCVYGGGdRDGQIQdvskgvdIIIATPGRlndLQMNNFVNLKSVTYLVL---DEADKMLDMG--F 404
Cdd:PRK11057   90 VAAACLNSTQTREQQLEVMAGC-RTGQIK-------LLYIAPER---LMMDNFLEHLAHWNPALlavDEAHCISQWGhdF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 405 EPQIMKI-LLDVR-PDRQTIMTSATWPYAVRR--LAQSYLKEPMIvYVGTLDlvavstvKQNIIITTEEEKR--THIQTF 478
Cdd:PRK11057  159 RPEYAALgQLRQRfPTLPFMALTATADDTTRQdiVRLLGLNDPLI-QISSFD-------RPNIRYTLVEKFKplDQLMRY 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 479 LENMSPKDKVIVFVSRKAVADhLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLASRGLDVHDITHVY 558
Cdd:PRK11057  231 VQEQRGKSGIIYCNSRAKVED-TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
                         330       340
                  ....*....|....*....|..
gi 1907194079 559 NYDFPRNIEEYVHRVGRTGRAG 580
Cdd:PRK11057  310 HFDIPRNIESYYQETGRAGRDG 331
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
489-579 3.48e-11

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: 61.07  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 489 IVFVSRKAVADHLSSDL-----ILRHISVESL--HGNR--------EQSDREKALENFKTGKVRILIATDLASRGLDVHD 553
Cdd:cd18802    29 IIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSsqrkrslmTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
                          90       100
                  ....*....|....*....|....*.
gi 1907194079 554 ITHVYNYDFPRNIEEYVHRVGRtGRA 579
Cdd:cd18802   109 CNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
483-574 6.48e-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: 60.18  E-value: 6.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 483 SPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGK--VRILIATDLASRGLDVHDITHVYNY 560
Cdd:cd18793    25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILY 104
                          90       100
                  ....*....|....*....|
gi 1907194079 561 DFPRN--IEEY----VHRVG 574
Cdd:cd18793   105 DPWWNpaVEEQaidrAHRIG 124
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
73-129 1.20e-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: 1.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEA---EIKIFGNKAMQTKAKTVIDN 129
Cdd:pfam00013   6 VPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGnerIVTITGTPEAVEAAKALIEE 65
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
249-581 2.09e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 63.38  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWP-IVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAreqrngpgmLVLTPTRELA 327
Cdd:COG1204     9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKA---------LYIVPLRALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 328 LQVEAECSK-YSYGDLKSVCVYGGGDRDGqiqDVSKGVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEAdKMLDmgfEP 406
Cdd:COG1204    80 SEKYREFKRdFEELGIKVGVSTGDYDSDD---EWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA-HLID---DE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 407 Q-------IMKILLDVRPDRQTIMTSATWPyAVRRLAQsYLKEPMIV--YVGTLDLVAVstVKQNIIITTEEEKRTHIQT 477
Cdd:COG1204   153 SrgptlevLLARLRRLNPEAQIVALSATIG-NAEEIAE-WLDAELVKsdWRPVPLNEGV--LYDGVLRFDDGSRRSKDPT 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 478 F---LENMSPKDKVIVFVSR--------KAVADHLSSDLI------LRHISVESL-----------------------HG 517
Cdd:COG1204   229 LalaLDLLEEGGQVLVFVSSrrdaeslaKKLADELKRRLTpeereeLEELAEELLevseethtnekladclekgvafhHA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194079 518 NREQSDREKALENFKTGKVRILIATD-------LASRGLDVHDITHVYNYDFPrnIEEYVHRVGRTGRAGY 581
Cdd:COG1204   309 GLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGY 377
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
73-128 2.41e-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: 2.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVID 128
Cdd:cd00105     5 VPSELVGLIIGKGGSTIKEIEEETGARIQIPKegeGSGERVVTITGTPEAVEKAKELIE 63
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
466-580 2.82e-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: 55.68  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 466 TTEEEKRTHIQTFLENmSPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGKVRILIATDLA 545
Cdd:cd18794    12 DKKDEKLDLLKRIKVE-HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAF 90
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194079 546 SRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:cd18794    91 GMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
538-581 1.41e-08

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 51.94  E-value: 1.41e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907194079 538 ILIATDLASRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGRAGY 581
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
264-396 2.30e-08

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: 54.19  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 264 TPIQSQAW-PIVLQGIDLIGVAQTGTGKTL-SYLMpgfihldsqpLAREQRNGPG-MLVLTPTRELALQVEAECSKySYG 340
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLiAELA----------ILRALATSGGkAVYIAPTRALVNQKEADLRE-RFG 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194079 341 DLKSVCVYGGGDRDGQIQDVSKGvDIIIATPGRLnDLQMNNF--VNLKSVTYLVLDEA 396
Cdd:cd17921    72 PLGKNVGLLTGDPSVNKLLLAEA-DILVATPEKL-DLLLRNGgeRLIQDVRLVVVDEA 127
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
480-576 5.25e-08

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 56.00  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 480 ENMSPKDKVIVFVSRKAVADHLSSDLILRHISVESLHGNREQSDREKALENFKTGK--VRILIATDLASRGLDVHDITHV 557
Cdd:COG0553   544 ELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHV 623
                          90       100
                  ....*....|....*....|....*
gi 1907194079 558 YNYDFPRN--IEEY----VHRVGRT 576
Cdd:COG0553   624 IHYDLWWNpaVEEQaidrAHRIGQT 648
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
484-580 5.32e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 55.89  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 484 PKDKVIVFVSRKAVADHLSSDLILRHISVESLHG--NREQSD------REKALENFKTGKVRILIATDLASRGLDVHDIT 555
Cdd:COG1111   352 PDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaSKEGDKgltqkeQIEILERFRAGEFNVLVATSVAEEGLDIPEVD 431
                          90       100
                  ....*....|....*....|....*.
gi 1907194079 556 HVYNYD-FPRNIeEYVHRVGRTGRAG 580
Cdd:COG1111   432 LVIFYEpVPSEI-RSIQRKGRTGRKR 456
KH smart00322
K homology RNA-binding domain;
73-131 5.66e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 5.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079   73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVI-KGNPEAEIKIFGNKAMQTKAKTVIDNVV 131
Cdd:smart00322   9 IPADKVGLIIGKGGSTIKKIEEETGVKIDIPgPGSEERVVEITGPPENVEKAAELILEIL 68
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
448-578 1.09e-07

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: 51.50  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 448 VGTLDLVAVSTVKQNIIITTEEEKRTHIQTFLENMSPKDKVIVFV-SRKAV-----------ADHLSSDLILRHisvesl 515
Cdd:cd18796     1 KKKLDIKVILPVAPEIFPWAGESGADAYAEVIFLLERHKSTLVFTnTRSQAerlaqrlrelcPDRVPPDFIALH------ 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079 516 HGNREQSDREKALENFKTGKVRILIAT---DLasrGLDVHDITHVYNYDFPRNIEEYVHRVGRTGR 578
Cdd:cd18796    75 HGSLSRELREEVEAALKRGDLKVVVATsslEL---GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
78-132 1.12e-07

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


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 49.11  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  78 VGAVIGRGGSKIREIQNTTNTRIQVIKGNPEA-EIKIFGNKAMQTKAKTVIDNVVK 132
Cdd:cd02394    13 HGHIIGKGGANIKRIREESGVSIRIPDDEANSdEIRIEGSPEGVKKAKAEILELVD 68
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
76-133 8.10e-07

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: 46.70  E-value: 8.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079  76 DVVGAVIGRGGSKIREIQNTTNTRIQVikgNPEAEIKIFG-NKAMQTKAKTVIDNVVKK 133
Cdd:cd02393    13 DKIGDVIGPGGKTIRAIIEETGAKIDI---EDDGTVTIFAtDKESAEAAKAMIEDIVAE 68
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
73-117 1.21e-06

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: 46.07  E-value: 1.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVI---KGNPEAEIKIFGNK 117
Cdd:cd22439     8 IPNDLIGCIIGKGGTKINEIRQLSGATIKIAnseDGSTERSVTITGTP 55
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
249-580 1.33e-06

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: 51.37  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 249 PEVMENIKRAGFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREqrngpgmLVLTPTRELAL 328
Cdd:COG1205    43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-------LYLYPTKALAR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 QVEAECSKY-SYGDLK-SVCVYgGGDRDGQI-QDVSKGVDIIIATPGRLNdLQM--------NNFVNLKsvtYLVLDEA- 396
Cdd:COG1205   116 DQLRRLRELaEALGLGvRVATY-DGDTPPEErRWIREHPDIVLTNPDMLH-YGLlphhtrwaRFFRNLR---YVVIDEAh 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 397 --------------DKML----DMGFEPQImkilldvrpdrqtIMTSATW--PyavRRLAQSYLKEPMIVyV-------G 449
Cdd:COG1205   191 tyrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIgnP---AEHAERLTGRPVTV-VdedgsprG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 450 TLDLVAVstvkqNIIITTEEEKRTHIQT----FLENMSPKDKVIVFV-SRKAV---ADHLSSDLILRHI--SVESLHGNR 519
Cdd:COG1205   254 ERTFVLW-----NPPLVDDGIRRSALAEaarlLADLVREGLRTLVFTrSRRGAellARYARRALREPDLadRVAAYRAGY 328
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079 520 EQSDReKALEN-FKTGKVRILIAT-------DLAsrGLDVhdithVYNYDFPRNIEEYVHRVGRTGRAG 580
Cdd:COG1205   329 LPEER-REIERgLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRG 389
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
260-327 1.81e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 50.87  E-value: 1.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079 260 FQKPTPIQSQAWPIVLQGID-LIgVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNGPGMLVLTPTRELA 327
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGEStLL-IAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLYISPLKALA 89
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
79-131 4.80e-06

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: 44.10  E-value: 4.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907194079  79 GAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKIFGNKAMQ-TKAKTVIDNVV 131
Cdd:cd22419    13 KFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGvDSARTRIEVLV 66
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
73-113 6.75e-06

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: 43.79  E-value: 6.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKI 113
Cdd:cd22398     6 VPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRI 46
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
73-109 8.51e-06

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: 43.80  E-value: 8.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQV--------------IKGNPEA 109
Cdd:cd22400     6 VPSEFVGAIIGKGGATIRQITQQTGARIDIhrkenagaaekaitIYGTPEG 56
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
475-580 9.86e-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: 45.70  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 475 IQTFLENMSPKDKVIVFvsrkavADHLSSdliLRHIS----VESLHGNREQSDREKALENFKTGKVRILIATDLASRGLD 550
Cdd:cd18789    39 LEELLKRHEQGDKIIVF------TDNVEA---LYRYAkrllKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907194079 551 VHD----ITHVYNYDFPRnieEYVHRVGRTGRAG 580
Cdd:cd18789   110 LPEanvaIQISGHGGSRR---QEAQRLGRILRPK 140
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
73-128 1.28e-05

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 43.56  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQV---IKGNPEAEIKIFGNKAMQTKAKTVID 128
Cdd:cd22522    15 IPNDLIGCIIGRQGTKINEIRQMSGAQIKIanaTEGSSERQITITGSPANISLAQYLIN 73
PRK13766 PRK13766
Hef nuclease; Provisional
483-581 1.28e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 48.33  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 483 SPKDKVIVFV-SR---KAVADHLSSDlilrHISVESLHGnreQSDRE-----------KALENFKTGKVRILIATDLASR 547
Cdd:PRK13766  363 NPDSRIIVFTqYRdtaEKIVDLLEKE----GIKAVRFVG---QASKDgdkgmsqkeqiEILDKFRAGEFNVLVSTSVAEE 435
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907194079 548 GLDVHDITHVYNYDfP-----RNIEeyvhRVGRTGRAGY 581
Cdd:PRK13766  436 GLDIPSVDLVIFYE-PvpseiRSIQ----RKGRTGRQEE 469
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
281-396 1.51e-05

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.11  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 281 IGVAQTGTGKTLSYLMpgFIHLDSQPLAREQRNGPGMLVLTPTRELALQvEAECSKySYGDLKSVCVYGGGDRDGQIQDV 360
Cdd:cd18034    20 IVVLPTGSGKTLIAVM--LIKEMGELNRKEKNPKKRAVFLVPTVPLVAQ-QAEAIR-SHTDLKVGEYSGEMGVDKWTKER 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907194079 361 SKGV----DIIIATPGRLNDLQMNNFVNLKSVTYLVLDEA 396
Cdd:cd18034    96 WKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
73-127 1.73e-05

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: 42.98  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQV------IKGNPEAEIKIFGNKAMQTKAKTVI 127
Cdd:cd22437     5 VPNSSCGLIIGKGGSTIKELREDSNANIKIspkdqlLPGSSERIVTITGSFDQVVKAVALI 65
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
72-104 2.42e-05

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: 42.56  E-value: 2.42e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907194079  72 GVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK 104
Cdd:cd09031     6 EVPENLVGAILGKGGKTLVEIQELTGARIQISK 38
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
73-106 2.59e-05

first 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 first one.


Pssm-ID: 411863 [Multi-domain]  Cd Length: 73  Bit Score: 42.52  E-value: 2.59e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN 106
Cdd:cd22435     8 VPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNN 41
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
71-134 2.85e-05

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


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 42.78  E-value: 2.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEA-----------EIKIFGNKAMQTKAKTVIDNVVKKQ 134
Cdd:cd22446    11 ISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGnydeddddetvEISIEGDAEGVELAKKEIEAIVKER 85
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
71-133 3.30e-05

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


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 42.24  E-value: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22479     5 YRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPdsgGLPERSVSLTGSPEAVQKAKMMLDDIVSR 70
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
253-452 4.19e-05

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 44.83  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 253 ENIKRAGFQKPTPIQSQAwpI--VLQGIDLIGVAQTGTGKTLSYLMPGFIhldsqplareqRNGPGmLVLTPTreLAL-- 328
Cdd:cd17920     3 ILKEVFGYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVT-LVVSPL--ISLmq 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 329 -QVEAECSKysygDLKSVCVYGGGDRDGQIQDVSK----GVDIIIATPGRLNDLQMNNFVN----LKSVTYLVLDEADKM 399
Cdd:cd17920    67 dQVDRLQQL----GIRAAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAHCV 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194079 400 LDMG--FEPQIMKI--LLDVRPDRQTIMTSATWPYAVRRLAQSYLK-EPMIVYVGTLD 452
Cdd:cd17920   143 SQWGhdFRPDYLRLgrLRRALPGVPILALTATATPEVREDILKRLGlRNPVIFRASFD 200
MOEP19 pfam16005
KH-like RNA-binding domain; MOEP19 is a family of mammalian KH-like RNA-binding motifs. The ...
68-130 4.52e-05

KH-like RNA-binding domain; MOEP19 is a family of mammalian KH-like RNA-binding motifs. The family is expressed during early embryogenesis. It appears to effect an early form of molecular asymmetry within the murine oocyte cytoplasm. The family marks a defined cortical cytoplasmic domain in oocytes and provides evidence for mammalian oocyte polarity and a form of pre-patterning that persists in zygotes and early embryos through the morula stage.


Pssm-ID: 464969  Cd Length: 85  Bit Score: 42.24  E-value: 4.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079  68 PLCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPE--AEIKIFGNKAMQTKAKTVIDNV 130
Cdd:pfam16005  14 PLVFYLEAWLLELIFGPDGERIPHIEWMSQTLLQVDVVDSEglAEITIFGRPRYQKRVKKMLLSL 78
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
461-578 5.25e-05

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: 43.50  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 461 QNIIITTE-EEKRTHIQTFLENMSPKDKVIVFVSrkavadhlssdlilrHISVESLHGnREQSDREKALENFKTGKVRIL 539
Cdd:cd18801    31 TRVIIFSEfRDSAEEIVNFLSKIRPGIRATRFIG---------------QASGKSSKG-MSQKEQKEVIEQFRKGGYNVL 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907194079 540 IATDLASRGLDVHDITHVYNYDFPRNIEEYVHRVGRTGR 578
Cdd:cd18801    95 VATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
262-414 5.75e-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: 44.35  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 262 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPlareQRNGPGMLVLTPTRELALQVEAECSKYsYGD 341
Cdd:cd17927     2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFP----AGRKGKVVFLANKVPLVEQQKEVFRKH-FER 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079 342 LKSVCVYGGGDRDGQI--QDVSKGVDIIIATPGRL-NDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLD 414
Cdd:cd17927    77 PGYKVTGLSGDTSENVsvEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRYLD 152
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
78-127 5.98e-05

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: 41.03  E-value: 5.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194079  78 VGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAE-IKIFGNKAMQTKAKTVI 127
Cdd:cd22411    11 HKNIIGKGGATIKKIREETNTRIDLPEENSDSDvITITGKKEDVEKARERI 61
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
75-123 6.03e-05

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: 41.08  E-value: 6.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907194079  75 NDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN----PEAEIKIFGNKAMQTKA 123
Cdd:cd22402     9 NKAVGAIIGTKGSHIRYIKRFSGASIKIAPADspdaPERKVTITGPPEAQWKA 61
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
283-396 6.11e-05

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: 44.04  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 283 VAQTGTGKTLSYLMPGfihldsqpLAREQRNGPGMLVLTPTRELALQVEAECSKYSYGDLKSVCVYGGGDRDGQIQDVSK 362
Cdd:cd18035    22 VLPTGLGKTIIAILVA--------ADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPEERAERWDA 93
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194079 363 GvDIIIATPGRL-NDLqMNNFVNLKSVTYLVLDEA 396
Cdd:cd18035    94 S-KIIVATPQVIeNDL-LAGRITLDDVSLLIFDEA 126
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
73-113 7.15e-05

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: 41.17  E-value: 7.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQV---------------IKGNPE----AEIKI 113
Cdd:cd22428    11 VPREAVGLIIGRQGATIKQIQKETGARIDFkdegsggelpervllIQGNPVqaqrAEEAI 70
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
71-131 7.32e-05

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: 41.09  E-value: 7.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVIDNVV 131
Cdd:cd22396     5 YKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPdsgGLPERPCTLTGTPDAIETAKRLIDQIV 68
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
69-133 7.52e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 7.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  69 LCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVikgNPEAEIKIFG-NKAMQTKAKTVIDNVVKK 133
Cdd:PRK11824  556 ETIKIPPDKIRDVIGPGGKTIREITEETGAKIDI---EDDGTVKIAAtDGEAAEAAKERIEGITAE 618
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
71-106 8.11e-05

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: 40.91  E-value: 8.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN 106
Cdd:cd22457     3 ISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAP 38
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
267-396 8.70e-05

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: 43.73  E-value: 8.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 267 QSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREqrngpgmLVLTPTRELALQVEAECSKYSYGDLKSVC 346
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA-------LYLYPTKALAQDQLRSLRELLEQLGLGIR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194079 347 V--YGG----GDRDGQIqdvSKGVDIIIATPGRLN-------DLQMNNFVNLKsvtYLVLDEA 396
Cdd:cd17923    78 VatYDGdtprEERRAII---RNPPRILLTNPDMLHyallphhDRWARFLRNLR---YVVLDEA 134
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
71-127 1.25e-04

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


Pssm-ID: 411951  Cd Length: 68  Bit Score: 40.26  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQV---IKGNPEAEIKIFGNKAMQTKAKTVI 127
Cdd:cd22523     6 FLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIgnqTEGTSERHVTITGSPVSITLAQYLI 65
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
76-127 1.31e-04

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: 40.31  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079  76 DVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVI 127
Cdd:cd22462     8 HAVGSVIGRGGSNINQIREISGAKVEVLKpdsATGERIVLISGTPDQARHAQNLI 62
KH-I_FUBP1_rpt1 cd22478
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
71-133 1.37e-04

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: 40.39  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22478     8 YKVPDGMVGFIIGRGGEQISRIQQESGCKIQIAPdsgGLPERSCMLTGTPESVQSAKRLLDQIVEK 73
KH-I_KHDC1_like cd22440
type I K homology (KH) RNA-binding domain found in KHDC1-like family; The KHDC1-like family ...
68-130 1.56e-04

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: 39.97  E-value: 1.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079  68 PLCFGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPE--AEIKIFGNKAMQTKAKTVIDNV 130
Cdd:cd22440     4 PSVFHVEARLLEKIFGPDGTLIPHLEQESHTLIHVDRWDPEgkAEITIFGPPRYRQRAKWMLQCL 68
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
75-136 1.71e-04

third 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 third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 40.00  E-value: 1.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079  75 NDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAE---IKIFGNKAMQTKAKTVIDNVVKKQQN 136
Cdd:cd22434    10 KDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEdriITITGTQDQIQNAQYLLQNSVKQYSG 74
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
73-128 3.27e-04

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411949  Cd Length: 76  Bit Score: 39.65  E-value: 3.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQV---IKGNPEAEIKIFGNKAMQTKAKTVID 128
Cdd:cd22521    11 IPNDLIGCIIGRQGAKINEIRQMSGAQIKIanpVEGSTDRQVTITGSAASISLAQYLIN 69
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
72-102 3.35e-04

third 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 third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 39.33  E-value: 3.35e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907194079  72 GVKNDVVGAVIGRGGSKIREIQNTTNTRIQV 102
Cdd:cd22514     6 GVPDEHIGAILGRGGRTINEIQQHSGARIKI 36
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
75-116 3.49e-04

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: 39.13  E-value: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907194079  75 NDVVGAVIGRGGSKIREIQNTTNTRIQVIK------GNPEAEIKIFGN 116
Cdd:cd22401     8 NNLCGRLIGKDGRNIKKIMEDTNTKITISSlqdltsYNPERTITIKGS 55
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
274-427 4.02e-04

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: 41.55  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 274 VLQGIDLIGVAQTGTGKTLSYLMPGFIHLDsqplareqrNGPGMLVLTPTRELALQVEAECSKYSYGDLKsvCVYGGGDR 353
Cdd:cd18028    14 LLKGENLLISIPTASGKTLIAEMAMVNTLL---------EGGKALYLVPLRALASEKYEEFKKLEEIGLK--VGISTGDY 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079 354 DGQIQDVSKgVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEADKMLDMGFEPQ---IMKILLDVRPDRQTIMTSAT 427
Cdd:cd18028    83 DEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTlesIVARLRRLNPNTQIIGLSAT 158
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
71-133 5.17e-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: 38.79  E-value: 5.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22449     8 FDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
73-115 5.72e-04

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


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 38.45  E-value: 5.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFG 115
Cdd:cd22454    10 IPNADVGKVIGKGGETIKRIEALTDTVITFERvngGSPNREVQITG 55
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
283-396 5.90e-04

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.79  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 283 VAQTGTGKTLSYLMPGfihldsqpLAREQRNGPGMLVLTPTRELALQVEAECSKYSYGDLKSVCVYGGGDRDGQIQDVSK 362
Cdd:COG1111    23 VLPTGLGKTAVALLVI--------AERLHKKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKELWE 94
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194079 363 GVDIIIATPGRL-NDLqMNNFVNLKSVTYLVLDEA 396
Cdd:COG1111    95 KARIIVATPQVIeNDL-IAGRIDLDDVSLLIFDEA 128
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
77-132 6.13e-04

second 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 second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 38.94  E-value: 6.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079  77 VVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEA-----------EIKIFGNKAMQTKAKTVIDNVVK 132
Cdd:cd22447    14 TRARIIGKKGANLKQIREKTGVRIDIPPRDADAapadedddtmvEVTITGDEFNVQHAKQRIEEIIS 80
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
262-414 9.28e-04

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: 40.92  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 262 KPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHLDSQPLAREQRNgpgMLVLTPTRELALQVEAECSKYSYGD 341
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGR---VVVLVNKVPLVEQQLEKFFKYFRKG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079 342 LKSVCVYGGGDRDGQIQDVSKGVDIIIATPGRL-NDLQ---MNNFVNLKSVTYLVLDEADKMLDMGFEPQIMKILLD 414
Cdd:cd18036    79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILiNNLLsgrEEERVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLD 155
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
259-396 1.53e-03

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 39.93  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 259 GFQKPTPIQSQAWPIVLQGIDLIGVAQTGTGKTLSYLMPGFIHldsqplareQRNGPGM-LVLTPTreLAL---QVEAEC 334
Cdd:cd18018     9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLL---------RRRGPGLtLVVSPL--IALmkdQVDALP 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 335 SKysygdLKSVCVYGG---GDRDGQIQDVSKG-VDIIIATPGRLNDlqmNNFVNL----KSVTYLVLDEA 396
Cdd:cd18018    78 RA-----IKAAALNSSltrEERRRILEKLRAGeVKILYVSPERLVN---ESFRELlrqtPPISLLVVDEA 139
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
391-551 1.62e-03

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.88  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 391 LVLDEADKMLD--MGFEPQIMKILLDVrpDRQTIMTSATWPYAVRRLAQSYLkepMIVYVGTLDLVAVSTVKQNIIITTE 468
Cdd:cd09639   127 LIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEKIG---YVEENEPLDLKPNERAPFIKIESDK 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 469 EEKRTHIQTFLENMSPKDKVIVFVS--RKAVAdhlSSDLILRHISVES---LHGNREQSDREKA----LENFKTGKVRIL 539
Cdd:cd09639   202 VGEISSLERLLEFIKKGGSVAIIVNtvDRAQE---FYQQLKEKGPEEEimlIHSRFTEKDRAKKeaelLLEFKKSEKFVI 278
                         170
                  ....*....|..
gi 1907194079 540 IATDLASRGLDV 551
Cdd:cd09639   279 VATQVIEASLDI 290
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
79-134 2.18e-03

sixth 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 sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 37.05  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194079  79 GAVIGRGGSKIREIQNTTNTRIQV-IKGNPEAEIKIFGNKAMQTKAKTVIDNVVKKQ 134
Cdd:cd22451    13 RAIIGKGGAVLRELEAETGCRIQVpKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
262-399 2.40e-03

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 39.32  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 262 KPTPIQSQAWPIVLQGI------DLIGVAQTGTGKTLSYLMPGFIHLDsqplareqrNGPGMLVLTPTRELALQVEAECS 335
Cdd:cd17918    15 SLTKDQAQAIKDIEKDLhspepmDRLLSGDVGSGKTLVALGAALLAYK---------NGKQVAILVPTEILAHQHYEEAR 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907194079 336 KYsYGDLKSVCVYGggdrdGQIQDVSKGVDIIIATPGRLNDLqmnnfVNLKSVTYLVLDEADKM 399
Cdd:cd17918    86 KF-LPFINVELVTG-----GTKAQILSGISLLVGTHALLHLD-----VKFKNLDLVIVDEQHRF 138
KH-I_BTR1_rpt1 cd22513
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
71-106 3.08e-03

first 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 first one.


Pssm-ID: 411941 [Multi-domain]  Cd Length: 73  Bit Score: 36.65  E-value: 3.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN 106
Cdd:cd22513     6 LLVSNAAAGSVIGKGGATINDFQAQSGARIQLSRAQ 41
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
79-102 3.14e-03

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


Pssm-ID: 411948 [Multi-domain]  Cd Length: 72  Bit Score: 36.54  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|....
gi 1907194079  79 GAVIGRGGSKIREIQNTTNTRIQV 102
Cdd:cd22520    14 GSLIGKAGSKIKEIRESTGAQVQV 37
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
73-127 3.19e-03

seventh 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 seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 36.14  E-value: 3.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAE-IKIFGNKAMQTKAKTVI 127
Cdd:cd22452     8 VSPRYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDvITLRGTKEGVEKAEEMI 63
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
73-106 3.79e-03

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 36.42  E-value: 3.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN 106
Cdd:cd22404     7 VPNSAISRVIGRGGCNINAIREVSGAHIEIDKQK 40
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
71-133 3.99e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; 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. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 36.41  E-value: 3.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194079  71 FGVKNDVVGAVIGRGGSKIREIQNTTNTRIQVIK---GNPEAEIKIFGNKAMQTKAKTVIDNVVKK 133
Cdd:cd22480     5 YKVPDKMVGFIIGRGGEQISRIQLESGCKIQIAPdsgGMPERPCVLTGTPESIEQAKRLLGQIVDR 70
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
78-102 4.42e-03

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


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 36.08  E-value: 4.42e-03
                          10        20
                  ....*....|....*....|....*
gi 1907194079  78 VGAVIGRGGSKIREIQNTTNTRIQV 102
Cdd:cd22433    13 AGCIIGRAGFKIKELREKTGATIKV 37
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
76-105 4.63e-03

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 36.77  E-value: 4.63e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907194079  76 DVVGAVIGRGGSKIREIQNTTNTRIQvIKG 105
Cdd:cd22386    19 NVRGKLIGPGGSNVKHIQQETGAKVQ-LRG 47
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
78-110 5.20e-03

first 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 KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 35.66  E-value: 5.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907194079  78 VGAVIGRGGSKIREIQNTTNTRIQVIKGNPEAE 110
Cdd:cd22459    13 AGSVIGKGGEIIKQLRQETGARIKVEDGVPGTE 45
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
79-102 5.42e-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: 5.42e-03
                          10        20
                  ....*....|....*....|....
gi 1907194079  79 GAVIGRGGSKIREIQNTTNTRIQV 102
Cdd:cd02396    14 GSLIGKGGSKIKEIRESTGASVQV 37
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
78-116 5.88e-03

fourth 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 fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 35.68  E-value: 5.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907194079  78 VGAVIGRGGSKIREIQNTTNTRIQVIK--GNPEAE---IKIFGN 116
Cdd:cd22403    11 VGRIIGKGGQNVRELQRLTGAIIKLPRdqTPDEGDevpVEIIGN 54
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
81-117 6.43e-03

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


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 35.75  E-value: 6.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907194079  81 VIGRGGSKIREIQNTTNTRIQVIKGNPEA-EIKIFGNK 117
Cdd:cd22406    19 ILGKKGKKLQELELKTATKIVIPRQEDNSdEIKITGTK 56
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
485-578 6.60e-03

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 38.05  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 485 KDKVIVFVSR---KAVADHLSSDLILRHISVESLHgnreqSDREKALENFKTGKVRILIATdlAS------RGLDV-HDI 554
Cdd:cd18798    24 GDGGLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGV--ASyygvlvRGIDLpERI 96
                          90       100
                  ....*....|....*....|....
gi 1907194079 555 THVYNYDFPrnIEEYVHRVGRTGR 578
Cdd:cd18798    97 KYAIFYGVP--VTTYIQASGRTSR 118
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
246-311 7.44e-03

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 39.42  E-value: 7.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194079 246 QSYPEVMENIKraGFqKPTPIQSQ-AWPI--VLQGIDL----IGVAQ--TGTGKTLSYLMPGFihldsqPLAREQ 311
Cdd:PRK11747   12 QAYKALQEQLP--GF-IPRAGQRQmIAEVakTLAGEYLkdgrILVIEagTGVGKTLSYLLAGI------PIARAE 77
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
73-106 7.78e-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: 35.29  E-value: 7.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907194079  73 VKNDVVGAVIGRGGSKIREIQNTTNTRIQVIKGN 106
Cdd:cd22460     6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEE 39
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
283-396 8.73e-03

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 36.90  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194079 283 VAQTGTGKTLSylmpgfihldSQPLAREQRNGPgMLVLTPTRELALQVEAECSKYSYGDlkSVCVYGGGDRDGQIqdvsk 362
Cdd:cd17926    24 VLPTGSGKTLT----------ALALIAYLKELR-TLIVVPTDALLDQWKERFEDFLGDS--SIGLIGGGKKKDFD----- 85
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907194079 363 GVDIIIATPGRLNDLQMNNFVNLKSVTYLVLDEA 396
Cdd:cd17926    86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
 
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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