NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24644479|ref|NP_524243|]
View 

Rm62, isoform A [Drosophila melanogaster]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 1000205)

DEAD/DEAH box helicase family protein such as a DEAD/DEAH box-containing ATP-dependent helicase, which catalyzes the unwinding of DNA or RNA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
231-669 0e+00

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


The actual alignment was detected with superfamily member PTZ00110:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 545  Bit Score: 604.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  231 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 306
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  307 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 386
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  387 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 466
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  467 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 545
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  546 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSN 625
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 24644479  626 TKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLArNSRY 669
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLS-NERS 515
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
231-669 0e+00

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 604.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  231 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 306
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  307 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 386
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  387 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 466
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  467 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 545
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  546 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSN 625
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 24644479  626 TKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLArNSRY 669
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLS-NERS 515
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
283-658 3.90e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 453.45  E-value: 3.90e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgDGPIALVLAP 362
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 442
Cdd:COG0513  80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 443 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANhNIRQVVDVCDEFSKEEKLKTLLSD 522
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLRD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 523 iydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYV 602
Cdd:COG0513 239 -----EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644479 603 INFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTknnAKQAKALVDVLREANQEINP 658
Cdd:COG0513 314 INYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT---PDERRLLRAIEKLIGQKIEE 366
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
292-488 5.38e-147

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: 426.40  E-value: 5.38e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 451
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24644479 452 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
305-476 7.16e-60

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: 199.01  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   305 TAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAPTRELAQQIQQVATEFGSSSYVR 384
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   385 NTCVFGGAPKGGQMRDLqRGCEIVIATPGRLIDFLSAgSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 464
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 24644479   465 WSATWPKEVKQL 476
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
296-503 1.54e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 188.47  E-value: 1.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479    296 IRRQGYKAPTAIQAQGWPIAMSG-SNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVA 374
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479    375 TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIV 453
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24644479    454 SQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlelSANHNIRQV 503
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
231-669 0e+00

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 604.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  231 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 306
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  307 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 386
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  387 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 466
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  467 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 545
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  546 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSN 625
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 24644479  626 TKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLArNSRY 669
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLS-NERS 515
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
283-658 3.90e-154

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 453.45  E-value: 3.90e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgDGPIALVLAP 362
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 442
Cdd:COG0513  80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 443 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANhNIRQVVDVCDEFSKEEKLKTLLSD 522
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLRD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 523 iydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYV 602
Cdd:COG0513 239 -----EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644479 603 INFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTknnAKQAKALVDVLREANQEINP 658
Cdd:COG0513 314 INYDLPEDPEDYVHRIGRTGRAGAEGTAISLVT---PDERRLLRAIEKLIGQKIEE 366
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
292-488 5.38e-147

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: 426.40  E-value: 5.38e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 451
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24644479 452 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
235-490 8.95e-139

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: 408.24  E-value: 8.95e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 235 DFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQV-PNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWP 313
Cdd:cd18050  15 DLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGcPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 314 IAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAP 393
Cdd:cd18050  95 LALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 394 KGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEV 473
Cdd:cd18050 175 KGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEV 254
                       250
                ....*....|....*..
gi 24644479 474 KQLAEDFLGNYIQINIG 490
Cdd:cd18050 255 RQLAEDFLRDYVQINIG 271
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
260-491 3.14e-136

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: 400.54  E-value: 3.14e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 260 EVQRYREEQEITVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILP 338
Cdd:cd18049   2 EVEQYRRSKEITVRGHnCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 339 AIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDF 418
Cdd:cd18049  82 AIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644479 419 LSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGS 491
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
292-487 2.18e-98

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 301.28  E-value: 2.18e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINnQQPLQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLL-PEPKKKGRGPQALVLAPTRELAMQIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 451
Cdd:cd00268  80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24644479 452 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
271-487 1.06e-94

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: 292.74  E-value: 1.06e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 271 TVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPL 349
Cdd:cd17953   1 KVRGKdCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 350 QRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGS---TNL 426
Cdd:cd17953  81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644479 427 KRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
282-664 1.42e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 300.95  E-value: 1.42e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  282 DFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgdGPIALVLA 361
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  362 PTRELAQQiqqVATEfgsssyVR-------NTCVF---GGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTY 431
Cdd:PRK11776  80 PTRELADQ---VAKE------IRrlarfipNIKVLtlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  432 LVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLElsANHNIRQVVDVCDEFS 511
Cdd:PRK11776 151 LVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  512 KEEKLKTLLSDiydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 591
Cdd:PRK11776 229 RLPALQRLLLH-----HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644479  592 RGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKALVDVLreaNQEIN----PALENLA 664
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYL---GRKLNweplPSLSPLS 377
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
292-487 7.24e-93

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: 287.00  E-value: 7.24e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 451
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24644479 452 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
282-633 4.64e-85

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 275.28  E-value: 4.64e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  282 DFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQqPLQRGDGPIALVLA 361
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDF-PRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  362 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRML 441
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  442 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKE-VKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCDefSKEEKLKtLL 520
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEP-SRRERKKIHQWYYRAD--DLEHKTA-LL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  521 SDIYdTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIK 600
Cdd:PRK11192 237 CHLL-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
                        330       340       350
                 ....*....|....*....|....*....|...
gi 24644479  601 YVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAF 633
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
283-490 9.69e-85

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: 266.66  E-value: 9.69e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDG----PIA 357
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLlEDGPPSVGRGRrkayPSA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 358 LVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 437
Cdd:cd17967  82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24644479 438 DRMLDMGFEPQIRKIVSQ----IRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 490
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
292-656 2.55e-82

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 268.99  E-value: 2.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPI-ALVLAPTRELAQQI 370
Cdd:PRK10590  12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  371 QQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIR 450
Cdd:PRK10590  92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  451 KIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLElSANHNIRQVVDVCDEFSKEEKLKTLLSDiydtsESP 530
Cdd:PRK10590 172 RVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKRELLSQMIGK-----GNW 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  531 GKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQN 610
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 24644479  611 SEDYIHRIGRTGRSNTKGTSFAFFTknnAKQAKALVDVLREANQEI 656
Cdd:PRK10590 326 PEDYVHRIGRTGRAAATGEALSLVC---VDEHKLLRDIEKLLKKEI 368
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
292-487 9.27e-79

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: 250.07  E-value: 9.27e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINnQQPLQRG--DGPIALVLAPTRELAQQ 369
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLD-LQPIPREqrNGPGVLVLTPTRELALQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 370 IQQVATEFGSSSYvRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQI 449
Cdd:cd17958  80 IEAECSKYSYKGL-KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24644479 450 RKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
246-662 5.64e-77

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 256.64  E-value: 5.64e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  246 FYQEHPNVANR-SPYEVQRYREEQEITVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVG 323
Cdd:PLN00206  84 FYVRDPGSTSGlSSSQAELLRRKLEIHVKGEaVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  324 IAKTGSGKTLGYILPAIVH---INNQQPLQRgDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRD 400
Cdd:PLN00206 164 SADTGSGKTASFLVPIISRcctIRSGHPSEQ-RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYR 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  401 LQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVsQIRPDRQTLMWSATWPKEVKQLAEDF 480
Cdd:PLN00206 243 IQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSL 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  481 LGNYIQINIGSLElSANHNIRQVVDVCDefSKEEKLKtlLSDIYDTSE---SPGkiIIFVETKRRVDNLVRFIR-SFGVR 556
Cdd:PLN00206 322 AKDIILISIGNPN-RPNKAVKQLAIWVE--TKQKKQK--LFDILKSKQhfkPPA--VVFVSSRLGADLLANAITvVTGLK 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  557 CGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTK 636
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
                        410       420
                 ....*....|....*....|....*.
gi 24644479  637 NNAKQAKALVDVLREANQEINPALEN 662
Cdd:PLN00206 475 EDRNLFPELVALLKSSGAAIPRELAN 500
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
283-659 5.66e-77

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 255.22  E-value: 5.66e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDG-PIALVL 360
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlQTPPPKERYMGePRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  361 APTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQ-RGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 439
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  440 MLDMGFEPQIRKIVSQIRP--DRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCdefSKEEKLK 517
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP-ENVASDTVEQHVYAV---AGSDKYK 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  518 tLLSDIYdTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVD 597
Cdd:PRK01297 325 -LLYNLV-TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644479  598 GIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKALVDVL-REANQEINPA 659
Cdd:PRK01297 403 GISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgRKISCEMPPA 465
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
276-490 1.11e-76

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: 246.88  E-value: 1.11e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 276 VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP---LQRG 352
Cdd:cd18051  16 CPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgesLPSE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 353 DG--------PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST 424
Cdd:cd18051  96 SGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKI 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 425 NLKRCTYLVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 490
Cdd:cd18051 176 GLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
276-490 6.77e-75

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: 242.57  E-value: 6.77e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 276 VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLQRGDG 354
Cdd:cd18052  38 PPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTASSFSE 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 355 ---PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTY 431
Cdd:cd18052 118 vqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKY 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24644479 432 LVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVKQLAEDFL-GNYIQINIG 490
Cdd:cd18052 198 LILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVG 261
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
279-633 1.50e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 251.41  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  279 PIQD--FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPL--QRGDG 354
Cdd:PRK04537   5 PLTDltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  355 PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST-NLKRCTYLV 433
Cdd:PRK04537  85 PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  434 LDEADRMLDMGFEPQIRKIVSQI--RPDRQTLMWSATWPKEVKQLAEDFLgNYIQINIGSLELSANHNIRQVVdvcdEFS 511
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHM-NEPEKLVVETETITAARVRQRI----YFP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  512 KEEKLKTLLSDIYDTSESpGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 591
Cdd:PRK04537 240 ADEEKQTLLLGLLSRSEG-ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 24644479  592 RGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAF 633
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
281-633 6.04e-72

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 240.26  E-value: 6.04e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  281 QDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYiLPAIVH--INNQQPLQR-GDGPIA 357
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTATFHylLSHPAPEDRkVNQPRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  358 LVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 437
Cdd:PRK04837  87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  438 DRMLDMGFEPQIRKIVSQIRP--DRQTLMWSATWPKEVKQLAEDFLGN--YIQInigSLELSANHNIRQVVdvcdeF--S 511
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNpeYVEV---EPEQKTGHRIKEEL-----FypS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  512 KEEKLKTLLSDIYDtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 591
Cdd:PRK04837 239 NEEKMRLLQTLIEE--EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 24644479  592 RGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAF 633
Cdd:PRK04837 317 RGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PTZ00424 PTZ00424
helicase 45; Provisional
280-656 6.74e-69

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 231.25  E-value: 6.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  280 IQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHIN-NQQPLQrgdgpiAL 358
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDyDLNACQ------AL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  359 VLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEAD 438
Cdd:PTZ00424 101 ILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  439 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSAnHNIRQVVDVCDefSKEEKLKT 518
Cdd:PTZ00424 181 EMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFYVAVE--KEEWKFDT 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  519 LLsDIYDTSeSPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDG 598
Cdd:PTZ00424 258 LC-DLYETL-TITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644479  599 IKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKalvDVLREANQEI 656
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLK---EIERHYNTQI 390
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
292-487 1.79e-67

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: 221.42  E-value: 1.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQ---RGDGPIALVLAPTRELAQ 368
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetKDDGPYALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 369 QIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQ 448
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24644479 449 IRKI-----VSQIRPD---------------RQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17945 161 VTKIldampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
283-633 1.50e-65

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 228.58  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhiNNQQPLQRGdgPIALVLAP 362
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL---HNLDPELKA--PQILVLAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  363 TRELAQQIQQVATEFgsSSYVRNTCV---FGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 439
Cdd:PRK11634  83 TRELAVQVAEAMTDF--SKHMRGVNVvalYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  440 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCDEFSKEEKLKTL 519
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  520 LSdiydtSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGI 599
Cdd:PRK11634 240 LE-----AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
                        330       340       350
                 ....*....|....*....|....*....|....
gi 24644479  600 KYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAF 633
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
305-476 7.16e-60

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: 199.01  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   305 TAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAPTRELAQQIQQVATEFGSSSYVR 384
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   385 NTCVFGGAPKGGQMRDLqRGCEIVIATPGRLIDFLSAgSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 464
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 24644479   465 WSATWPKEVKQL 476
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
292-488 1.43e-58

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: 196.79  E-value: 1.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQ---PLQRGDGPIALVLAPTRELAQ 368
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 369 QIQQVATEF------GSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 442
Cdd:cd17951  81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24644479 443 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
500-634 3.78e-57

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 190.41  E-value: 3.78e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 500 IRQVVDVCDEFSKEEKLKTLLsdiyDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSG 579
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLL----LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24644479 580 KSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFF 634
Cdd:cd18787  77 KVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
296-503 1.54e-55

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 188.47  E-value: 1.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479    296 IRRQGYKAPTAIQAQGWPIAMSG-SNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVA 374
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479    375 TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIV 453
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24644479    454 SQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlelSANHNIRQV 503
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
292-477 5.33e-55

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: 187.41  E-value: 5.33e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGW-PIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQI 370
Cdd:cd17964   5 LLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 371 qqvATEFGS-SSYVRNT---CVFGGAPKGGQMRDLQR-GCEIVIATPGRLIDFLS--AGSTNLKRCTYLVLDEADRMLDM 443
Cdd:cd17964  85 ---AAEAKKlLQGLRKLrvqSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDM 161
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 24644479 444 GFEPQIRKIVSQIRP----DRQTLMWSATWPKEVKQLA 477
Cdd:cd17964 162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIA 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
283-487 1.01e-53

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 183.67  E-value: 1.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLqrgdgpIALVLA 361
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAlLENPQRF------FALVLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 362 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSagST---NLKRCTYLVLDEAD 438
Cdd:cd17954  76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLE--NTkgfSLKSLKFLVMDEAD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24644479 439 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
300-487 1.78e-52

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: 180.86  E-value: 1.78e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 300 GYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQRGDGPIALVLAPTRELAQQIQQVATEFG 378
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrVDRSDGTLALVLVPTRELALQIYEVLEKLL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 379 SSS-YVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFL-SAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQI 456
Cdd:cd17949  90 KPFhWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24644479 457 R-------------PDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17949 170 DdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
283-481 2.80e-51

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: 177.03  E-value: 2.80e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPaIVHINNQQPLqrgdGPIALVLAP 362
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSEDPY----GIFALVLTP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST---NLKRCTYLVLDEADR 439
Cdd:cd17955  76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24644479 440 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFL 481
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFG 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
292-488 2.19e-50

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: 174.80  E-value: 2.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQrgdGPIALVLAPTRELAQQIQ 371
Cdd:cd17959  12 LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV---GARALILSPTRELALQTL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 451
Cdd:cd17959  89 KVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHE 168
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24644479 452 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17959 169 ILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
292-490 2.53e-49

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: 171.62  E-value: 2.53e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQqplQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVATEFGSSSYVRnTCVF--GGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQI 449
Cdd:cd17957  78 RELLKLSKGTGLR-IVLLskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24644479 450 RKIVSQIR-PDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 490
Cdd:cd17957 157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
292-477 4.09e-49

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: 170.90  E-value: 4.09e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAI---VHINNQQPLQRgdgpiALVLAPTRELAQ 368
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILerlLYRPKKKAATR-----VLVLVPTRELAM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 369 QIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFL-SAGSTNLKRCTYLVLDEADRMLDMGFEP 447
Cdd:cd17947  76 QCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFAD 155
                       170       180       190
                ....*....|....*....|....*....|
gi 24644479 448 QIRKIVSQIRPDRQTLMWSATWPKEVKQLA 477
Cdd:cd17947 156 ELKEILRLCPRTRQTMLFSATMTDEVKDLA 185
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
283-488 1.07e-47

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 167.09  E-value: 1.07e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQrgdgpiALVLA 361
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDvIQ------ALILV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 362 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPkggqMRD----LQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 437
Cdd:cd17940  75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTS----LRDdimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEA 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24644479 438 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17940 151 DKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
296-487 7.08e-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: 7.08e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 296 IRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVhinnqQPLQRGDGPIALVLAPTRELAQQIQQVAT 375
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII-----RCLTEHRNPSALILTPTRELAVQIEDQAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 376 EFGSSS-YVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVS 454
Cdd:cd17962  80 ELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                       170       180       190
                ....*....|....*....|....*....|...
gi 24644479 455 QIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17962 160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
292-468 1.10e-45

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: 162.79  E-value: 1.10e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGS-NFVGIAKTGSGKTLGYILPAIVHINNQQpLQRGD-----GPIALVLAPTRE 365
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQK-SSNGVggkqkPLRALILTPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 366 LAQQIQQVATEFGSSSYVRNTCVFGG--APKggQMRDLQRGCEIVIATPGRLIDFLSAGST---NLKRCTYLVLDEADRM 440
Cdd:cd17946  80 LAVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRM 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24644479 441 LDMG-FEpQIRKIVSQI-------RPDRQTLMWSAT 468
Cdd:cd17946 158 LEKGhFA-ELEKILELLnkdragkKRKRQTFVFSAT 192
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
292-488 8.48e-45

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 159.28  E-value: 8.48e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 371
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 372 QVA---TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLS--AGSTNLKRCTYLVLDEADRMLDMGFE 446
Cdd:cd17960  81 EVLqsfLEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24644479 447 PQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 488
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
294-489 1.91e-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: 158.22  E-value: 1.91e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 294 KEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQpLQRGDGPIALVLAPTRELAQQIQQV 373
Cdd:cd17941   3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 374 ATEFGSSSYVRNTCVFGGapkggqmRDLQR------GCEIVIATPGRLIDFL----SAGSTNLKrctYLVLDEADRMLDM 443
Cdd:cd17941  82 LRKVGKYHSFSAGLIIGG-------KDVKEekerinRMNILVCTPGRLLQHMdetpGFDTSNLQ---MLVLDEADRILDM 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24644479 444 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINI 489
Cdd:cd17941 152 GFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
293-477 7.30e-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: 156.37  E-value: 7.30e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 293 MKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRgDGPIALVLAPTRELAQQIQQ 372
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 373 VATE---FGSSSYvrnTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGS----TNLKrctYLVLDEADRMLDMGF 445
Cdd:cd17942  81 VAKEllkYHSQTF---GIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGF 154
                       170       180       190
                ....*....|....*....|....*....|..
gi 24644479 446 EPQIRKIVSQIRPDRQTLMWSATWPKEVKQLA 477
Cdd:cd17942 155 EEEMRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
288-487 1.09e-38

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


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 142.08  E-value: 1.09e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 288 LPDYVMKEIRRQGYKAPTAIQAQG-WPIaMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQrgdgpiALVLAPTRE 365
Cdd:cd17939   4 LSEDLLRGIYAYGFEKPSAIQQRAiVPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVReTQ------ALVLAPTRE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 366 LAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGF 445
Cdd:cd17939  77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24644479 446 EPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
288-487 2.99e-38

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: 140.79  E-value: 2.99e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 288 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLqrgdgPIALVLAPTRE 365
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS-----PQALCLAPTRE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 366 LAQQIQQVATEFGSSSYVRNTCVFGG--APKGGQMRDlqrgcEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDM 443
Cdd:cd17963  76 LARQIGEVVEKMGKFTGVKVALAVPGndVPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDT 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24644479 444 -GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17963 151 qGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
292-487 1.57e-36

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 135.85  E-value: 1.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAI--VHINNQQPLqrgdgpiALVLAPTRELAQQ 369
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALesLDLERRHPQ-------VLILAPTREIAVQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 370 IQQVATEFGSSSYVRNTCVF-GGAPkggQMRDLQR--GCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFE 446
Cdd:cd17943  74 IHDVFKKIGKKLEGLKCEVFiGGTP---VKEDKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24644479 447 PQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17943 151 KDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
283-478 7.31e-36

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: 134.37  E-value: 7.31e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQrgdgpiALVLAP 362
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL------QIVV------ALILEP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQ----IQQVATEFGSSSyVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEAD 438
Cdd:cd17938  69 SRELAEQtyncIENFKKYLDNPK-LRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24644479 439 RMLDMGFEPQIRKIVSQI-----RPDR-QTLMWSATWPK-EVKQLAE 478
Cdd:cd17938 148 RLLSQGNLETINRIYNRIpkitsDGKRlQVIVCSATLHSfEVKKLAD 194
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
288-483 1.36e-35

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 133.48  E-value: 1.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 288 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDGPIALVLAPTREL 366
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 367 AQQIQQVATEF--GSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST-NLKRCTYLVLDEADRMLDM 443
Cdd:cd17961  81 AQQVSKVLEQLtaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24644479 444 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGN 483
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
511-625 1.57e-35

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: 130.02  E-value: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   511 SKEEKLKTLLSdiydtSESPGKIIIFVETKRRVDnLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVA 590
Cdd:pfam00271   1 EKLEALLELLK-----KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24644479   591 ARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSN 625
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
307-488 3.13e-35

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: 132.28  E-value: 3.13e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 307 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHIN-NQQPLQRGDGPIALVLAPTRELAQQiqqVATEFGS-SSYVR 384
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQ---VTKDFKDiTRKLS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 385 NTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVS-QIRPDR--- 460
Cdd:cd17944  93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSedn 172
                       170       180       190
                ....*....|....*....|....*....|
gi 24644479 461 -QTLMWSATWPKEVKQLAEDFL-GNYIQIN 488
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMkSQYEQVD 202
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
283-487 2.95e-34

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: 129.49  E-value: 2.95e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgdGPIALVLAP 362
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK-----ATQALVLAP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 442
Cdd:cd18046  76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24644479 443 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
296-479 3.73e-32

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: 124.79  E-value: 3.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 296 IRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRG--DGPIALVLAPTRELAQQIQQV 373
Cdd:cd17948   5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQIGSV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 374 ATEFGSSSYVRNTCVFGGAPKGgQMRDLQRG-CEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKI 452
Cdd:cd17948  85 AQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHF 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24644479 453 VSQIR-------------PDRQTLMWSATWPKEVKQLAED 479
Cdd:cd17948 164 LRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
283-487 7.34e-31

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: 120.14  E-value: 7.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQRGDGPI-ALVLA 361
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVsVLVIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 362 PTRELAQQIQQVATEFgsSSY---VRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 437
Cdd:cd17950  78 HTRELAFQISNEYERF--SKYmpnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDEC 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24644479 438 DRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17950 156 DKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
HELICc smart00490
helicase superfamily c-terminal domain;
544-623 3.76e-29

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 110.76  E-value: 3.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479    544 DNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGR 623
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
283-487 2.34e-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: 109.86  E-value: 2.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 283 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAP 362
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV-----RETQALILSP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 363 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 442
Cdd:cd18045  76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24644479 443 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
292-446 2.20e-22

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: 96.55  E-value: 2.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 292 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGI---------AKTGSGKTLGYILPaIVhinnqQPLQRGDGPI--ALVL 360
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTPPyrpgdlcvsAPTGSGKTLAYVLP-IV-----QALSKRVVPRlrALIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 361 APTRELAQQIQQVATEFGSSSYVRnTCVFGGAPK-GGQMRDLQRGCE--------IVIATPGRLIDFLSAGST-NLKRCT 430
Cdd:cd17956  75 VPTKELVQQVYKVFESLCKGTGLK-VVSLSGQKSfKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPGfTLKHLR 153
                       170
                ....*....|....*.
gi 24644479 431 YLVLDEADRMLDMGFE 446
Cdd:cd17956 154 FLVIDEADRLLNQSFQ 169
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
321-487 2.99e-21

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 93.60  E-value: 2.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 321 FVGIAKTGSGKTLGYILPAIVHINNQ------------QPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCV 388
Cdd:cd17965  64 FLLAAETGSGKTLAYLAPLLDYLKRQeqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 389 fgGAPKGGQMRDLQR----GCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 464
Cdd:cd17965 144 --SSGFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
                       170       180
                ....*....|....*....|...
gi 24644479 465 WSATWPKEVKQLAEDFLGNYIQI 487
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
318-620 3.94e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 91.62  E-value: 3.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 318 GSNFVGIAKTGSGKTlgYILPAIVHinnqqplQRGDGPIALVLAPTRELAQQIQQVATEFgsssyvrntcvFGGAPKGGQ 397
Cdd:COG1061 100 GGRGLVVAPTGTGKT--VLALALAA-------ELLRGKRVLVLVPRRELLEQWAEELRRF-----------LGDPLAGGG 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 398 MRDlqRGCEIVIATPGRLIDFLSAGSTNlKRCTYLVLDEADRmldmGFEPQIRKIVSQIRPDRQTLMwSAT-WPKEVKQL 476
Cdd:COG1061 160 KKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpFRSDGREI 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 477 AEDFLGNyIQINIGSLELSANHNIRQV------VDVCDEFSKEEKLKTLLSDIYDTSE---------------SPGKIII 535
Cdd:COG1061 232 LLFLFDG-IVYEYSLKEAIEDGYLAPPeyygirVDLTDERAEYDALSERLREALAADAerkdkilrellrehpDDRKTLV 310
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 536 FVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYI 615
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390

                ....*
gi 24644479 616 HRIGR 620
Cdd:COG1061 391 QRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
280-478 3.67e-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: 3.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 280 IQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLqrgdgPIA 357
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 358 LVLAPTRELAQQIQQVATEFGS-SSYVRNTCVFGG--APKGGQMRdlqrgCEIVIATPGRLIDF-LSAGSTNLKRCTYLV 433
Cdd:cd18048  92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGnrPGKGTDIE-----AQIVIGTPGTVLDWcFKLRLIDVTNISVFV 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24644479 434 LDEADRMLDM-GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAE 478
Cdd:cd18048 167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAE 212
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
493-629 1.33e-17

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 87.09  E-value: 1.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 493 ELSANHNIRQVVDVCDEF----SKEEKLKTLLSDIYDTSESpGKIIIFVETKRRVDNLVRFIRSFGVRC------GAIHG 562
Cdd:COG1111 313 RLVSDPRFRKAMRLAEEAdiehPKLSKLREILKEQLGTNPD-SRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEG 391
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644479 563 DK--SQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDyPQNSE-DYIHRIGRTGRSN--------TKGT 629
Cdd:COG1111 392 DKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKRegrvvvliAKGT 468
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
281-478 7.87e-15

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 73.99  E-value: 7.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 281 QDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRgdgpiAL 358
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 359 VLAPTRELAQQIQQVATEFGsSSYVRNTCVFggAPKGGQM-RDLQRGCEIVIATPGRLIDF-LSAGSTNLKRCTYLVLDE 436
Cdd:cd18047  76 CLSPTYELALQTGKVIEQMG-KFYPELKLAY--AVRGNKLeRGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24644479 437 ADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAE 478
Cdd:cd18047 153 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQ 195
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
509-623 1.35e-13

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: 68.39  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 509 EFSKEEKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATD 588
Cdd:cd18794   9 RPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATV 88
                        90       100       110
                ....*....|....*....|....*....|....*
gi 24644479 589 VAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGR 623
Cdd:cd18794  89 AFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
510-635 5.53e-13

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: 66.85  E-value: 5.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 510 FSKEEKLKTLLSDIYDTSESPgKIIIFVETKRRVDNLVRFIRSFG-----VRCGAI--HGDKSQSERDF--------VLR 574
Cdd:cd18802   6 IPKLQKLIEILREYFPKTPDF-RGIIFVERRATAVVLSRLLKEHPstlafIRCGFLigRGNSSQRKRSLmtqrkqkeTLD 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644479 575 EFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKgtsFAFFT 635
Cdd:cd18802  85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK---YILMV 142
PRK13766 PRK13766
Hef nuclease; Provisional
493-667 9.23e-13

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 71.83  E-value: 9.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  493 ELSANHNIRQVVDVCDEFSKE----EKLKTLLSDIYDTSESPgKIIIFVETKRRVDNLVRFIRSFGVRC------GAIHG 562
Cdd:PRK13766 325 RLVEDPRFRKAVRKAKELDIEhpklEKLREIVKEQLGKNPDS-RIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDG 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  563 DK--SQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVInFDYPQNSE-DYIHRIGRTGRSN--------TKGTS- 630
Cdd:PRK13766 404 DKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI-FYEPVPSEiRSIQRKGRTGRQEegrvvvliAKGTRd 482
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24644479  631 FAFFTKNNAKQaKALVDVLREANQEINPALENLARNS 667
Cdd:PRK13766 483 EAYYWSSRRKE-KKMKEELKNLKGILNKKLQELDEEQ 518
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
288-631 1.47e-11

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: 67.94  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 288 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQRGDGPIALVLAPTRELA 367
Cdd:COG1205  41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVL------EALLEDPGATALYLYPTKALA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 368 Q-Q---IQQVATEFGSSsyVRNTCVFGGAPKgGQMRDLQRGCEIVIATPgrliDFLSAG--------STNLKRCTYLVLD 435
Cdd:COG1205 115 RdQlrrLRELAEALGLG--VRVATYDGDTPP-EERRWIREHPDIVLTNP----DMLHYGllphhtrwARFFRNLRYVVID 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 436 EA---------------DRML----DMGFEPQIrkIVSqirpdrqtlmwSATW--PKEvkqLAEDFLG------------ 482
Cdd:COG1205 188 EAhtyrgvfgshvanvlRRLRricrHYGSDPQF--ILA-----------SATIgnPAE---HAERLTGrpvtvvdedgsp 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 483 ----NYIQIN----IGSLELSANhniRQVVDVCDEFSKEEkLKTllsdiydtsespgkiIIFVETKRRVDNLVRFIR--- 551
Cdd:COG1205 252 rgerTFVLWNpplvDDGIRRSAL---AEAARLLADLVREG-LRT---------------LVFTRSRRGAELLARYARral 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 552 ---SFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVAT-------DVAarGLDVdgikyVINFDYPQNSEDYIHRIGRT 621
Cdd:COG1205 313 repDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRA 385
                       410
                ....*....|
gi 24644479 622 GRSNTKGTSF 631
Cdd:COG1205 386 GRRGQDSLVV 395
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
500-619 2.56e-11

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 61.72  E-value: 2.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 500 IRQVVDVcdefskeeKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSG 579
Cdd:cd18793   5 IEEVVSG--------KLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24644479 580 KSN--ILVATDVAARGLDVDGIKYVINFDYPQNS------EDYIHRIG 619
Cdd:cd18793  77 PDIrvFLLSTKAGGVGLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
512-625 3.19e-11

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: 61.60  E-value: 3.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 512 KEEKLKTLLSDiYDTSESPGK---IIIFVETKRRVDNLVRFIRSFGVRCGAI----HGDK------SQSERDFVLREFRS 578
Cdd:cd18801  10 KLEKLEEIVKE-HFKKKQEGSdtrVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRK 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24644479 579 GKSNILVATDVAARGLDVDGIKYVINFDyPQNSE-DYIHRIGRTGRSN 625
Cdd:cd18801  89 GGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGRKR 135
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
306-623 4.53e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 65.93  E-value: 4.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 306 AIQAqgwpiAMSGSNFVGIAKTGSGKTLGYILPAIVhinnqqplqrGDGPiALVLAPTRELAQ-QIQQvATEFGsssyVR 384
Cdd:COG0514  25 IIEA-----VLAGRDALVVMPTGGGKSLCYQLPALL----------LPGL-TLVVSPLIALMKdQVDA-LRAAG----IR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 385 NTCVFGGAPKGGQ---MRDLQRG-CEIVIATPGRL-----IDFLSAGSTNLkrctyLVLDEA--------DrmldmgFEP 447
Cdd:COG0514  84 AAFLNSSLSAEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 448 ---QIRKIVSQIrPDRQTLMWSATWPKEV-----KQLAedfLGNyIQINIGSLelsANHNIR-QVVdvcdEFSKEEKLKT 518
Cdd:COG0514 153 dyrRLGELRERL-PNVPVLALTATATPRVradiaEQLG---LED-PRVFVGSF---DRPNLRlEVV----PKPPDDKLAQ 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 519 LLSDIYDTSESPGkiIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATdvAARGLDVD- 597
Cdd:COG0514 221 LLDFLKEHPGGSG--IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGMGIDk 296
                       330       340
                ....*....|....*....|....*..
gi 24644479 598 -GIKYVINFDYPQNSEDYIHRIGRTGR 623
Cdd:COG0514 297 pDVRFVIHYDLPKSIEAYYQEIGRAGR 323
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
318-468 5.00e-11

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: 61.27  E-value: 5.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 318 GSNFVGIAKTGSGKTLGYILPAIVHINNQqplqrgdGPIALVLAPTRELA-QQIQQVATEFGSSSYVRntcVFGGAPKGG 396
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALAlQTAERLRELFGPGIRVA---VLVGGSSAE 70
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24644479 397 QMRDLQRGCE-IVIATPGRLI-DFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK--IVSQIRPDRQTLMWSAT 468
Cdd:cd00046  71 EREKNKLGDAdIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
511-621 1.19e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 64.86  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 511 SKEEKLKTLLSDIYDTSEspgKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSN--ILVATD 588
Cdd:COG0553 533 AKLEALLELLEELLAEGE---KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLK 609
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24644479 589 VAARGLDVDGIKYVINFDYPQN------SEDYIHRIGRT 621
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLWWNpaveeqAIDRAHRIGQT 648
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
280-662 1.44e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 64.15  E-value: 1.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 280 IQDFSEVHLPDYVmkeiRRQGYKAPTAIQAQGWP-IAMSGSNFVGIAKTGSGKTL-GYIlpAIV-HINNqqplqrgdGPI 356
Cdd:COG1204   3 VAELPLEKVIEFL----KERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL--AILkALLN--------GGK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 357 ALVLAPTRELAQQIQQ----VATEFGSSSYVrntcVFGGAPKGGqmRDLQRgCEIVIATPGRLIDFLSAGSTNLKRCTYL 432
Cdd:COG1204  69 ALYIVPLRALASEKYRefkrDFEELGIKVGV----STGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 433 VLDEA------DRmldmGfePQIRKIVSQIR---PDRQTLMWSATWPkEVKQLAEDFLGNYIQINIGSLELSANHNIRQV 503
Cdd:COG1204 142 VVDEAhliddeSR----G--PTLEVLLARLRrlnPEAQIVALSATIG-NAEEIAEWLDAELVKSDWRPVPLNEGVLYDGV 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 504 VDVCDEFSKEekLKTLLSDIYDTSESPGKIIIFVETKRRV-----------------------DNLVRFIRSFG------ 554
Cdd:COG1204 215 LRFDDGSRRS--KDPTLALALDLLEEGGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSeethtn 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 555 ------VRCGAI--HGDKSQSERDFVLREFRSGKSNILVATD-VAArgldvdGI----KYVI------NFDYPQNSEDYI 615
Cdd:COG1204 293 ekladcLEKGVAfhHAGLPSELRRLVEDAFREGLIKVLVATPtLAA------GVnlpaRRVIirdtkrGGMVPIPVLEFK 366
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 24644479 616 HRIGRTGRSN--TKGTsfAFFTKNNAKQAKALVD--VLREAnQEINPALEN 662
Cdd:COG1204 367 QMAGRAGRPGydPYGE--AILVAKSSDEADELFEryILGEP-EPIRSKLAN 414
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
315-623 1.56e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.27  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  315 AMSGSNFVGIAKTGSGKTLGYILPAIVHinnqqplqrgDGpIALVLAPTRELAQ-QIQQ-----VATEFGSSSYVRNtcv 388
Cdd:PRK11057  37 VLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLMKdQVDQllangVAAACLNSTQTRE--- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  389 fggapkggQMRDLQRGC-----EIVIATPGRLI--DFL-SAGSTNLkrcTYLVLDEADRMLDMG--FEPQIRKIvSQIR- 457
Cdd:PRK11057 103 --------QQLEVMAGCrtgqiKLLYIAPERLMmdNFLeHLAHWNP---ALLAVDEAHCISQWGhdFRPEYAAL-GQLRq 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  458 --PDRQTLMWSATWPKEVKQLAEDFLG-NYIQINIGSLElsaNHNIRqvvdvcdeFSKEEKLKTLLSDIYDTSESPGKI- 533
Cdd:PRK11057 171 rfPTLPFMALTATADDTTRQDIVRLLGlNDPLIQISSFD---RPNIR--------YTLVEKFKPLDQLMRYVQEQRGKSg 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479  534 IIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSED 613
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                        330
                 ....*....|
gi 24644479  614 YIHRIGRTGR 623
Cdd:PRK11057 320 YYQETGRAGR 329
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
582-623 3.53e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 50.78  E-value: 3.53e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24644479 582 NILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGR 623
Cdd:cd18785  24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
511-634 1.16e-07

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: 51.87  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 511 SKEEKLKTLLsdiyDTSESPGKIIIFVETkrrVDNLVRFIRSFGVRcgAIHGDKSQSERDFVLREFRSGKSNILVATDVA 590
Cdd:cd18789  34 NKLRALEELL----KRHEQGDKIIVFTDN---VEALYRYAKRLLKP--FITGETPQSEREEILQNFREGEYNTLVVSKVG 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24644479 591 ARGLDVDGIKYVINFDYPQNSE-DYIHRIGRTGRSNTKGTSFAFF 634
Cdd:cd18789 105 DEGIDLPEANVAIQISGHGGSRrQEAQRLGRILRPKKGGGKNAFF 149
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
307-437 5.34e-06

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 47.26  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 307 IQAQGWPIAM-SGSNFVGIAKTGSGKTL-GYIlpAIVHINNQQplqrgdGPIALVLAPTRELAQQIQQVATEFGSSSYVR 384
Cdd:cd17921   5 IQREALRALYlSGDSVLVSAPTSSGKTLiAEL--AILRALATS------GGKAVYIAPTRALVNQKEADLRERFGPLGKN 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24644479 385 NTCVFGGAPKGGQMrdlQRGCEIVIATPGRLiDFLS--AGSTNLKRCTYLVLDEA 437
Cdd:cd17921  77 VGLLTGDPSVNKLL---LAEADILVATPEKL-DLLLrnGGERLIQDVRLVVVDEA 127
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
327-437 6.62e-06

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: 46.53  E-value: 6.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 327 TGSGKTLgYILPAIVHinnqqplqRGDGPIaLVLAPTRELAQQIQQVATEFGSSSYVrntCVFGGAPKggqmrDLQRGCE 406
Cdd:cd17926  27 TGSGKTL-TALALIAY--------LKELRT-LIVVPTDALLDQWKERFEDFLGDSSI---GLIGGGKK-----KDFDDAN 88
                        90       100       110
                ....*....|....*....|....*....|.
gi 24644479 407 IVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 437
Cdd:cd17926  89 VVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
308-437 7.29e-06

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: 47.19  E-value: 7.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 308 QAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSY--VRN 385
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEA------LLRDPGSRALYLYPTKALAQDQLRSLRELLEQLGlgIRV 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644479 386 TCVFGGAPKGGQMRDLQRGCEIVIATP-----------GRLIDFLSagstNLKrctYLVLDEA 437
Cdd:cd17923  79 ATYDGDTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
316-623 9.72e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 49.12  E-value: 9.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   316 MSGSNFVGIAKTGSGKTLGYILPAIVHinnqqplqrgdGPIALVLAPTRELAQ-QIQQVATEFGSSSYVRntcvfGGAPK 394
Cdd:PLN03137  473 MSGYDVFVLMPTGGGKSLTYQLPALIC-----------PGITLVISPLVSLIQdQIMNLLQANIPAASLS-----AGMEW 536
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   395 GGQMRDLQRGC------EIVIATPG---------RLIDFLSAGSTnLKRctyLVLDEADRMLDMG--FEPQIRK--IVSQ 455
Cdd:PLN03137  537 AEQLEILQELSseyskyKLLYVTPEkvaksdsllRHLENLNSRGL-LAR---FVIDEAHCVSQWGhdFRPDYQGlgILKQ 612
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   456 IRPDRQTLMWSATWPKEVKQLAEDFLG--NYI----QINIGSLELSANHNIRQVVDVCDEFSKEEKlktllsdiYDTSEs 529
Cdd:PLN03137  613 KFPNIPVLALTATATASVKEDVVQALGlvNCVvfrqSFNRPNLWYSVVPKTKKCLEDIDKFIKENH--------FDECG- 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   530 pgkiIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQ 609
Cdd:PLN03137  684 ----IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPK 759
                         330
                  ....*....|....
gi 24644479   610 NSEDYIHRIGRTGR 623
Cdd:PLN03137  760 SIEGYHQECGRAGR 773
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
519-623 1.84e-05

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 45.70  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 519 LLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDG 598
Cdd:cd18790  16 LLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPE 95
                        90       100       110
                ....*....|....*....|....*....|
gi 24644479 599 IKYVINFD-----YPQNSEDYIHRIGRTGR 623
Cdd:cd18790  96 VSLVAILDadkegFLRSETSLIQTIGRAAR 125
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
501-623 2.25e-05

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 45.24  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 501 RQVVDVCDEFSKEEKLKTLLSD-------IYDTSESPGKIIIFVETKRRVDNLVRFIRsfGVrcGAIHGDKSQSERDFVL 573
Cdd:cd18795   7 EYVLGFNGLGIKLRVDVMNKFDsdiivllKIETVSEGKPVLVFCSSRKECEKTAKDLA--GI--AFHHAGLTREDRELVE 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644479 574 REFRSGKSNILVATDVAARGLD-------VDGIKYVINFDYPQ-NSEDYIHRIGRTGR 623
Cdd:cd18795  83 ELFREGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKGYRElSPLEYLQMIGRAGR 140
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
532-620 5.28e-05

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 42.93  E-value: 5.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 532 KIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSER-DFVLREFRSGKS--NILVATDVAARGLDVDGIKYVInFDYP 608
Cdd:cd18799   8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-FLRP 86
                        90
                ....*....|...
gi 24644479 609 QNSED-YIHRIGR 620
Cdd:cd18799  87 TESRTlFLQMLGR 99
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
558-633 1.22e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.10  E-value: 1.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24644479 558 GAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRI-GRTGRSNTKgtSFAF 633
Cdd:cd18811  65 GLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQ--SYCL 139
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
301-372 1.22e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.48  E-value: 1.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644479 301 YKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLQRGDGPIALVLAPTRELAQQIQQ 372
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLKALANDIER 94
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
463-623 1.32e-04

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 44.73  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 463 LMwSATWPKEVKQLAEDFLgnyIQINIGSLELSANHNIRQVVDVCDEFSKEeklkTLLSDIYDTSESPGKIIIFVETKRR 542
Cdd:cd09639 159 LM-SATLPKFLKEYAEKIG---YVEENEPLDLKPNERAPFIKIESDKVGEI----SSLERLLEFIKKGGSVAIIVNTVDR 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 543 VDNLVRFIRSFGVRCGAI--HGDKSQSER----DFVLREFRSGKSNILVATDVAARGLDVDgIKYVINFDYPQNSedYIH 616
Cdd:cd09639 231 AQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDIS-VDVMITELAPIDS--LIQ 307

                ....*..
gi 24644479 617 RIGRTGR 623
Cdd:cd09639 308 RLGRLHR 314
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
556-641 2.07e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 42.25  E-value: 2.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 556 RCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVI-----NFDYPQnsedyIHRI-GRTGRSNTKgt 629
Cdd:cd18792  62 RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGLSQ-----LHQLrGRVGRGKHQ-- 134
                        90
                ....*....|..
gi 24644479 630 SFAFFTKNNAKQ 641
Cdd:cd18792 135 SYCYLLYPDPKK 146
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
310-475 2.85e-04

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: 42.63  E-value: 2.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 310 QGWPIA--MSGSNFVGIAKTGSGKTLGYILPAIVhinnqqpLQRGDGPIALVLAPTreLAQQIQQVAtefGSSSYVRNTC 387
Cdd:cd18018  17 QEEAIArlLSGRSTLVVLPTGAGKSLCYQLPALL-------LRRRGPGLTLVVSPL--IALMKDQVD---ALPRAIKAAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 388 VFGGAPKGGQMRDLQR----GCEIVIATPGRLI--DFLSAGSTnLKRCTYLVLDEADRMLDMG--FEP---QIRKIVSQI 456
Cdd:cd18018  85 LNSSLTREERRRILEKlragEVKILYVSPERLVneSFRELLRQ-TPPISLLVVDEAHCISEWShnFRPdylRLCRVLREL 163
                       170
                ....*....|....*....
gi 24644479 457 RPDRQTLMWSATWPKEVKQ 475
Cdd:cd18018 164 LGAPPVLALTATATKRVVE 182
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
555-641 4.21e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 41.18  E-value: 4.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 555 VRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRI-GRTGRSNTKGtsFAF 633
Cdd:cd18810  52 ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERA--YAY 129

                ....*...
gi 24644479 634 FTKNNAKQ 641
Cdd:cd18810 130 FLYPDQKK 137
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
554-589 1.46e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 41.96  E-value: 1.46e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 24644479 554 GVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDV 589
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
553-589 1.85e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 41.67  E-value: 1.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 24644479  553 FGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDV 589
Cdd:PRK10917 504 PELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTV 540
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
324-439 2.21e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 39.81  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 324 IAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIaLVLAPTRELAQQIQQVATEFGSSSyvrNTCV-FGGAPKGGQMRDLQ 402
Cdd:cd18035  22 VLPTGLGKTIIAILVAADR------LTKKGGKV-LILAPSRPLVEQHAENLKRVLNIP---DKITsLTGEVKPEERAERW 91
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 24644479 403 RGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 439
Cdd:cd18035  92 DASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
306-475 2.97e-03

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 39.44  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 306 AIQAqgwpiAMSGSNFVGIAKTGSGKTLGYILPAIVhinnqqplqrgDGPIALVLAPTRELAQ-QIQQvATEFGsssyVR 384
Cdd:cd17920  20 AINA-----VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDR-LQQLG----IR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479 385 NTCVFGGAPKGGQMRDLQR----GCEIVIATPGRL-----IDFLsAGSTNLKRCTYLVLDEADRMLDMG--FEPQIRKIv 453
Cdd:cd17920  79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdfLELL-QRLPERKRLALIVVDEAHCVSQWGhdFRPDYLRL- 156
                       170       180
                ....*....|....*....|....*
gi 24644479 454 SQIR---PDRQTLMWSATWPKEVKQ 475
Cdd:cd17920 157 GRLRralPGVPILALTATATPEVRE 181
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
324-378 5.34e-03

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 39.97  E-value: 5.34e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24644479 324 IAKTGSGKTLGYILPAIVHinnqqpLQRGDGpiALVLAPTRELAQQIQQVATEFG 378
Cdd:COG3505   5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAG 51
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
573-628 8.06e-03

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 38.77  E-value: 8.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644479 573 LREFRSGKSNILVATDVAARGLDVDGIKYV--INFDYPQNSEDY---------IHRI-GRTGRSNTKG 628
Cdd:cd18804 137 LDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPG 204
ResIII pfam04851
Type III restriction enzyme, res subunit;
327-439 8.46e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644479   327 TGSGKTLGYILpAIVHINNQQPLQRgdgpiALVLAPTRELAQQIQQVATEFGSSSYvrNTCVFGgapKGGQMRDLQRGCE 406
Cdd:pfam04851  32 TGSGKTLTAAK-LIARLFKKGPIKK-----VLFLVPRKDLLEQALEEFKKFLPNYV--EIGEII---SGDKKDESVDDNK 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24644479   407 IVIATPGRLIDFLSAGSTNLKRCTYLVL--DEADR 439
Cdd:pfam04851 101 IVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH