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Conserved domains on  [gi|386765198|ref|NP_001246940|]
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Rm62, isoform L [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

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
87-451 2.40e-177

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: 508.16  E-value: 2.40e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  87 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 162
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 163 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 242
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 243 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 322
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 323 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 401
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 386765198 402 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
87-451 2.40e-177

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 508.16  E-value: 2.40e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  87 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 162
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 163 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 242
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 243 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 322
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 323 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 401
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 386765198 402 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
148-344 7.17e-149

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: 422.16  E-value: 7.17e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 307
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386765198 308 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
Cdd:cd17966  161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
139-450 7.85e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 377.18  E-value: 7.85e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgDGPIALVLAP 218
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 298
Cdd:COG0513   80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 299 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANhNIRQVVDVCDEFSKEEKLKTLLSD 378
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765198 379 iydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGL 450
Cdd:COG0513  239 -----EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGI 305
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
161-332 2.21e-61

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: 197.46  E-value: 2.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  161 TAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAPTRELAQQIQQVATEFGSSSYVR 240
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  241 NTCVFGGAPKGGQMRDLqRGCEIVIATPGRLIDFLSAgSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 320
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 386765198  321 WSATWPKEVKQL 332
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
152-359 1.05e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 186.93  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198   152 IRRQGYKAPTAIQAQGWPIAMSG-SNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVA 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198   231 TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIV 309
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386765198   310 SQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlelSANHNIRQV 359
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
 
Name Accession Description Interval E-value
PTZ00110 PTZ00110
helicase; Provisional
87-451 2.40e-177

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 508.16  E-value: 2.40e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  87 MRPVDFS--NLAPFKKNFYQEHPNVANRSPYEVQRYREEQEIT-VRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTA 162
Cdd:PTZ00110  76 LQPIDWKsiNLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGEnVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 163 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNT 242
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 243 CVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 322
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 323 ATWPKEVKQLAEDFLGNY-IQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYdtsESPGKIIIFVETKRRVDN 401
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIM---RDGDKILIFVETKKGADF 392
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 386765198 402 LVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
148-344 7.17e-149

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: 422.16  E-value: 7.17e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 307
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386765198 308 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
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 ...
91-346 4.18e-142

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: 4.18e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  91 DFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQV-PNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWP 169
Cdd:cd18050   15 DLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGcPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 170 IAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAP 249
Cdd:cd18050   95 LALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 250 KGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEV 329
Cdd:cd18050  175 KGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEV 254
                        250
                 ....*....|....*..
gi 386765198 330 KQLAEDFLGNYIQINIG 346
Cdd:cd18050  255 RQLAEDFLRDYVQINIG 271
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
116-347 1.27e-139

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: 1.27e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 116 EVQRYREEQEITVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILP 194
Cdd:cd18049    2 EVEQYRRSKEITVRGHnCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 195 AIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDF 274
Cdd:cd18049   82 AIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765198 275 LSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGS 347
Cdd:cd18049  162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
139-450 7.85e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 377.18  E-value: 7.85e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgDGPIALVLAP 218
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 298
Cdd:COG0513   80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 299 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANhNIRQVVDVCDEFSKEEKLKTLLSD 378
Cdd:COG0513  160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLRD 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386765198 379 iydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGL 450
Cdd:COG0513  239 -----EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGI 305
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
148-343 3.52e-100

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 298.20  E-value: 3.52e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINnQQPLQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLL-PEPKKKGRGPQALVLAPTRELAMQIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 307
Cdd:cd00268   80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 386765198 308 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
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) ...
127-343 1.51e-96

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: 290.05  E-value: 1.51e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 127 TVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPL 205
Cdd:cd17953    1 KVRGKdCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 206 QRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGS---TNL 282
Cdd:cd17953   81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765198 283 KRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17953  161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
148-343 1.87e-94

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: 283.92  E-value: 1.87e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 307
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 386765198 308 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17952  161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
139-346 1.90e-86

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: 264.35  E-value: 1.90e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDG----PIA 213
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLlEDGPPSVGRGRrkayPSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 214 LVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:cd17967   82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765198 294 DRMLDMGFEPQIRKIVSQ----IRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 346
Cdd:cd17967  162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
148-343 4.23e-80

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: 246.99  E-value: 4.23e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINnQQPLQRG--DGPIALVLAPTRELAQQ 225
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLD-LQPIPREqrNGPGVLVLTPTRELALQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 226 IQQVATEFGSSSYvRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQI 305
Cdd:cd17958   80 IEAECSKYSYKGL-KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386765198 306 RKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
132-346 1.19e-78

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: 245.33  E-value: 1.19e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 132 VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP---LQRG 208
Cdd:cd18051   16 CPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgesLPSE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 209 DG--------PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST 280
Cdd:cd18051   96 SGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKI 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 281 NLKRCTYLVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 346
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 ...
132-346 1.43e-76

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: 240.25  E-value: 1.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 132 VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLQRGDG 210
Cdd:cd18052   38 PPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTASSFSE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 211 ---PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTY 287
Cdd:cd18052  118 vqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKY 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765198 288 LVLDEADRMLDMGFEPQIRKIVSQI----RPDRQTLMWSATWPKEVKQLAEDFL-GNYIQINIG 346
Cdd:cd18052  198 LILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVG 261
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-453 4.72e-76

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 245.48  E-value: 4.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 138 DFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgdGPIALVLA 217
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 218 PTRELAQQiqqVATEfgsssyVR-------NTCVF---GGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTY 287
Cdd:PRK11776  80 PTRELADQ---VAKE------IRrlarfipNIKVLtlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 288 LVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLElsANHNIRQVVDVCDEFS 367
Cdd:PRK11776 151 LVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 368 KEEKLKTLLSDiydtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 447
Cdd:PRK11776 229 RLPALQRLLLH-----HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303

                 ....*.
gi 386765198 448 RGLEAD 453
Cdd:PRK11776 304 RGLDIK 309
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
148-343 6.76e-69

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: 219.11  E-value: 6.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQ---RGDGPIALVLAPTRELAQ 224
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 225 QIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQ 304
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386765198 305 IRKI-----VSQIRPD---------------RQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17945  161 VTKIldampVSNKKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
148-453 2.64e-68

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 225.07  E-value: 2.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPI-ALVLAPTRELAQQI 226
Cdd:PRK10590  12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 227 QQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIR 306
Cdd:PRK10590  92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 307 KIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLElSANHNIRQVVDVCDEFSKEEKLKTLLSDiydtsESP 386
Cdd:PRK10590 172 RVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKRELLSQMIGK-----GNW 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386765198 387 GKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLEAD 453
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIE 312
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
138-453 1.21e-66

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 220.20  E-value: 1.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 138 DFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQqPLQRGDGPIALVLA 217
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDF-PRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 218 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRML 297
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 298 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKE-VKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCDefSKEEKLKtLL 376
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEP-SRRERKKIHQWYYRAD--DLEHKTA-LL 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386765198 377 SDIYdTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLEAD 453
Cdd:PRK11192 237 CHLL-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
102-451 5.56e-62

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 210.41  E-value: 5.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 102 FYQEHPNVANR-SPYEVQRYREEQEITVRGQ-VPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVG 179
Cdd:PLN00206  84 FYVRDPGSTSGlSSSQAELLRRKLEIHVKGEaVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 180 IAKTGSGKTLGYILPAIVH---INNQQPLQRgDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRD 256
Cdd:PLN00206 164 SADTGSGKTASFLVPIISRcctIRSGHPSEQ-RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYR 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 257 LQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVsQIRPDRQTLMWSATWPKEVKQLAEDF 336
Cdd:PLN00206 243 IQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSL 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 337 LGNYIQINIGSLElSANHNIRQVVDVCDefSKEEKLKtlLSDIYDTSE---SPGkiIIFVETKRRVDNLVRFIR-SFGVR 412
Cdd:PLN00206 322 AKDIILISIGNPN-RPNKAVKQLAIWVE--TKQKKQK--LFDILKSKQhfkPPA--VVFVSSRLGADLLANAITvVTGLK 394
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 386765198 413 CGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVD 433
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
161-332 2.21e-61

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: 197.46  E-value: 2.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  161 TAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAPTRELAQQIQQVATEFGSSSYVR 240
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  241 NTCVFGGAPKGGQMRDLqRGCEIVIATPGRLIDFLSAgSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 320
Cdd:pfam00270  76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
                         170
                  ....*....|..
gi 386765198  321 WSATWPKEVKQL 332
Cdd:pfam00270 154 LSATLPRNLEDL 165
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
148-344 2.01e-59

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: 194.09  E-value: 2.01e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQ---PLQRGDGPIALVLAPTRELAQ 224
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEkklPFIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 225 QIQQVATEF------GSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 298
Cdd:cd17951   81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386765198 299 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
135-453 3.82e-58

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 201.33  E-value: 3.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 135 PIQD--FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPL--QRGDG 210
Cdd:PRK04537   5 PLTDltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 211 PIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGS-TNLKRCTYLV 289
Cdd:PRK04537  85 PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKvVSLHACEICV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 290 LDEADRMLDMGFEPQIRKIVSQI--RPDRQTLMWSATWPKEVKQLAEDFLgNYIQINIGSLELSANHNIRQVVdvcdEFS 367
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHM-NEPEKLVVETETITAARVRQRI----YFP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 368 KEEKLKTLLSDIYDTSESpGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 447
Cdd:PRK04537 240 ADEEKQTLLLGLLSRSEG-ARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318

                 ....*.
gi 386765198 448 RGLEAD 453
Cdd:PRK04537 319 RGLHID 324
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
139-453 8.39e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 195.52  E-value: 8.39e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDG-PIALVL 216
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlQTPPPKERYMGePRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 217 APTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQ-RGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 295
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 296 MLDMGFEPQIRKIVSQIRP--DRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCdefSKEEKLK 373
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP-ENVASDTVEQHVYAV---AGSDKYK 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 374 tLLSDIYdTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLEAD 453
Cdd:PRK01297 325 -LLYNLV-TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
DEXDc smart00487
DEAD-like helicases superfamily;
152-359 1.05e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 186.93  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198   152 IRRQGYKAPTAIQAQGWPIAMSG-SNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVA 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198   231 TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIV 309
Cdd:smart00487  75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386765198   310 SQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlelSANHNIRQV 359
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 ...
148-333 1.24e-56

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: 187.02  E-value: 1.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGW-PIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQI 226
Cdd:cd17964    5 LLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 227 qqvATEFGS-SSYVRNT---CVFGGAPKGGQMRDLQR-GCEIVIATPGRLIDFLS--AGSTNLKRCTYLVLDEADRMLDM 299
Cdd:cd17964   85 ---AAEAKKlLQGLRKLrvqSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDM 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386765198 300 GFEPQIRKIVSQIRP----DRQTLMWSATWPKEVKQLA 333
Cdd:cd17964  162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIA 199
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
137-450 2.37e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 192.88  E-value: 2.37e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 137 QDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYiLPAIVH--INNQQPLQR-GDGPIA 213
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTATFHylLSHPAPEDRkVNQPRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 214 LVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:PRK04837  87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 294 DRMLDMGFEPQIRKIVSQIRP--DRQTLMWSATWPKEVKQLAEDFLGN--YIQInigSLELSANHNIRQVVdvcdeF--S 367
Cdd:PRK04837 167 DRMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNpeYVEV---EPEQKTGHRIKEEL-----FypS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 368 KEEKLKTLLSDIYDtsESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAA 447
Cdd:PRK04837 239 NEEKMRLLQTLIEE--EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316

                 ...
gi 386765198 448 RGL 450
Cdd:PRK04837 317 RGL 319
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
139-343 1.56e-55

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: 1.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLqrgdgpIALVLA 217
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAlLENPQRF------FALVLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 218 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSagST---NLKRCTYLVLDEAD 294
Cdd:cd17954   76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLE--NTkgfSLKSLKFLVMDEAD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 386765198 295 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17954  154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
156-343 5.57e-54

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: 180.09  E-value: 5.57e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 156 GYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQRGDGPIALVLAPTRELAQQIQQVATEFG 234
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrVDRSDGTLALVLVPTRELALQIYEVLEKLL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 235 SSS-YVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFL-SAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQI 312
Cdd:cd17949   90 KPFhWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386765198 313 R-------------PDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17949  170 DdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
PTZ00424 PTZ00424
helicase 45; Provisional
136-451 7.55e-53

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 183.10  E-value: 7.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 136 IQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHIN-NQQPLQrgdgpiAL 214
Cdd:PTZ00424  27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDyDLNACQ------AL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 215 VLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEAD 294
Cdd:PTZ00424 101 ILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEAD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 295 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSAnHNIRQVVDVCDefSKEEKLKT 374
Cdd:PTZ00424 181 EMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFYVAVE--KEEWKFDT 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386765198 375 LLsDIYDTSeSPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:PTZ00424 258 LC-DLYETL-TITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
139-337 1.32e-52

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: 176.26  E-value: 1.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPaIVHINNQQPLqrgdGPIALVLAP 218
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP-ILQRLSEDPY----GIFALVLTP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST---NLKRCTYLVLDEADR 295
Cdd:cd17955   76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 386765198 296 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFL 337
Cdd:cd17955  156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFG 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
148-344 6.02e-52

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 174.42  E-value: 6.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQrgdGPIALVLAPTRELAQQIQ 227
Cdd:cd17959   12 LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV---GARALILSPTRELALQTL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK 307
Cdd:cd17959   89 KVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHE 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386765198 308 IVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
Cdd:cd17959  169 ILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
148-346 6.59e-51

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: 6.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQqplQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVATEFGSSSYVRnTCVF--GGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQI 305
Cdd:cd17957   78 RELLKLSKGTGLR-IVLLskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 386765198 306 RKIVSQIR-PDRQTLMWSATWPKEVKQLAEDFLGNYIQINIG 346
Cdd:cd17957  157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
139-453 1.44e-50

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 181.97  E-value: 1.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhiNNQQPLQRGdgPIALVLAP 218
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL---HNLDPELKA--PQILVLAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFgsSSYVRNTCV---FGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 295
Cdd:PRK11634  83 TRELAVQVAEAMTDF--SKHMRGVNVvalYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 296 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSlELSANHNIRQVVDVCDEFSKEEKLKTL 375
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRF 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765198 376 LSdiydtSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLEAD 453
Cdd:PRK11634 240 LE-----AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
148-333 2.22e-50

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: 170.13  E-value: 2.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAI---VHINNQQPLQRgdgpiALVLAPTRELAQ 224
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILerlLYRPKKKAATR-----VLVLVPTRELAM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 225 QIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFL-SAGSTNLKRCTYLVLDEADRMLDMGFEP 303
Cdd:cd17947   76 QCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFAD 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 386765198 304 QIRKIVSQIRPDRQTLMWSATWPKEVKQLA 333
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 ...
139-344 1.04e-48

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


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 165.93  E-value: 1.04e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQrgdgpiALVLA 217
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDvIQ------ALILV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 218 PTRELAQQIQQVATEFGSSSYVRNTCVFGGAPkggqMRD----LQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:cd17940   75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTS----LRDdimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386765198 294 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
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 ...
152-343 2.86e-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: 161.95  E-value: 2.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 152 IRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVhinnqQPLQRGDGPIALVLAPTRELAQQIQQVAT 231
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII-----RCLTEHRNPSALILTPTRELAVQIEDQAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 232 EFGSSS-YVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVS 310
Cdd:cd17962   80 ELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 386765198 311 QIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
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 ...
148-324 5.89e-47

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: 162.41  E-value: 5.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGS-NFVGIAKTGSGKTLGYILPAIVHINNQQpLQRGD-----GPIALVLAPTRE 221
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQK-SSNGVggkqkPLRALILTPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 222 LAQQIQQVATEFGSSSYVRNTCVFGG--APKggQMRDLQRGCEIVIATPGRLIDFLSAGST---NLKRCTYLVLDEADRM 296
Cdd:cd17946   80 LAVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRM 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 386765198 297 LDMG-FEpQIRKIVSQI-------RPDRQTLMWSAT 324
Cdd:cd17946  158 LEKGhFA-ELEKILELLnkdragkKRKRQTFVFSAT 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
150-345 7.79e-46

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: 7.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 150 KEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQpLQRGDGPIALVLAPTRELAQQIQQV 229
Cdd:cd17941    3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 230 ATEFGSSSYVRNTCVFGGapkggqmRDLQR------GCEIVIATPGRLIDFL----SAGSTNLKrctYLVLDEADRMLDM 299
Cdd:cd17941   82 LRKVGKYHSFSAGLIIGG-------KDVKEekerinRMNILVCTPGRLLQHMdetpGFDTSNLQ---MLVLDEADRILDM 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386765198 300 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINI 345
Cdd:cd17941  152 GFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
148-344 9.31e-46

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


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 158.12  E-value: 9.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQ 227
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 228 QVA---TEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLS--AGSTNLKRCTYLVLDEADRMLDMGFE 302
Cdd:cd17960   81 EVLqsfLEHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 386765198 303 PQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQIN 344
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
149-333 5.17e-45

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: 155.98  E-value: 5.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 149 MKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRgDGPIALVLAPTRELAQQIQQ 228
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 229 VATE---FGSSSYvrnTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGS----TNLKrctYLVLDEADRMLDMGF 301
Cdd:cd17942   81 VAKEllkYHSQTF---GIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGF 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 386765198 302 EPQIRKIVSQIRPDRQTLMWSATWPKEVKQLA 333
Cdd:cd17942  155 EEEMRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
144-343 3.42e-39

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


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 140.54  E-value: 3.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 144 LPDYVMKEIRRQGYKAPTAIQAQG-WPIaMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQP-LQrgdgpiALVLAPTRE 221
Cdd:cd17939    4 LSEDLLRGIYAYGFEKPSAIQQRAiVPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVReTQ------ALVLAPTRE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 222 LAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGF 301
Cdd:cd17939   77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 386765198 302 EPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17939  157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
144-343 6.75e-39

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: 139.63  E-value: 6.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 144 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLqrgdgPIALVLAPTRE 221
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS-----PQALCLAPTRE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 222 LAQQIQQVATEFGSSSYVRNTCVFGG--APKGGQMRDlqrgcEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDM 299
Cdd:cd17963   76 LARQIGEVVEKMGKFTGVKVALAVPGndVPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDT 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386765198 300 -GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
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, ...
148-343 6.04e-37

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: 134.31  E-value: 6.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAI--VHINNQQPLqrgdgpiALVLAPTRELAQQ 225
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALesLDLERRHPQ-------VLILAPTREIAVQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 226 IQQVATEFGSSSYVRNTCVF-GGAPkggQMRDLQR--GCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFE 302
Cdd:cd17943   74 IHDVFKKIGKKLEGLKCEVFiGGTP---VKEDKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQ 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 386765198 303 PQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
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 ...
139-334 8.40e-37

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: 8.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQrgdgpiALVLAP 218
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL------QIVV------ALILEP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQ----IQQVATEFGSSSyVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEAD 294
Cdd:cd17938   69 SRELAEQtyncIENFKKYLDNPK-LRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 386765198 295 RMLDMGFEPQIRKIVSQI-----RPDR-QTLMWSATWPK-EVKQLAE 334
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 ...
144-339 1.60e-36

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


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 133.48  E-value: 1.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 144 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHI-NNQQPLQRGDGPIALVLAPTREL 222
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 223 AQQIQQVATEF--GSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGST-NLKRCTYLVLDEADRMLDM 299
Cdd:cd17961   81 AQQVSKVLEQLtaYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 386765198 300 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGN 339
Cdd:cd17961  161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
163-344 2.77e-36

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 133.05  E-value: 2.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 163 IQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHIN-NQQPLQRGDGPIALVLAPTRELAQQiqqVATEFGS-SSYVR 240
Cdd:cd17944   16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQ---VTKDFKDiTRKLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 241 NTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVS-QIRPDR--- 316
Cdd:cd17944   93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSedn 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 386765198 317 -QTLMWSATWPKEVKQLAEDFL-GNYIQIN 344
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 ...
139-343 1.19e-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: 128.33  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPlqrgdGPIALVLAP 218
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK-----ATQALVLAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 298
Cdd:cd18046   76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386765198 299 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd18046  156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
152-335 6.47e-33

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


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 124.79  E-value: 6.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 152 IRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRG--DGPIALVLAPTRELAQQIQQV 229
Cdd:cd17948    5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQIGSV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 230 ATEFGSSSYVRNTCVFGGAPKGgQMRDLQRG-CEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKI 308
Cdd:cd17948   85 AQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHF 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 386765198 309 VSQIR-------------PDRQTLMWSATWPKEVKQLAED 335
Cdd:cd17948  164 LRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
356-450 3.47e-32

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: 119.15  E-value: 3.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 356 IRQVVDVCDEFSKEEKLKTLLsdiyDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSG 435
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLL----LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSG 76
                         90
                 ....*....|....*
gi 386765198 436 KSNILVATDVAARGL 450
Cdd:cd18787   77 KVRVLVATDVAARGL 91
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
139-343 2.03e-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: 119.76  E-value: 2.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQRGDGPI-ALVLA 217
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVsVLVIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 218 PTRELAQQIQQVATEFgsSSY---VRNTCVFGGAPKGGQMRDLQRGC-EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:cd17950   78 HTRELAFQISNEYERF--SKYmpnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDEC 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386765198 294 DRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17950  156 DKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
139-343 1.62e-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: 109.09  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 139 FSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQplqrgDGPIALVLAP 218
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV-----RETQALILSP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 219 TRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLD 298
Cdd:cd18045   76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386765198 299 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd18045  156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
148-302 8.66e-23

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: 8.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 148 VMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGI---------AKTGSGKTLGYILPaIVhinnqQPLQRGDGPI--ALVL 216
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTPPyrpgdlcvsAPTGSGKTLAYVLP-IV-----QALSKRVVPRlrALIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 217 APTRELAQQIQQVATEFGSSSYVRnTCVFGGAPK-GGQMRDLQRGCE--------IVIATPGRLIDFLSAGST-NLKRCT 286
Cdd:cd17956   75 VPTKELVQQVYKVFESLCKGTGLK-VVSLSGQKSfKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPGfTLKHLR 153
                        170
                 ....*....|....*.
gi 386765198 287 YLVLDEADRMLDMGFE 302
Cdd:cd17956  154 FLVIDEADRLLNQSFQ 169
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
177-343 1.36e-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: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 177 FVGIAKTGSGKTLGYILPAIVHINNQ------------QPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCV 244
Cdd:cd17965   64 FLLAAETGSGKTLAYLAPLLDYLKRQeqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 245 fgGAPKGGQMRDLQR----GCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 320
Cdd:cd17965  144 --SSGFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
                        170       180
                 ....*....|....*....|...
gi 386765198 321 WSATWPKEVKQLAEDFLGNYIQI 343
Cdd:cd17965  222 CSATIPKEFDKTLRKLFPDVVRI 244
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
367-450 1.73e-18

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: 80.72  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  367 SKEEKLKTLLSdiydtSESPGKIIIFVETKRRVDnLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVA 446
Cdd:pfam00271   1 EKLEALLELLK-----KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74

                  ....
gi 386765198  447 ARGL 450
Cdd:pfam00271  75 ERGL 78
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
136-334 1.94e-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: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 136 IQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLqrgdgPIA 213
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 214 LVLAPTRELAQQIQQVATEFGS-SSYVRNTCVFGG--APKGGQMRdlqrgCEIVIATPGRLIDF-LSAGSTNLKRCTYLV 289
Cdd:cd18048   92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGnrPGKGTDIE-----AQIVIGTPGTVLDWcFKLRLIDVTNISVFV 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386765198 290 LDEADRMLDM-GFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAE 334
Cdd:cd18048  167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAE 212
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
174-446 7.85e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 83.15  E-value: 7.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 174 GSNFVGIAKTGSGKTlgYILPAIVHinnqqplQRGDGPIALVLAPTRELAQQIQQVATEFgsssyvrntcvFGGAPKGGQ 253
Cdd:COG1061  100 GGRGLVVAPTGTGKT--VLALALAA-------ELLRGKRVLVLVPRRELLEQWAEELRRF-----------LGDPLAGGG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 254 MRDlqRGCEIVIATPGRLIDFLSAGSTNlKRCTYLVLDEADRmldmGFEPQIRKIVSQIRPDRQTLMwSAT-WPKEVKQL 332
Cdd:COG1061  160 KKD--SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpFRSDGREI 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 333 AEDFLGNyIQINIGSLELSANHNIRQV------VDVCDEFSKEEKLKTLLSDIYDTSE---------------SPGKIII 391
Cdd:COG1061  232 LLFLFDG-IVYEYSLKEAIEDGYLAPPeyygirVDLTDERAEYDALSERLREALAADAerkdkilrellrehpDDRKTLV 310
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765198 392 FVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVA 446
Cdd:COG1061  311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVL 365
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
137-334 9.31e-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: 72.83  E-value: 9.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 137 QDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSG--SNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRgdgpiAL 214
Cdd:cd18047    1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 215 VLAPTRELAQQIQQVATEFGsSSYVRNTCVFggAPKGGQM-RDLQRGCEIVIATPGRLIDF-LSAGSTNLKRCTYLVLDE 292
Cdd:cd18047   76 CLSPTYELALQTGKVIEQMG-KFYPELKLAY--AVRGNKLeRGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 386765198 293 ADRML-DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAE 334
Cdd:cd18047  153 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQ 195
HELICc smart00490
helicase superfamily c-terminal domain;
400-450 4.08e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.54  E-value: 4.08e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386765198   400 DNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGL 450
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGL 51
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
174-324 3.06e-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: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 174 GSNFVGIAKTGSGKTLGYILPAIVHINNQqplqrgdGPIALVLAPTRELA-QQIQQVATEFGSSSYVRntcVFGGAPKGG 252
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALAlQTAERLRELFGPGIRVA---VLVGGSSAE 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386765198 253 QMRDLQRGCE-IVIATPGRLI-DFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRK--IVSQIRPDRQTLMWSAT 324
Cdd:cd00046   71 EREKNKLGDAdIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
144-293 1.18e-10

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: 63.70  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 144 LPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIvhinnqQPLQRGDGPIALVLAPTRELA 223
Cdd:COG1205   41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVL------EALLEDPGATALYLYPTKALA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 224 Q-Q---IQQVATEFGSSsyVRNTCVFGGAPKgGQMRDLQRGCEIVIATPgrliDFLSAG--------STNLKRCTYLVLD 291
Cdd:COG1205  115 RdQlrrLRELAEALGLG--VRVATYDGDTPP-EERRWIREHPDIVLTNP----DMLHYGllphhtrwARFFRNLRYVVID 187

                 ..
gi 386765198 292 EA 293
Cdd:COG1205  188 EA 189
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
136-443 1.56e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 62.99  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 136 IQDFSEVHLPDYVmkeiRRQGYKAPTAIQAQGWP-IAMSGSNFVGIAKTGSGKTL-GYIlpAIV-HINNqqplqrgdGPI 212
Cdd:COG1204    3 VAELPLEKVIEFL----KERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL--AILkALLN--------GGK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 213 ALVLAPTRELAQQIQQ----VATEFGSSSYVrntcVFGGAPKGGqmRDLQRgCEIVIATPGRLIDFLSAGSTNLKRCTYL 288
Cdd:COG1204   69 ALYIVPLRALASEKYRefkrDFEELGIKVGV----STGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 289 VLDEA------DRmldmGfePQIRKIVSQIR---PDRQTLMWSATWPkEVKQLAEDFLGNYIQINIGSLELSANHNIRQV 359
Cdd:COG1204  142 VVDEAhliddeSR----G--PTLEVLLARLRrlnPEAQIVALSATIG-NAEEIAEWLDAELVKSDWRPVPLNEGVLYDGV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 360 VDVCDEFSKEekLKTLLSDIYDTSESPGKIIIFVETKRRV-----------------------DNLVRFIRSFG------ 410
Cdd:COG1204  215 LRFDDGSRRS--KDPTLALALDLLEEGGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSeethtn 292
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 386765198 411 ------VRCGAI--HGDKSQSERDFVLREFRSGKSNILVAT 443
Cdd:COG1204  293 ekladcLEKGVAfhHAGLPSELRRLVEDAFREGLIKVLVAT 333
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
349-450 2.76e-10

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 62.83  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 349 ELSANHNIRQVVDVCDEF----SKEEKLKTLLSDIYDTSESpGKIIIFVETKRRVDNLVRFIRSFGVRC------GAIHG 418
Cdd:COG1111  313 RLVSDPRFRKAMRLAEEAdiehPKLSKLREILKEQLGTNPD-SRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEG 391
                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765198 419 DK--SQSERDFVLREFRSGKSNILVATDVAARGL 450
Cdd:COG1111  392 DKglTQKEQIEILERFRAGEFNVLVATSVAEEGL 425
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
356-450 8.33e-07

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: 48.24  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 356 IRQVVDVcdefskeeKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSG 435
Cdd:cd18793    5 IEEVVSG--------KLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED 76
                         90
                 ....*....|....*..
gi 386765198 436 KSN--ILVATDVAARGL 450
Cdd:cd18793   77 PDIrvFLLSTKAGGVGL 93
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
367-467 3.36e-06

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 46.86  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 367 SKEEKLKTLLsdiyDTSESPGKIIIFVETkrrVDNLVRFIRSFGVRcgAIHGDKSQSERDFVLREFRSGKSNILVATDVA 446
Cdd:cd18789   34 NKLRALEELL----KRHEQGDKIIVFTDN---VEALYRYAKRLLKP--FITGETPQSEREEILQNFREGEYNTLVVSKVG 104
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 386765198 447 ARGL---EAD--------FGSM------MGRIMnerRP 467
Cdd:cd18789  105 DEGIdlpEANvaiqisghGGSRrqeaqrLGRIL---RP 139
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
164-293 3.94e-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: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 164 QAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSY--VRN 241
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEA------LLRDPGSRALYLYPTKALAQDQLRSLRELLEQLGlgIRV 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765198 242 TCVFGGAPKGGQMRDLQRGCEIVIATP-----------GRLIDFLSagstNLKrctYLVLDEA 293
Cdd:cd17923   79 ATYDGDTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
183-293 4.07e-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: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 183 TGSGKTLgYILPAIVHinnqqplqRGDGPIaLVLAPTRELAQQIQQVATEFGSSSYVrntCVFGGAPKggqmrDLQRGCE 262
Cdd:cd17926   27 TGSGKTL-TALALIAY--------LKELRT-LIVVPTDALLDQWKERFEDFLGDSSI---GLIGGGKK-----KDFDDAN 88
                         90       100       110
                 ....*....|....*....|....*....|.
gi 386765198 263 IVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:cd17926   89 VVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
163-293 4.37e-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: 46.87  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 163 IQAQGWPIAM-SGSNFVGIAKTGSGKTL-GYIlpAIVHINNQQplqrgdGPIALVLAPTRELAQQIQQVATEFGSSSYVR 240
Cdd:cd17921    5 IQREALRALYlSGDSVLVSAPTSSGKTLiAEL--AILRALATS------GGKAVYIAPTRALVNQKEADLRERFGPLGKN 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765198 241 NTCVFGGAPKGGQMrdlQRGCEIVIATPGRLiDFLS--AGSTNLKRCTYLVLDEA 293
Cdd:cd17921   77 VGLLTGDPSVNKLL---LAEADILVATPEKL-DLLLrnGGERLIQDVRLVVVDEA 127
PRK13766 PRK13766
Hef nuclease; Provisional
349-450 4.55e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.10  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 349 ELSANHNIRQVVDVCDEFSKE----EKLKTLLSDIYDTSESPgKIIIFVETKRRVDNLVRFIRSFGVRC------GAIHG 418
Cdd:PRK13766 325 RLVEDPRFRKAVRKAKELDIEhpklEKLREIVKEQLGKNPDS-RIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDG 403
                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765198 419 DK--SQSERDFVLREFRSGKSNILVATDVAARGL 450
Cdd:PRK13766 404 DKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGL 437
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
367-450 6.26e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 48.68  E-value: 6.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 367 SKEEKLKTLLSDIYDTSEspgKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSN--ILVATD 444
Cdd:COG0553  533 AKLEALLELLEELLAEGE---KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLK 609

                 ....*.
gi 386765198 445 VAARGL 450
Cdd:COG0553  610 AGGEGL 615
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
365-459 9.39e-06

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: 45.28  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 365 EFSKEEKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATd 444
Cdd:cd18794    9 RPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT- 87
                         90
                 ....*....|....*
gi 386765198 445 VAargleadFGsmMG 459
Cdd:cd18794   88 VA-------FG--MG 93
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
366-450 1.28e-05

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: 44.89  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 366 FSKEEKLKTLLSDIYDTSESPgKIIIFVETKRRVDNLVRFIRSFG-----VRCGAI--HGDKSQSERDF--------VLR 430
Cdd:cd18802    6 IPKLQKLIEILREYFPKTPDF-RGIIFVERRATAVVLSRLLKEHPstlafIRCGFLigRGNSSQRKRSLmtqrkqkeTLD 84
                         90       100
                 ....*....|....*....|
gi 386765198 431 EFRSGKSNILVATDVAARGL 450
Cdd:cd18802   85 KFRDGELNLLIATSVLEEGI 104
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
319-457 6.42e-05

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: 45.11  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 319 LMwSATWPKEVKQLAEDFLgnyIQINIGSLELSANHNIRQVVDVCDEFSKEeklkTLLSDIYDTSESPGKIIIFVETKRR 398
Cdd:cd09639  159 LM-SATLPKFLKEYAEKIG---YVEENEPLDLKPNERAPFIKIESDKVGEI----SSLERLLEFIKKGGSVAIIVNTVDR 230
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386765198 399 VDNLVRFIRSFGVRCGAI--HGDKSQSER----DFVLREFRSGKSNILVATDVAARGLEADFGSM 457
Cdd:cd09639  231 AQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDISVDVM 295
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
157-228 8.24e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.09  E-value: 8.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765198 157 YKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVH-INNQQPLQRGDGPIALVLAPTRELAQQIQQ 228
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLKALANDIER 94
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
357-443 1.09e-04

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: 42.54  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 357 RQVVDVCDEFSKEEKLKTLLSD-------IYDTSESPGKIIIFVETKRRVDNLVRFIRsfGVrcGAIHGDKSQSERDFVL 429
Cdd:cd18795    7 EYVLGFNGLGIKLRVDVMNKFDsdiivllKIETVSEGKPVLVFCSSRKECEKTAKDLA--GI--AFHHAGLTREDRELVE 82
                         90
                 ....*....|....
gi 386765198 430 REFRSGKSNILVAT 443
Cdd:cd18795   83 ELFREGLIKVLVAT 96
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
166-331 2.07e-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: 42.24  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 166 QGWPIA--MSGSNFVGIAKTGSGKTLGYILPAIVhinnqqpLQRGDGPIALVLAPTreLAQQIQQVAtefGSSSYVRNTC 243
Cdd:cd18018   17 QEEAIArlLSGRSTLVVLPTGAGKSLCYQLPALL-------LRRRGPGLTLVVSPL--IALMKDQVD---ALPRAIKAAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 244 VFGGAPKGGQMRDLQR----GCEIVIATPGRLI--DFLSAGSTnLKRCTYLVLDEADRMLDMG--FEP---QIRKIVSQI 312
Cdd:cd18018   85 LNSSLTREERRRILEKlragEVKILYVSPERLVneSFRELLRQ-TPPISLLVVDEAHCISEWShnFRPdylRLCRVLREL 163
                        170
                 ....*....|....*....
gi 386765198 313 RPDRQTLMWSATWPKEVKQ 331
Cdd:cd18018  164 LGAPPVLALTATATKRVVE 182
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
368-451 5.61e-04

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: 40.03  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 368 KEEKLKTLLSDiYDTSESPGK---IIIFVETKRRVDNLVRFIRSFGVRCGAI----HGDK------SQSERDFVLREFRS 434
Cdd:cd18801   10 KLEKLEEIVKE-HFKKKQEGSdtrVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRK 88
                         90
                 ....*....|....*..
gi 386765198 435 GKSNILVATDVAARGLE 451
Cdd:cd18801   89 GGYNVLVATSIGEEGLD 105
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
410-445 1.02e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 41.57  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 386765198 410 GVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDV 445
Cdd:COG1200  503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
409-445 1.29e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 41.29  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386765198 409 FGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDV 445
Cdd:PRK10917 504 PELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTV 540
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
180-295 1.35e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 39.81  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 180 IAKTGSGKTLGYILPAIVHinnqqpLQRGDGPIaLVLAPTRELAQQIQQVATEFGSSSyvrNTCV-FGGAPKGGQMRDLQ 258
Cdd:cd18035   22 VLPTGLGKTIIAILVAADR------LTKKGGKV-LILAPSRPLVEQHAENLKRVLNIP---DKITsLTGEVKPEERAERW 91
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 386765198 259 RGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADR 295
Cdd:cd18035   92 DASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
414-471 2.41e-03

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: 38.48  E-value: 2.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386765198 414 GAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLEADFGSMMgRIMN-ERRPLRTL 471
Cdd:cd18811   65 GLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVM-VIEDaERFGLSQL 122
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
162-331 2.93e-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: 39.05  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 162 AIQAqgwpiAMSGSNFVGIAKTGSGKTLGYILPAIVhinnqqplqrgDGPIALVLAPTRELAQ-QIQQVATEFgsssyVR 240
Cdd:cd17920   20 AINA-----VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDRLQQLG-----IR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 241 NTCVFGGAPKGGQMRDLQR----GCEIVIATPGRL-----IDFLsAGSTNLKRCTYLVLDEADRMLDMG--FEPQIRKIV 309
Cdd:cd17920   79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdfLELL-QRLPERKRLALIVVDEAHCVSQWGhdFRPDYLRLG 157
                        170       180
                 ....*....|....*....|....
gi 386765198 310 SQIR--PDRQTLMWSATWPKEVKQ 331
Cdd:cd17920  158 RLRRalPGVPILALTATATPEVRE 181
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
180-234 3.42e-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: 39.58  E-value: 3.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765198 180 IAKTGSGKTLGYILPAIVHinnqqpLQRGDGpiALVLAPTRELAQQIQQVATEFG 234
Cdd:COG3505    5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAG 51
ResIII pfam04851
Type III restriction enzyme, res subunit;
183-295 4.22e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198  183 TGSGKTLGYILpAIVHINNQQPLQRgdgpiALVLAPTRELAQQIQQVATEFGSSSYvrNTCVFGgapKGGQMRDLQRGCE 262
Cdd:pfam04851  32 TGSGKTLTAAK-LIARLFKKGPIKK-----VLFLVPRKDLLEQALEEFKKFLPNYV--EIGEII---SGDKKDESVDDNK 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 386765198  263 IVIATPGRLIDFLSAGSTNLKRCTYLVL--DEADR 295
Cdd:pfam04851 101 IVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR 135
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
375-451 5.97e-03

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: 37.61  E-value: 5.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386765198 375 LLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLE 451
Cdd:cd18790   16 LLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLD 92
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
171-295 6.02e-03

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 38.18  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 171 AMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDgpiALVLAPTREL-AQQIQQVATEFGSSSYvRNTCVFGGAP 249
Cdd:cd17927   14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPLvEQQKEVFRKHFERPGY-KVTGLSGDTS 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386765198 250 KGGQMRDLQRGCEIVIATPGRLI-DFLSAGSTNLKRCTYLVLDEADR 295
Cdd:cd17927   90 ENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
388-445 7.04e-03

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: 36.38  E-value: 7.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765198 388 KIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSER-DFVLREFRSGKS--NILVATDV 445
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDL 68
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
183-293 9.33e-03

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 37.25  E-value: 9.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765198 183 TGSGKTLGYILpAIVHINNQQPLQRGDGPIALVLAPTRELAQQiQqvATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGC- 261
Cdd:cd18034   25 TGSGKTLIAVM-LIKEMGELNRKEKNPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVDKWTKERWKEEl 100
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 386765198 262 ---EIVIATPGRLIDFLSAGSTNLKRCTYLVLDEA 293
Cdd:cd18034  101 ekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 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.
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