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Conserved domains on  [gi|2288627546|ref|NP_001398028|]
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eukaryotic initiation factor 4A-III isoform 2 [Homo sapiens]

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 ...
35-390 0e+00

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


The actual alignment was detected with superfamily member PTZ00424:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 401  Bit Score: 561.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  35 DVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD------------- 101
Cdd:PTZ00424   25 EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDydlnacqalilap 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 102 -------IQGL-LALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLN 173
Cdd:PTZ00424  105 trelaqqIQKVvLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 174 KGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDT 253
Cdd:PTZ00424  185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 254 LTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDL 333
Cdd:PTZ00424  265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2288627546 334 PNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI 390
Cdd:PTZ00424  345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
35-390 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 561.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  35 DVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD------------- 101
Cdd:PTZ00424   25 EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDydlnacqalilap 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 102 -------IQGL-LALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLN 173
Cdd:PTZ00424  105 trelaqqIQKVvLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 174 KGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDT 253
Cdd:PTZ00424  185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 254 LTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDL 333
Cdd:PTZ00424  265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2288627546 334 PNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI 390
Cdd:PTZ00424  345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
37-384 4.92e-143

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 413.00  E-value: 4.92e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  37 TPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD------IQGL----- 105
Cdd:COG0513     1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDpsrpraPQALilapt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 --LA---------LGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNK 174
Cdd:COG0513    81 reLAlqvaeelrkLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 175 GFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEwKFDTLCDLYDTL 254
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 255 TITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLP 334
Cdd:COG0513   240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2288627546 335 NNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPM 384
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
40-219 2.38e-120

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: 346.76  E-value: 2.38e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ---------------- 103
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQvretqalilsptrela 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 104 -----GLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKE 178
Cdd:cd18045    81 vqiqkVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 179 QIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRIL 219
Cdd:cd18045   161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
DEXDc smart00487
DEAD-like helicases superfamily;
53-233 6.37e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 140.70  E-value: 6.37e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546   53 IYAYGFEKPSAIQQRAIKQIIKG-RDVIAQSQSGTGKTATFSISVLQCLDIQG--------------------LLALGDY 111
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKggrvlvlvptrelaeqwaeeLKKLGPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  112 MNVQCHACIGGTNVGEDIRKLDYGQ-HVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPA 190
Cdd:smart00487  81 LGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2288627546  191 TQVVLISATLPHEILEMTNKFMTDPIRILVKRdeLTLEGIKQF 233
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
62-206 5.60e-39

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: 136.99  E-value: 5.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  62 SAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGLL----------------ALGDYMNVQCHACI 120
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDkldngPQALVlaptrelaeqiyeelkKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 121 GGTNVGEDIRKLDyGQHVVAGTPGRVFDMIRRRSlRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATL 200
Cdd:pfam00270  81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*.
gi 2288627546 201 PHEILE 206
Cdd:pfam00270 159 PRNLED 164
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
35-390 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 561.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  35 DVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD------------- 101
Cdd:PTZ00424   25 EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDydlnacqalilap 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 102 -------IQGL-LALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLN 173
Cdd:PTZ00424  105 trelaqqIQKVvLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 174 KGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDT 253
Cdd:PTZ00424  185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 254 LTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDL 333
Cdd:PTZ00424  265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2288627546 334 PNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI 390
Cdd:PTZ00424  345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
37-384 4.92e-143

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 413.00  E-value: 4.92e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  37 TPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD------IQGL----- 105
Cdd:COG0513     1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDpsrpraPQALilapt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 --LA---------LGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNK 174
Cdd:COG0513    81 reLAlqvaeelrkLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 175 GFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEwKFDTLCDLYDTL 254
Cdd:COG0513   161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 255 TITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLP 334
Cdd:COG0513   240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2288627546 335 NNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPM 384
Cdd:COG0513   320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
40-219 2.38e-120

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: 346.76  E-value: 2.38e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ---------------- 103
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQvretqalilsptrela 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 104 -----GLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKE 178
Cdd:cd18045    81 vqiqkVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 179 QIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRIL 219
Cdd:cd18045   161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
42-219 2.71e-111

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: 323.89  E-value: 2.71e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  42 TMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDI------------------- 102
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTtvretqalvlaptrelaqq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 103 --QGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQI 180
Cdd:cd17939    81 iqKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2288627546 181 YDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRIL 219
Cdd:cd17939   161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
40-219 1.35e-105

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: 309.38  E-value: 1.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDI-----QGL--------- 105
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTslkatQALvlaptrela 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 -------LALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKE 178
Cdd:cd18046    81 qqiqkvvMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 179 QIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRIL 219
Cdd:cd18046   161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
37-380 5.81e-92

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 283.62  E-value: 5.81e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  37 TPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGL------ 105
Cdd:PRK11776    3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDvkrfrVQALvlcptr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 -LA---------LGDYM-NVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNK 174
Cdd:PRK11776   83 eLAdqvakeirrLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 175 GFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILV--KRDELTlegIKQFFVAVEREEwKFDTLCDLYD 252
Cdd:PRK11776  163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPA---IEQRFYEVSPDE-RLPALQRLLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 253 TLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYD 332
Cdd:PRK11776  239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2288627546 333 LPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQID 380
Cdd:PRK11776  319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
27-390 5.07e-74

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 242.06  E-value: 5.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  27 EFETseevdvtpTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD----- 101
Cdd:PRK11634    3 EFET--------TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDpelka 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 102 -------------IQGLLALGDYM----NVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLV 164
Cdd:PRK11634   75 pqilvlaptrelaVQVAEAMTDFSkhmrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 165 LDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEwKF 244
Cdd:PRK11634  155 LDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 245 DTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQ 324
Cdd:PRK11634  234 EALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVER 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2288627546 325 VSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI 390
Cdd:PRK11634  314 ISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
38-374 2.06e-71

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 229.83  E-value: 2.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  38 PTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQ-CLD----------IQGL- 105
Cdd:PRK11192    1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhLLDfprrksgpprILILt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 ----LAlgdyMNVQCHAC-------------IGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEA 168
Cdd:PRK11192   81 ptreLA----MQVADQARelakhthldiatiTGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 169 DEMLNKGFK---EQIYDVYRYlppATQVVLISATLPHE-ILEMTNKFMTDPIRILVK--RDELtlEGIKQFFVAVEREEW 242
Cdd:PRK11192  157 DRMLDMGFAqdiETIAAETRW---RKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEpsRRER--KKIHQWYYRADDLEH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 243 KFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDV 322
Cdd:PRK11192  232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2288627546 323 PQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQY 374
Cdd:PRK11192  312 DDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
39-382 7.67e-70

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 226.61  E-value: 7.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALG--------- 109
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrpvralil 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 110 ------------------DYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEM 171
Cdd:PRK10590   82 tptrelaaqigenvrdysKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 172 LNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEwKFDTLCDLY 251
Cdd:PRK10590  162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 252 DTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINY 331
Cdd:PRK10590  241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2288627546 332 DLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEM 382
Cdd:PRK10590  321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
49-218 1.74e-65

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: 206.91  E-value: 1.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD---------IQGL-------LA----- 107
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkkkgrgPQALvlaptreLAmqiae 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 ----LGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDV 183
Cdd:cd00268    81 varkLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2288627546 184 YRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd00268   161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
14-383 1.04e-63

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 210.92  E-value: 1.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  14 RKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFS 93
Cdd:PRK01297   63 RERKPKPASLWKLEDFVVEPQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  94 ISVLQCL------------DIQGLL----------------ALGDYMNVQCHACIGGTNVGEDIRKLDyGQH--VVAGTP 143
Cdd:PRK01297  143 ISIINQLlqtpppkerymgEPRALIiaptrelvvqiakdaaALTKYTGLNVMTFVGGMDFDKQLKQLE-ARFcdILVATP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 144 GRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT--QVVLISATLPHEILEMTNKFMTDPIRILVK 221
Cdd:PRK01297  222 GRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 222 RDELTLEGIKQFFVAVEREEwKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKE 301
Cdd:PRK01297  302 PENVASDTVEQHVYAVAGSD-KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEG 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 302 FRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQID- 380
Cdd:PRK01297  381 FREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISc 460

                  ...
gi 2288627546 381 EMP 383
Cdd:PRK01297  461 EMP 463
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
230-360 1.52e-63

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: 199.27  E-value: 1.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 230 IKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRV 309
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2288627546 310 LISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFV 360
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PTZ00110 PTZ00110
helicase; Provisional
8-371 2.92e-60

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 203.85  E-value: 2.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546   8 ATSGSARKRLLKEEDMTKVEFEtseevDV---TPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQS 84
Cdd:PTZ00110  102 ALSSKEVDEIRKEKEITIIAGE-----NVpkpVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAET 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  85 GTGKTATFSISVLQCLDIQGLLALGD---------------YMNVQC----------HACI-GGTNVGEDIRKLDYGQHV 138
Cdd:PTZ00110  177 GSGKTLAFLLPAIVHINAQPLLRYGDgpivlvlaptrelaeQIREQCnkfgasskirNTVAyGGVPKRGQIYALRRGVEI 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 139 VAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTD-PIR 217
Cdd:PTZ00110  257 LIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVH 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 218 ILVKRDELTL-EGIKQFFVAVEREEwKFDTLCDLYDTLTI--TQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKE 294
Cdd:PTZ00110  337 VNVGSLDLTAcHNIKQEVFVVEEHE-KRGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEE 415
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2288627546 295 RESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDI 371
Cdd:PTZ00110  416 RTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
39-384 1.81e-58

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 199.79  E-value: 1.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL------------DIQGL- 105
Cdd:PRK04537   10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrkpeDPRALi 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 LALGDYMNVQCH--------------ACI-GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRT-RAIKMLVLDEAD 169
Cdd:PRK04537   90 LAPTRELAIQIHkdavkfgadlglrfALVyGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSlHACEICVLDEAD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 170 EMLNKGFKEQIYDVYRYLPPAT--QVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQ--FFVAverEEWKFD 245
Cdd:PRK04537  170 RMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQriYFPA---DEEKQT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 246 TLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQV 325
Cdd:PRK04537  247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2288627546 326 SLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPM 384
Cdd:PRK04537  327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
40-379 5.30e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 186.72  E-value: 5.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKT-----ATFSiSVLQCLDIQG---------L 105
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFH-YLLSHPAPEDrkvnqpralI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 LALGDYMNVQCHA---------------CIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADE 170
Cdd:PRK04837   89 MAPTRELAVQIHAdaeplaqatglklglAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 171 MLNKGFKEQIYDVYRYLPPATQ--VVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQ--FFVAVE-------- 238
Cdd:PRK04837  169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEekmrllqt 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 239 --REEWKfdtlcdlydtltiTQAVIFCNTKRKV----DWLT-EKMReanftVSSMHGDMPQKERESIMKEFRSGASRVLI 311
Cdd:PRK04837  249 liEEEWP-------------DRAIIFANTKHRCeeiwGHLAaDGHR-----VGLLTGDVAQKKRLRILEEFTRGDLDILV 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2288627546 312 STDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQI 379
Cdd:PRK04837  311 ATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
39-373 4.71e-54

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 186.53  E-value: 4.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVL-QCLDI--------QGLLA-- 107
Cdd:PLN00206  122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsRCCTIrsghpseqRNPLAmv 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 -----------------LGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADE 170
Cdd:PLN00206  202 ltptrelcvqvedqakvLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 171 MLNKGFKEQIYDVYRYLPpATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKfdtlCDL 250
Cdd:PLN00206  282 MLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK----QKL 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 251 YDTLTITQ-----AVIFCNTKRKVDWLTEKMREAN-FTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQ 324
Cdd:PLN00206  357 FDILKSKQhfkppAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2288627546 325 VSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQ 373
Cdd:PLN00206  437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
40-218 1.64e-53

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: 175.95  E-value: 1.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGL-------LA 107
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDpkkdvIQALilvptreLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 L---------GDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKE 178
Cdd:cd17940    81 LqtsqvckelGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2288627546 179 QIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17940   161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
45-218 7.79e-52

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: 171.60  E-value: 7.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  45 LREDLLRGIYAYGFEKPSAIQQRAIKQIIKG--RDVIAQSQSGTGKTATFSISVLQCLDI-----QGL-------LA--- 107
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPtlkspQALclaptreLArqi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 ------LGDYMNVQCHACIGGTNV--GEDIRkldygQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLN-KGFKE 178
Cdd:cd17963    81 gevvekMGKFTGVKVALAVPGNDVprGKKIT-----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2288627546 179 QIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17963   156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
49-218 1.56e-43

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: 149.72  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGLL----------------A 107
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDlerrhPQVLIlaptreiavqihdvfkK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 LGDYM-NVQCHACIGGTNVGEDIRKLDyGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRY 186
Cdd:cd17943    81 IGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2288627546 187 LPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17943   160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
40-220 8.90e-41

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: 143.25  E-value: 8.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGL-------LA 107
Cdd:cd17950     4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEpvdgqVSVLvichtreLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 ---------LGDYM-NVQCHACIGGTNVGEDIRKL-DYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNK-G 175
Cdd:cd17950    84 fqisneyerFSKYMpNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2288627546 176 FKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILV 220
Cdd:cd17950   164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEXDc smart00487
DEAD-like helicases superfamily;
53-233 6.37e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 140.70  E-value: 6.37e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546   53 IYAYGFEKPSAIQQRAIKQIIKG-RDVIAQSQSGTGKTATFSISVLQCLDIQG--------------------LLALGDY 111
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKggrvlvlvptrelaeqwaeeLKKLGPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  112 MNVQCHACIGGTNVGEDIRKLDYGQ-HVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPA 190
Cdd:smart00487  81 LGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2288627546  191 TQVVLISATLPHEILEMTNKFMTDPIRILVKRdeLTLEGIKQF 233
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
62-206 5.60e-39

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: 136.99  E-value: 5.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  62 SAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-----IQGLL----------------ALGDYMNVQCHACI 120
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDkldngPQALVlaptrelaeqiyeelkKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 121 GGTNVGEDIRKLDyGQHVVAGTPGRVFDMIRRRSlRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATL 200
Cdd:pfam00270  81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158

                  ....*.
gi 2288627546 201 PHEILE 206
Cdd:pfam00270 159 PRNLED 164
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
242-351 2.31e-38

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: 133.49  E-value: 2.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 242 WKFDTLCDLYDTLTITQAVIFCNTKRKVDwlTEKMREA-NFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGL 320
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2288627546 321 DVPQVSLIINYDLPNNRELYIHRIGRSGRYG 351
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
40-215 7.42e-36

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: 130.04  E-value: 7.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQG------------- 104
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLseDPYGifalvltptrela 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 105 ------LLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRT---RAIKMLVLDEADEMLNKG 175
Cdd:cd17955    81 yqiaeqFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2288627546 176 FKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDP 215
Cdd:cd17955   161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
39-218 1.47e-35

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: 129.35  E-value: 1.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD-------IQGLL----- 106
Cdd:cd17959     2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKahsptvgARALIlsptr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 107 -----------ALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKG 175
Cdd:cd17959    82 elalqtlkvtkELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2288627546 176 FKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17959   162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
49-218 1.26e-32

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: 121.21  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVL--------------------------QCLDI 102
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILerllyrpkkkaatrvlvlvptrelamQCFSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 103 qgLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRR-RSLRTRAIKMLVLDEADEMLNKGFKEQIY 181
Cdd:cd17947    81 --LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELK 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2288627546 182 DVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17947   159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
49-212 8.01e-32

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: 119.61  E-value: 8.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQII-KGRDVIAQSQSGTGKTATFSISVLQCL----------DIQGL-------LA--- 107
Cdd:cd17964     5 LLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpagrrsGVSALiisptreLAlqi 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 ------LGDYM-NVQCHACIGGTNVGEDIRKL-DYGQHVVAGTPGRVFDMIRRRSLRTRA--IKMLVLDEADEMLNKGFK 177
Cdd:cd17964    85 aaeakkLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKAFtdLDYLVLDEADRLLDMGFR 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2288627546 178 EQIYDVYRYLPPA----TQVVLISATLPHEILEMTNKFM 212
Cdd:cd17964   165 PDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
39-218 1.06e-31

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: 118.96  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQ-------------------- 98
Cdd:cd17954     1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQallenpqrffalvlaptrel 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  99 CLDIQG-LLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRR-RSLRTRAIKMLVLDEADEMLNKGF 176
Cdd:cd17954    81 AQQISEqFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLLNMDF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2288627546 177 KEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17954   161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
39-212 1.12e-31

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: 120.84  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLAlGDYMNVQCHA 118
Cdd:cd18052    44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTA-SSFSEVQEPQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 119 CI-------------------------------GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDE 167
Cdd:cd18052   123 ALivaptrelanqiflearkfsygtcirpvvvyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2288627546 168 ADEMLNKGFKEQIYDVYRYL--PPAT--QVVLISATLPHEILEMTNKFM 212
Cdd:cd18052   203 ADRMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFL 251
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
40-215 3.03e-31

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 117.81  E-value: 3.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  40 FDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQ---CLDI-----------QGL 105
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQivvALILepsrelaeqtyNCI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 LALGDYMN---VQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYD 182
Cdd:cd17938    81 ENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 183 VYRYLPPAT------QVVLISATLpH--EILEMTNKFMTDP 215
Cdd:cd17938   161 IYNRIPKITsdgkrlQVIVCSATL-HsfEVKKLADKIMHFP 200
HELICc smart00490
helicase superfamily c-terminal domain;
270-351 3.65e-31

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 113.46  E-value: 3.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  270 DWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGR 349
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 2288627546  350 YG 351
Cdd:smart00490  81 AG 82
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
39-222 6.06e-31

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: 117.59  E-value: 6.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVlqcldIQGLLALGDYMN----- 113
Cdd:cd17967     1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPI-----ISKLLEDGPPSVgrgrr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 114 -------------------------------VQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKM 162
Cdd:cd17967    76 kaypsalilaptrelaiqiyeearkfsyrsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2288627546 163 LVLDEADEMLNKGFKEQIYDVYRY--LPPAT--QVVLISATLPHEILEMTNKFMTDPIRILVKR 222
Cdd:cd17967   156 LVLDEADRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
39-226 8.37e-31

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: 117.43  E-value: 8.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKG--RDVIAQSQSGTGKTATFSISVLQ------------CLDIQG 104
Cdd:cd18048    19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSrvdalklypqclCLSPTF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 105 LLAL---------GDYMN-VQCHACIGGTNVGediRKLDYGQHVVAGTPGRVFD-MIRRRSLRTRAIKMLVLDEADEMLN 173
Cdd:cd18048    99 ELALqtgkvveemGKFCVgIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMIN 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2288627546 174 -KGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELT 226
Cdd:cd18048   176 vQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
49-218 4.46e-30

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: 114.43  E-value: 4.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGD------------------ 110
Cdd:cd17952     1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEgpiavivaptrelaqqiy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 111 --------YMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYD 182
Cdd:cd17952    81 leakkfgkAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2288627546 183 VYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17952   161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
44-218 1.47e-29

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: 114.01  E-value: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  44 GLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ----------GL-------L 106
Cdd:cd17953    18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvkpgegpiGLimaptreL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 107 ALGDY---------MNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMI---RRRSLRTRAIKMLVLDEADEMLNK 174
Cdd:cd17953    98 ALQIYveckkfskaLGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDM 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2288627546 175 GFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17953   178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
49-218 1.71e-28

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: 110.15  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGD-------------YMNVQ 115
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDgpivlvlaptrelAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 116 ------CH------ACI-GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYD 182
Cdd:cd17966    81 qeankfGGssrlrnTCVyGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2288627546 183 VYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17966   161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
49-218 1.94e-28

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: 110.51  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSIS-VLQCLD-------IQG---------------- 104
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEqekklpfIKGegpyglivcpsrelar 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 105 -----------LLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLN 173
Cdd:cd17951    81 qthevieyyckALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2288627546 174 KGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
49-218 3.28e-28

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: 109.59  E-value: 3.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL----------DIQGL-------LA---- 107
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkanlkkgQVGALiisptreLAtqiy 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 --LGDYMNVQ-----CHACIGGTNVGEDIRKLD-YGQHVVAGTPGRVFDMIRRRS--LRTRAIKMLVLDEADEMLNKGFK 177
Cdd:cd17960    81 evLQSFLEHHlpklkCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 178 EQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17960   161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
49-218 3.88e-28

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: 109.18  E-value: 3.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQ--------------------CLDIQG---L 105
Cdd:cd17962     1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIrcltehrnpsaliltptrelAVQIEDqakE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 LALGdYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYR 185
Cdd:cd17962    81 LMKG-LPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2288627546 186 YLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17962   160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
49-218 1.20e-27

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: 107.94  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ----------GLLALGDY--MNVQC 116
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpipreqrngpGVLVLTPTreLALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 117 HA-------------CI-GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYD 182
Cdd:cd17958    81 EAecskysykglksvCVyGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2288627546 183 VYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17958   161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
49-220 1.79e-27

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: 107.68  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL----DIQGLLA----------------- 107
Cdd:cd17957     1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkprKKKGLRAlilaptrelasqiyrel 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 108 --LGDYMNVQCHACIGGTNVG-----EDIRKLDygqhVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQI 180
Cdd:cd17957    81 lkLSKGTGLRIVLLSKSLEAKakdgpKSITKYD----ILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288627546 181 YDVYRYLP-PATQVVLISATLPHEILEMTNKFMTDPIRILV 220
Cdd:cd17957   157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
39-222 2.61e-27

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: 108.59  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQG-------------- 104
Cdd:cd18051    22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGpgeslpsesgyygr 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 105 --------LLALGDYMNVQCH-------------ACI--GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIK 161
Cdd:cd18051   102 rkqyplalVLAPTRELASQIYdearkfayrsrvrPCVvyGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2288627546 162 MLVLDEADEMLNKGFKEQIYDVYRY--LPPA--TQVVLISATLPHEILEMTNKFMTDPIRILVKR 222
Cdd:cd18051   182 YLVLDEADRMLDMGFEPQIRRIVEQdtMPPTgeRQTLMFSATFPKEIQMLARDFLDNYIFLAVGR 246
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
49-216 3.14e-27

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: 106.90  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL--------DIQGLLAL------------ 108
Cdd:cd17961     5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaesgEEQGTRALilvptrelaqqv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 109 GDYMNVQCHACiggtnvGEDIRKLDYGQH---------------VVAGTPGRVFDMIRRRSLRTRA-IKMLVLDEADEML 172
Cdd:cd17961    85 SKVLEQLTAYC------RKDVRVVNLSASssdsvqrallaekpdIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2288627546 173 NKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPI 216
Cdd:cd17961   159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
50-220 2.14e-26

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: 104.68  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  50 LRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ------GLLAL--------------- 108
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwtpedGLGALiisptrelamqifev 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 109 ----GDYMNVQCHACIGGTNVGEDIRKLDyGQHVVAGTPGRVFD-MIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDV 183
Cdd:cd17941    82 lrkvGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2288627546 184 YRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILV 220
Cdd:cd17941   161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
39-215 2.16e-24

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: 99.41  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  39 TFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKG--RDVIAQSQSGTGKTATFSISVL----------QCLDIQGL- 105
Cdd:cd18047     2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLsqvepankypQCLCLSPTy 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 106 -LALGD----------YMNVQCHACIGGTNVGEDIRKLDygqHVVAGTPGRVFD-MIRRRSLRTRAIKMLVLDEADEML- 172
Cdd:cd18047    82 eLALQTgkvieqmgkfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2288627546 173 NKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDP 215
Cdd:cd18047   159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
49-218 4.25e-24

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: 98.93  E-value: 4.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLD----------IQGLLAL---------- 108
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeetkDDGPYALilaptrelaq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 109 ---------GDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQ 179
Cdd:cd17945    81 qieeetqkfAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2288627546 180 IYDVYRYLPP--------------------ATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17945   161 VTKILDAMPVsnkkpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
57-218 1.05e-23

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: 97.66  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  57 GFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFS---ISVLQCLDI-----QGLLAL---------------GDYMN 113
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLlpiIQRLLSLEPrvdrsDGTLALvlvptrelalqiyevLEKLL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 114 VQCHACIGGTNVGEDIRK-----LDYGQHVVAGTPGRVFDMIRR-RSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYL 187
Cdd:cd17949    90 KPFHWIVPGYLIGGEKRKsekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2288627546 188 -------------PPATQVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd17949   170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
50-199 1.48e-23

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: 97.05  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  50 LRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQ------------------------CLDIQG- 104
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklkfkprngtgviiisptrelALQIYGv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 105 LLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRS-LRTRAIKMLVLDEADEMLNKGFKEQIYDV 183
Cdd:cd17942    82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
                         170
                  ....*....|....*.
gi 2288627546 184 YRYLPPATQVVLISAT 199
Cdd:cd17942   162 IKLLPKRRQTMLFSAT 177
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
58-218 2.02e-21

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: 91.99  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  58 FEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGD-------------YMNVQ------CHA 118
Cdd:cd18049    44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDgpiclvlaptrelAQQVQqvaaeyGRA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 119 C-------IGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT 191
Cdd:cd18049   124 CrlkstciYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 203
                         170       180
                  ....*....|....*....|....*..
gi 2288627546 192 QVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd18049   204 QTLMWSATWPKEVRQLAEDFLKDYIHI 230
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
58-218 4.98e-21

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: 91.61  E-value: 4.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  58 FEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGD-------------YMNVQCHA------ 118
Cdd:cd18050    82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDgpiclvlaptrelAQQVQQVAddygks 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 119 ------CI-GGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT 191
Cdd:cd18050   162 srlkstCIyGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
                         170       180
                  ....*....|....*....|....*..
gi 2288627546 192 QVVLISATLPHEILEMTNKFMTDPIRI 218
Cdd:cd18050   242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
49-178 7.24e-18

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: 81.90  E-value: 7.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIK-GRDVIAQSQSGTGKTATFSISVLQ-CLD----------IQGLLAL-------- 108
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILErLLSqkssngvggkQKPLRALiltptrel 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 109 -----------GDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRR-----SLRTraIKMLVLDEADEML 172
Cdd:cd17946    81 avqvkdhlkaiAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehlaNLKS--LRFLVLDEADRML 158

                  ....*..
gi 2288627546 173 NKG-FKE 178
Cdd:cd17946   159 EKGhFAE 165
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
64-212 1.03e-17

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: 80.66  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  64 IQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQGL----------------LA---------LGDYMNVQC 116
Cdd:cd17944    16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqeDQQPRkrgrapkvlvlaptreLAnqvtkdfkdITRKLSVAC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 117 HacIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVY--RYLPPAT--- 191
Cdd:cd17944    96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvSYKKDSEdnp 173
                         170       180
                  ....*....|....*....|.
gi 2288627546 192 QVVLISATLPHEILEMTNKFM 212
Cdd:cd17944   174 QTLLFSATCPDWVYNVAKKYM 194
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
49-210 1.43e-14

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: 72.40  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  49 LLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGDY----------------- 111
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFnaprglvitpsrelaeq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 112 -------------MNVQChacIGGTNVGEDIRKLDYGQ-HVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFK 177
Cdd:cd17948    81 igsvaqslteglgLKVKV---ITGGRTKRQIRNPHFEEvDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2288627546 178 EQIYDVYRYLP-------------PATQVVLISATLPHEILEMTNK 210
Cdd:cd17948   158 EKLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
258-357 2.38e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 68.60  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 258 QAVIFCNTKRKVDWLTEKMREANFTV------SSMHGD--MPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLII 329
Cdd:COG1111   355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
                          90       100       110
                  ....*....|....*....|....*....|
gi 2288627546 330 NYDL-PNnrEL-YIHRIGRSGRYGRKGVAI 357
Cdd:COG1111   435 FYEPvPS--EIrSIQRKGRTGRKREGRVVV 462
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
244-346 4.42e-12

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 62.99  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 244 FDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMRE-----ANFTVSSMHG----------DMPQKERESIMKEFRSGASR 308
Cdd:cd18802    13 IEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2288627546 309 VLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGR 346
Cdd:cd18802    93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
259-345 4.73e-12

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: 62.88  E-value: 4.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 259 AVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGAS--RVLISTDVWARGLDVPQVSLIINYDLPNN 336
Cdd:cd18793    30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
                          90
                  ....*....|....*...
gi 2288627546 337 ---------RelyIHRIG 345
Cdd:cd18793   110 paveeqaidR---AHRIG 124
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
75-199 5.48e-12

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: 63.19  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  75 GRDVIAQSQSGTGKTATFSISVLQCLDIQGL----------LALGDYMNVQ--------CHACIGGTNVGEDIRKLDYGQ 136
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKKGKkvlvlvptkaLALQTAERLRelfgpgirVAVLVGGSSAEEREKNKLGDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2288627546 137 HVVAGTPGRVFDMIRR-RSLRTRAIKMLVLDEADEMLNKGFKEQIYD--VYRYLPPATQVVLISAT 199
Cdd:cd00046    81 DIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
260-369 1.02e-11

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 66.32  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 260 VIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNREL 339
Cdd:COG0514   234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
                          90       100       110
                  ....*....|....*....|....*....|
gi 2288627546 340 YIHRIGRSGRYGRKGVAINFVKNDDIRILR 369
Cdd:COG0514   314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
259-359 2.95e-11

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: 60.69  E-value: 2.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 259 AVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRE 338
Cdd:cd18794    33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
                          90       100
                  ....*....|....*....|.
gi 2288627546 339 LYIHRIGRSGRYGRKGVAINF 359
Cdd:cd18794   113 SYYQESGRAGRDGLPSECILF 133
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
258-346 9.31e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.51  E-value: 9.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 258 QAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNR 337
Cdd:COG1061   307 KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP 386

                  ....*....
gi 2288627546 338 ELYIHRIGR 346
Cdd:COG1061   387 REFIQRLGR 395
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
272-356 1.87e-10

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: 58.89  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 272 LTEKMReANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDlpnnrelyIHRIGRS---- 347
Cdd:cd18811    54 LKERFR-PELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--------AERFGLSqlhq 124
                          90
                  ....*....|.
gi 2288627546 348 --GRYGRKGVA 356
Cdd:cd18811   125 lrGRVGRGDHQ 135
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
290-354 2.28e-10

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: 58.14  E-value: 2.28e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2288627546 290 MPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDlPNNREL-YIHRIGRSGRyGRKG 354
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR-KRQG 137
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
260-369 4.06e-10

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 61.27  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 260 VIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNREL 339
Cdd:PRK11057  240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                          90       100       110
                  ....*....|....*....|....*....|
gi 2288627546 340 YIHRIGRSGRYGRKGVAINFVKNDDIRILR 369
Cdd:PRK11057  320 YYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
259-353 6.08e-10

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.01  E-value: 6.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 259 AVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSG--ASRVLISTDVWARGLDVPQVSLIINYDLPNN 336
Cdd:COG0553   552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
                          90
                  ....*....|....*..
gi 2288627546 337 RELYIHRIGRSGRYGRK 353
Cdd:COG0553   632 PAVEEQAIDRAHRIGQT 648
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
44-375 1.61e-08

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: 56.38  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  44 GLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCL-------------------D--- 101
Cdd:COG1205    40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALledpgatalylyptkalarDqlr 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 102 -IQGLLALGDyMNVQCHACIGGTNVGE--DIRKldyGQHVVAGTPgrvfDMIRRRSLRT--------RAIKMLVLDEAde 170
Cdd:COG1205   120 rLRELAEALG-LGVRVATYDGDTPPEErrWIRE---HPDIVLTNP----DMLHYGLLPHhtrwarffRNLRYVVIDEA-- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 171 mlnkgfkeQIYD----------------VYRYLPPATQVVLISATL--PHEILE-MTNK------------------FMT 213
Cdd:COG1205   190 --------HTYRgvfgshvanvlrrlrrICRHYGSDPQFILASATIgnPAEHAErLTGRpvtvvdedgsprgertfvLWN 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 214 DPIRILVKRDELTLEGIKQFFVAVEREewkfdtlcdlydtltiTQAVIFCNTKRKV----DWLTEKMREANFT--VSSMH 287
Cdd:COG1205   262 PPLVDDGIRRSALAEAARLLADLVREG----------------LRTLVFTRSRRGAellaRYARRALREPDLAdrVAAYR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 288 GDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAInFVKNDDIri 367
Cdd:COG1205   326 AGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDDP-- 402

                  ....*...
gi 2288627546 368 lrdIEQYY 375
Cdd:COG1205   403 ---LDQYY 407
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
275-357 1.88e-08

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 53.04  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 275 KMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDlPNN---RELYIHRiGRSGRYG 351
Cdd:cd18792    55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED-ADRfglSQLHQLR-GRVGRGK 132

                  ....*.
gi 2288627546 352 RKGVAI 357
Cdd:cd18792   133 HQSYCY 138
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
163-385 2.78e-08

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 55.47  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 163 LVLDEAdemlnkgfkeQIYDVYrYLPP-----------ATQVVLISATLPHEILEmtnkFMTDPIRILVKRDELTLEGIK 231
Cdd:COG1203   272 IILDEV----------QAYPPY-MLALllrllewlknlGGSVILMTATLPPLLRE----ELLEAYELIPDEPEELPEYFR 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 232 QFF---VAVEREEWKFDTLCDLYDTL--TITQAVIFCNTKRKVDWLTEKMREANFTVSSM--HGDMPQKER----ESIMK 300
Cdd:COG1203   337 AFVrkrVELKEGPLSDEELAELILEAlhKGKSVLVIVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRseieKEIKE 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 301 EFRSGASRVLISTDVWARGLDV----------PqVSLII--------NYDLPNNRELYIHRIGRSGR---YGRKGVAI-- 357
Cdd:COG1203   417 RLERGKPCILVSTQVVEAGVDIdfdvvirdlaP-LDSLIqragrcnrHGRKEEEGNVYVFDPEDEGGgyvYDKPLLERtr 495
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2288627546 358 ----NFVKNDDIRILRDIEQYYSTQIDEMPMN 385
Cdd:COG1203   496 ellrEHDEILPEDKRELIEEYYRELYELLPDE 527
PRK13766 PRK13766
Hef nuclease; Provisional
243-384 2.87e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 55.65  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 243 KFDTLCDLY-DTLTI---TQAVIFCNTKRKVDWLTEKMREANFTV------SSMHGD--MPQKERESIMKEFRSGASRVL 310
Cdd:PRK13766  348 KLEKLREIVkEQLGKnpdSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEFNVL 427
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2288627546 311 ISTDVWARGLDVPQVSLIINYDlPNNREL-YIHRIGRSGRyGRKGVAINFVKNDDirilRDIEQYYSTQIDEMPM 384
Cdd:PRK13766  428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEIrSIQRKGRTGR-QEEGRVVVLIAKGT----RDEAYYWSSRRKEKKM 496
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
309-360 7.94e-08

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 49.24  E-value: 7.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2288627546 309 VLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYG-RKGVAINFV 360
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
260-384 1.72e-07

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 53.36  E-value: 1.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  260 VIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNREL 339
Cdd:PLN03137   684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2288627546  340 YIHRIGRSGRYG-RKGVAINFVKNDDIRILRDIEQyysTQIDEMPM 384
Cdd:PLN03137   764 YHQECGRAGRDGqRSSCVLYYSYSDYIRVKHMISQ---GGVEQSPM 806
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
163-353 1.90e-07

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: 52.43  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 163 LVLDEAD--EMLNKGFKEQIYDVYRYLppATQVVLISATLPHEILEMTNKfmtdpIRILVKRDELTLEGIKQFFVAVERE 240
Cdd:cd09639   127 LIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEK-----IGYVEENEPLDLKPNERAPFIKIES 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 241 EWKFD--TLCDLYDTLT-ITQAVIFCNTKRKV----DWLTEKMREANFTVssMHGDMPQKERES----IMKEFRSGASRV 309
Cdd:cd09639   200 DKVGEisSLERLLEFIKkGGSVAIIVNTVDRAqefyQQLKEKGPEEEIML--IHSRFTEKDRAKkeaeLLLEFKKSEKFV 277
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2288627546 310 LISTDVWARGLDVpQVSLIINYDLPNNRelYIHRIGRSGRYGRK 353
Cdd:cd09639   278 IVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGEK 318
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
138-218 2.38e-07

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: 51.61  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 138 VVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIR 217
Cdd:cd17965   164 ILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVR 243

                  .
gi 2288627546 218 I 218
Cdd:cd17965   244 I 244
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
265-349 1.01e-06

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: 48.40  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 265 TKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYD------LPNNRE 338
Cdd:cd18790    36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegfLRSETS 115
                          90
                  ....*....|.
gi 2288627546 339 LyIHRIGRSGR 349
Cdd:cd18790   116 L-IQTIGRAAR 125
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
65-381 1.44e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 50.28  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  65 QQRAIKQ-IIKGRDVIAQSQSGTGKTATFSISVLQCLDIQG-------LLAL---------GDYMNVqchacigGTNVG- 126
Cdd:COG1204    27 QAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGkalyivpLRALasekyrefkRDFEEL-------GIKVGv 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 127 ------EDIRKLDYGQHVVAgTPGRVFDMIRRRSLRTRAIKMLVLDEA----DEmlNKGFK-EQIYDVYRYLPPATQVVL 195
Cdd:COG1204   100 stgdydSDDEWLGRYDILVA-TPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARLRRLNPEAQIVA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 196 ISATL--PHEILE-MTNKFMTDPIRIlVKRDELTLEGIKQFFVAVEREEwkFDTLCDL-YDTLTI-TQAVIFCNTKRKVD 270
Cdd:COG1204   177 LSATIgnAEEIAEwLDAELVKSDWRP-VPLNEGVLYDGVLRFDDGSRRS--KDPTLALaLDLLEEgGQVLVFVSSRRDAE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 271 WLTEKMREA-----------------------------NFTVSSM--------HGDMPQKERESIMKEFRSGASRVLIST 313
Cdd:COG1204   254 SLAKKLADElkrrltpeereeleelaeellevseethtNEKLADClekgvafhHAGLPSELRRLVEDAFREGLIKVLVAT 333
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2288627546 314 DVWARGLDVPQVSLII-NYDLPNNREL----YIHRIGRSGR--YGRKGVAInFVKNDDIRILRDIEQYYSTQIDE 381
Cdd:COG1204   334 PTLAAGVNLPARRVIIrDTKRGGMVPIpvleFKQMAGRAGRpgYDPYGEAI-LVAKSSDEADELFERYILGEPEP 407
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
287-356 1.78e-06

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 47.34  E-value: 1.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2288627546 287 HGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLII--NYDLPNNRELYIHRiGRSGRYGRKGVA 356
Cdd:cd18810    58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
258-357 3.57e-06

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: 46.39  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 258 QAVIFCNTKRKVDWLTEKMREANFtvssMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIIN----YDL 333
Cdd:cd18795    45 PVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYDG 120
                          90       100       110
                  ....*....|....*....|....*....|
gi 2288627546 334 PNNREL----YIHRIGRSGR--YGRKGVAI 357
Cdd:cd18795   121 KGYRELspleYLQMIGRAGRpgFDTRGEAI 150
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
274-329 3.96e-06

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 48.89  E-value: 3.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2288627546 274 EKMREA--NFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLII 329
Cdd:COG1200   495 EELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMV 552
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
286-329 3.99e-06

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 48.99  E-value: 3.99e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2288627546 286 MHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLII 329
Cdd:PRK10917  511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMV 554
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
259-346 1.15e-05

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 44.09  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 259 AVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERES---IMKEFRSGASRVLISTDVWARGLDVPQVSLIInYDLP- 334
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDealILLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPt 87
                          90
                  ....*....|..
gi 2288627546 335 NNRELYIHRIGR 346
Cdd:cd18799    88 ESRTLFLQMLGR 99
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
257-354 1.98e-05

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: 44.16  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 257 TQAVIFCNTKRKVDWLTEKMREANFTvssmhGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQ--VSLIINYDLP 334
Cdd:cd18789    50 DKIIVFTDNVEALYRYAKRLLKPFIT-----GETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISGHGG 124
                          90       100
                  ....*....|....*....|
gi 2288627546 335 NNRElYIHRIGRSGRYGRKG 354
Cdd:cd18789   125 SRRQ-EAQRLGRILRPKKGG 143
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
261-349 3.71e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.41  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 261 IFCNTKRKVDWLTEKMREA------NFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLP 334
Cdd:cd18796    43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
                          90
                  ....*....|....*
gi 2288627546 335 NNRELYIHRIGRSGR 349
Cdd:cd18796   123 KSVARLLQRLGRSGH 137
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
292-357 5.20e-05

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 44.16  E-value: 5.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2288627546 292 QKERESIMKEFRSGASRVLISTDVWARGLDVPQVSL--IINYD----LPNNR------ELYIHRIGRSGRYGRKGVAI 357
Cdd:cd18804   130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLvgILNADsglnSPDFRaserafQLLTQVSGRAGRGDKPGKVI 207
PRK01172 PRK01172
ATP-dependent DNA helicase;
65-360 1.23e-04

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 44.10  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  65 QQRAIKQIIKGRDVIAQSQSGTGKT--------ATFS-------ISVLQCLDIQG---LLALGDyMNVQCHACIGGTNVG 126
Cdd:PRK01172   27 QRMAIEQLRKGENVIVSVPTAAGKTliaysaiyETFLaglksiyIVPLRSLAMEKyeeLSRLRS-LGMRVKISIGDYDDP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 127 ED-IRKLDygqhVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEAdEMLNKGFK----EQIYDVYRYLPPATQVVLISATLP 201
Cdd:PRK01172  106 PDfIKRYD----VVILTSEKADSLIHHDPYIINDVGLIVADEI-HIIGDEDRgptlETVLSSARYVNPDARILALSATVS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 202 H--EILEMTN------KFMTDPIRI-LVKRDELTLEGikqffvaveREEWKFDTLCDLYDTLTIT-QAVIFCNTKRKVDW 271
Cdd:PRK01172  181 NanELAQWLNasliksNFRPVPLKLgILYRKRLILDG---------YERSQVDINSLIKETVNDGgQVLVFVSSRKNAED 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 272 LTEKMRE-----ANFTVSSM--------------------HGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPqVS 326
Cdd:PRK01172  252 YAEMLIQhfpefNDFKVSSEnnnvyddslnemlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-AR 330
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2288627546 327 LIINYDLPNNRELYI---------HRIGRSGR--YGRKGVAINFV 360
Cdd:PRK01172  331 LVIVRDITRYGNGGIrylsnmeikQMIGRAGRpgYDQYGIGYIYA 375
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
47-168 2.73e-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: 41.86  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  47 EDLLRgiYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLqCLDIQG---------LLALgdyMNVQCH 117
Cdd:cd18018     1 LKLLR--RVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL-LLRRRGpgltlvvspLIAL---MKDQVD 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2288627546 118 --------ACIGGTN----VGEDIRKLDYGQ-HVVAGTPGRVFD-MIRRRSLRTRAIKMLVLDEA 168
Cdd:cd18018    75 alpraikaAALNSSLtreeRRRILEKLRAGEvKILYVSPERLVNeSFRELLRQTPPISLLVVDEA 139
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
47-216 1.98e-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: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546  47 EDLLRGIYayGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSI-SVLQ---CLDIQGLLALGDYMNVQCH----- 117
Cdd:cd17920     1 EQILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLpALLLdgvTLVVSPLISLMQDQVDRLQqlgir 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 118 -ACIGGT----NVGEDIRKLDYGQ-HVVAGTP-----GRVFDMIRRRSLRTRaIKMLVLDEA-----------DEMLNKG 175
Cdd:cd17920    79 aAALNSTlspeEKREVLLRIKNGQyKLLYVTPerllsPDFLELLQRLPERKR-LALIVVDEAhcvsqwghdfrPDYLRLG 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2288627546 176 -FKEQIYDVyrylppatQVVLISATLP----HEILEMTNkfMTDPI 216
Cdd:cd17920   158 rLRRALPGV--------PILALTATATpevrEDILKRLG--LRNPV 193
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
258-357 2.65e-03

C-terminal helicase domain of HrQ family helicases; 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. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 38.01  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288627546 258 QAVIFCNTKRKVD----WLTEKMREANF---TVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIIN 330
Cdd:cd18797    37 KTIVFCRSRKLAElllrYLKARLVEEGPlasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
                          90       100
                  ....*....|....*....|....*..
gi 2288627546 331 YDLPNNRELYIHRIGRSGRYGRKGVAI 357
Cdd:cd18797   117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
PRK05580 PRK05580
primosome assembly protein PriA; Validated
296-357 4.56e-03

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 38.98  E-value: 4.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2288627546 296 ESIMKEFRSGASRVLISTDVWARGLDVPQVSL--IINYDL----PNNR------ELYIHRIGRSGRYGRKGVAI 357
Cdd:PRK05580  470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTLvgVLDADLglfsPDFRasertfQLLTQVAGRAGRAEKPGEVL 543
 
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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