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Conserved domains on  [gi|11513344]
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Chain A, YEAST INITIATION FACTOR 4A

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 ...
9-393 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: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    9 ESQIQTNYDKVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVK 88
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   89 APQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQ-IVVGTPGRVFDNIQRRRFRTDKIK*FI 167
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVhMVVGTPGRVYDMIDKRHLRVDDLKLFI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  168 LDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEYKY 247
Cdd:PTZ00424 176 LDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKF 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  248 ECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQ 327
Cdd:PTZ00424 256 DTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11513344  328 VSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLL 393
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
9-393 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    9 ESQIQTNYDKVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVK 88
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   89 APQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQ-IVVGTPGRVFDNIQRRRFRTDKIK*FI 167
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVhMVVGTPGRVYDMIDKRHLRVDDLKLFI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  168 LDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEYKY 247
Cdd:PTZ00424 176 LDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKF 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  248 ECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQ 327
Cdd:PTZ00424 256 DTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11513344  328 VSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLL 393
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
22-386 1.67e-133

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 388.74  E-value: 1.67e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV-KAPQAL*LAPTRE 100
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 101 LALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGF 179
Cdd:COG0513  83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 180 KEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEyKYECLTDLYDSISV 259
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 260 TQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPAN 339
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 11513344 340 KENYIHrigrggrfgrkgVAINFVTNEDVGA*RELEKFYSTQIEELP 386
Cdd:COG0513 322 PEDYVHrigrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
23-222 9.33e-126

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: 360.61  E-value: 9.33e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 182 QIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRIL 222
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
45-210 1.23e-57

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 185.52  E-value: 1.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    45 SAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACI 124
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   125 GGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRfRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*P 204
Cdd:pfam00270  81 GGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLP 159

                  ....*.
gi 11513344   205 NDVLEV 210
Cdd:pfam00270 160 RNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
36-236 3.02e-49

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 165.36  E-value: 3.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344     36 VFGYGFEEPSAIQQRAI*PIIEG-HDVLAQAQSGTGKTGTFSIAALQRIDtSVKAPQAL*LAPTRELALQIQKVV*ALAF 114
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    115 H*DIKVHACIGGTSFVEDAEGLR--DAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPP 192
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 11513344    193 TTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKkdELTLEGIKQF 236
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
9-393 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    9 ESQIQTNYDKVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVK 88
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   89 APQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQ-IVVGTPGRVFDNIQRRRFRTDKIK*FI 167
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVhMVVGTPGRVYDMIDKRHLRVDDLKLFI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  168 LDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEYKY 247
Cdd:PTZ00424 176 LDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKF 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  248 ECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQ 327
Cdd:PTZ00424 256 DTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11513344  328 VSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLL 393
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
22-386 1.67e-133

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 388.74  E-value: 1.67e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV-KAPQAL*LAPTRE 100
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 101 LALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGF 179
Cdd:COG0513  83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 180 KEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEyKYECLTDLYDSISV 259
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 260 TQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPAN 339
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 11513344 340 KENYIHrigrggrfgrkgVAINFVTNEDVGA*RELEKFYSTQIEELP 386
Cdd:COG0513 322 PEDYVHrigrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
23-222 9.33e-126

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: 360.61  E-value: 9.33e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 182 QIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRIL 222
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
25-222 3.63e-114

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: 331.21  E-value: 3.63e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  25 D*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQ 104
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 105 IQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLR-DAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQI 183
Cdd:cd17939  81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQyGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 11513344 184 YQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRIL 222
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
23-222 6.09e-93

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: 277.43  E-value: 6.09e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd18045  81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGqHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 182 QIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRIL 222
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
40-394 7.92e-79

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 250.10  E-value: 7.92e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   40 GFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQIQKVV*ALA-FH*DI 118
Cdd:PRK11776  23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLArFIPNI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  119 KVHACIGGTSFVEDAEGLR-DAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPPTTQVV 197
Cdd:PRK11776 103 KVLTLCGGVPMGPQIDSLEhGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  198 LLSAT*PNDVLEVTTKF*RNPVRILV--KKDELTLEgiKQFYvNVEEEEyKYECLTDLYDSISVTQAVIFCNTRRKVEEL 275
Cdd:PRK11776 183 LFSATYPEGIAAISQRFQRDPVEVKVesTHDLPAIE--QRFY-EVSPDE-RLPALQRLLLHHQPESCVVFCNTKKECQEV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  276 TTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKENYIHRIGRGGRFGR 355
Cdd:PRK11776 259 ADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGS 338
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 11513344  356 KGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLLN 394
Cdd:PRK11776 339 KGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLS 377
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
32-221 1.37e-77

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: 237.73  E-value: 1.37e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDT----SVKAPQAL*LAPTRELALQIQK 107
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 108 VV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQI 186
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKgPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 11513344 187 FTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
23-393 6.66e-68

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 225.88  E-value: 6.66e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:PRK11634   8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  103 LQIQKVV*ALAFH-*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFK 180
Cdd:PRK11634  88 VQVAEAMTDFSKHmRGVNVVALYGGQRYDVQLRALRQgPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  181 EQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEyKYECLTDLYDSISVT 260
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAEDFD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  261 QAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANK 340
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 11513344  341 ENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLL 393
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
28-221 9.96e-66

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: 207.43  E-value: 9.96e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  28 LDENLLRGVFGYGFEEPSAIQQRAI*PIIEG---HDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQ 104
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETAL-PLILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 105 IQKVV*ALAFH*DIKVHACIGGTSFveDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSS-GFKEQI 183
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDV--PRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQS 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 11513344 184 YQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
23-347 1.02e-65

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 215.19  E-value: 1.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQR-IDTSVK---APQAL*LAPT 98
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFPRRksgPPRILILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   99 RELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQ-IVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSS 177
Cdd:PRK11192  83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQdIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  178 GFKEQIYQIFTLLPPTTQVVLLSAT*P-NDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEYKYECLTDLYDS 256
Cdd:PRK11192 163 GFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  257 ISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDL 336
Cdd:PRK11192 243 PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
                        330
                 ....*....|.
gi 11513344  337 PANKENYIHRI 347
Cdd:PRK11192 323 PRSADTYLHRI 333
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
23-382 1.75e-61

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 205.04  E-value: 1.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQ------AL*LA 96
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   97 PTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*L 175
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGvDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  176 SSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFyVNVEEEEYKYECLTDLYD 255
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRKRELLSQMIG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  256 SISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYD 335
Cdd:PRK10590 242 KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 11513344  336 LPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQI 382
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
32-221 4.83e-61

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: 195.18  E-value: 4.83e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQIQKVV*A 111
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 112 LAFH*-DIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLL 190
Cdd:cd17943  81 IGKKLeGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL 160
                       170       180       190
                ....*....|....*....|....*....|.
gi 11513344 191 PPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17943 161 PKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
22-388 1.19e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 203.22  E-value: 1.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAAL-QRIDTSVKA------PQAL* 94
Cdd:PRK01297  88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPKerymgePRALI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   95 LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGL--RDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEAD 172
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  173 E*LSSGFKEQIYQIFTLLPPTT--QVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEyKYECL 250
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLL 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  251 TDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSL 330
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 11513344  331 VINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIE-ELPSD 388
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMPPA 465
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
23-221 2.46e-60

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: 194.05  E-value: 2.46e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 11513344 182 QIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
45-210 1.23e-57

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 185.52  E-value: 1.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    45 SAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACI 124
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   125 GGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRfRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*P 204
Cdd:pfam00270  81 GGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLP 159

                  ....*.
gi 11513344   205 NDVLEV 210
Cdd:pfam00270 160 RNLEDL 165
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
22-347 9.50e-52

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 178.24  E-value: 9.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI-------DTSVKAPQAL* 94
Cdd:PRK04837   9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   95 LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE 173
Cdd:PRK04837  89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESgVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  174 *LSSGFKEQIYQIFTLLPPTTQ--VVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQ--FYVNVEEeeyKYEC 249
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  250 LTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVS 329
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
                        330
                 ....*....|....*...
gi 11513344  330 LVINYDLPANKENYIHRI 347
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRI 343
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
23-345 4.00e-51

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 180.15  E-value: 4.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI-------DTSVKAPQAL*L 95
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   96 APTRELALQIQKvv*ALAFH*DIKVHACI--GGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKI-K*FILDEA 171
Cdd:PRK04537  91 APTRELAIQIHK--DAVKFGADLGLRFALvyGGVDYDKQRELLQQgVDVIIATPGRLIDYVKQHKVVSLHAcEICVLDEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  172 DE*LSSGFKEQIYQIFTLLPP--TTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQ-FYVNVEEEeyKYE 248
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQrIYFPADEE--KQT 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  249 CLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQV 328
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
                        330
                 ....*....|....*..
gi 11513344  329 SLVINYDLPANKENYIH 345
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVH 343
PTZ00110 PTZ00110
helicase; Provisional
15-394 5.19e-51

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 179.20  E-value: 5.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   15 NYDKVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVK-----A 89
Cdd:PTZ00110 124 NVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlrygdG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   90 PQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FIL 168
Cdd:PTZ00110 204 PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRgVEILIACPGRLIDFLESNVTNLRRVTYLVL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  169 DEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RN-PVRILVKKDELTL-EGIKQfYVNVEEEEYK 246
Cdd:PTZ00110 284 DEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEEHEK 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  247 YECLTDLYDSISV--TQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGID 324
Cdd:PTZ00110 363 RGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLD 442
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  325 VQQVSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*RELEKFYSTQIEELPSDIATLLN 394
Cdd:PTZ00110 443 VKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSN 512
DEXDc smart00487
DEAD-like helicases superfamily;
36-236 3.02e-49

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 165.36  E-value: 3.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344     36 VFGYGFEEPSAIQQRAI*PIIEG-HDVLAQAQSGTGKTGTFSIAALQRIDtSVKAPQAL*LAPTRELALQIQKVV*ALAF 114
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344    115 H*DIKVHACIGGTSFVEDAEGLR--DAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPP 192
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 11513344    193 TTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKkdELTLEGIKQF 236
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
23-223 9.47e-48

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: 161.36  E-value: 9.47e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALA-FH*DIKVHACIGGTSFVEDAEGLRDA--QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSS-G 178
Cdd:cd17950  84 FQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKcpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 11513344 179 FKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILV 223
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
28-221 1.17e-45

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: 155.93  E-value: 1.17e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  28 LDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTS--VKAPQAL*LAPTRELALQI 105
Cdd:cd17959   8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSPTRELALQT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 106 QKVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIY 184
Cdd:cd17959  88 LKVTKELGKFTDLRTALLVGGDSLEEQFEALaSNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLH 167
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 11513344 185 QIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17959 168 EILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
28-210 7.32e-45

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: 153.89  E-value: 7.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  28 LDENLLRGVFGYGFEEPSAIQQRAI*PIIE-GHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQ-----AL*LAPTREL 101
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 102 ALQIQKVV*AL-AFH*DIKVHACIGGTSFVEDAEGLR--DAQIVVGTPGRVFDNIQRRRFRTD--KIK*FILDEADE*LS 176
Cdd:cd17964  81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrgRPDILVATPGRLIDHLENPGVAKAftDLDYLVLDEADRLLD 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 11513344 177 SGFKEQIYQIFTLLPP----TTQVVLLSAT*PNDVLEV 210
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQI 198
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
28-219 3.24e-44

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: 152.35  E-value: 3.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  28 LDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI------DTSVKAPQAL*LAPTREL 101
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 102 ALQIQKVV*ALAFH--*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFR-TDKIK*FILDEADE*LSS 177
Cdd:cd17961  81 AQQVSKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEkPDIVVSTPARLLSHLESGSLLlLSTLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 11513344 178 GFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPV 219
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
23-374 4.37e-44

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 159.95  E-value: 4.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDT-------SVKAPQAL*L 95
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAMVL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   96 APTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE* 174
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGvELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  175 LSSGFKEQIYQIFTLLPpTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELTLEGIKQFYVNVEEEEYKYEcltdLY 254
Cdd:PLN00206 283 LERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----LF 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  255 DSISVTQ-----AVIFCNTRRKVEEL------TTKLRndkftVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGI 323
Cdd:PLN00206 358 DILKSKQhfkppAVVFVSSRLGADLLanaitvVTGLK-----ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGV 432
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 11513344  324 DVQQVSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGA*REL 374
Cdd:PLN00206 433 DLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
233-348 1.90e-42

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: 144.96  E-value: 1.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 233 IKQFYVNVEEEEYKYECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRI 312
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 11513344 313 LISTDLLARGIDVQQVSLVINYDLPANKENYIHRIG 348
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
32-221 3.79e-42

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: 146.63  E-value: 3.79e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI---DTSVKAPQAL*LAPTRELALQIQKV 108
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 109 V*ALAFH*DIKVHACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRR-FRTDKIK*FILDEADE*LSSGFKEQIYQI 186
Cdd:cd17947  81 LQQLAQFTDITFALAVGGLSLKAQEAALRARpDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEI 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 11513344 187 FTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
23-219 5.91e-42

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: 146.22  E-value: 5.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQ---RRRFRTDKIK*FILDEADE*LSSG 178
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELsKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 179 FKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPV 219
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
20-229 1.13e-40

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: 143.62  E-value: 1.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  20 VYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGH---DVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LA 96
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  97 PTRELALQIQKVV*ALA-FH*DIKVHACIGGTsfvEDAEGLR-DAQIVVGTPGRVFD-NIQRRRFRTDKIK*FILDEADE 173
Cdd:cd18048  96 PTFELALQTGKVVEEMGkFCVGIQVIYAIRGN---RPGKGTDiEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADV 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11513344 174 *LS-SGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILVKKDELT 229
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
23-221 1.87e-40

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: 142.46  E-value: 1.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELA 102
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQRRR-FRTDKIK*FILDEADE*LSSGFK 180
Cdd:cd17954  82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALaKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFE 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 181 EQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
23-217 1.65e-38

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: 137.62  E-value: 1.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI----------DTSVKAPQA 92
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPSA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  93 L*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEA 171
Cdd:cd17967  82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLlRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 11513344 172 DE*LSSGFKEQIYQIFTL--LPPTT--QVVLLSAT*PNDVLEVTTKF*RN 217
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
23-216 5.84e-38

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: 137.41  E-value: 5.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQR-----IDTS----VKAPQAL 93
Cdd:cd18052  45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkegLTASsfseVQEPQAL 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  94 *LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDA-EGLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEAD 172
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIrQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEAD 204
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11513344 173 E*LSSGFKEQIYQIFTLL--PPTT--QVVLLSAT*PNDVLEVTTKF*R 216
Cdd:cd18052 205 RMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
33-202 7.70e-38

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: 135.18  E-value: 7.70e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  33 LRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQ----AL*LAPTRELALQIQKV 108
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 109 V*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQ-IVVGTPGRVFDNIQRRR-FRTDKIK*FILDEADE*LSSGFKEQIYQI 186
Cdd:cd17942  82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVnILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
                       170
                ....*....|....*.
gi 11513344 187 FTLLPPTTQVVLLSAT 202
Cdd:cd17942 162 IKLLPKRRQTMLFSAT 177
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
32-221 1.16e-37

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: 135.53  E-value: 1.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PI-IEGHDVLAQAQSGTGKTGTFSIAALQRID--------TSVKAPQAL*LAPTRELA 102
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAI-PIgLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd17945  80 QQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNgCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 182 QIYQIFTLLPPTT--------------------QVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
32-223 5.74e-37

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: 133.10  E-value: 5.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKA--PQAL*LAPTRELALQIQKVV 109
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 110 *ALAFH*DIKVHACIGGT--SFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIF 187
Cdd:cd17957  81 LKLSKGTGLRIVLLSKSLeaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 11513344 188 TLLP-PTTQVVLLSAT*PNDVLEVTTKF*RNPVRILV 223
Cdd:cd17957 161 AACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
40-221 4.52e-35

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: 128.65  E-value: 4.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  40 GFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAAL-----QRIDTSVKAPQAL*LAPTRELALQIQKVV*ALAF 114
Cdd:cd17953  31 GYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPIGLIMAPTRELALQIYVECKKFSK 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 115 H*DIKVHACIGGTSFVED-AEGLRDAQIVVGTPGRVFDNI---QRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLL 190
Cdd:cd17953 111 ALGLRVVCVYGGSGISEQiAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNI 190
                       170       180       190
                ....*....|....*....|....*....|.
gi 11513344 191 PPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17953 191 RPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
40-221 5.81e-35

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: 127.66  E-value: 5.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  40 GFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRELALQIQKVV*ALAFH*-DI 118
Cdd:cd17962   9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 119 KVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPPTTQVV 197
Cdd:cd17962  89 KTALLVGGLPLPPQLYRLQQgVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTI 168
                       170       180
                ....*....|....*....|....
gi 11513344 198 LLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17962 169 LVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
33-223 6.22e-35

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: 127.41  E-value: 6.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  33 LRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRID----TSVKAPQAL*LAPTRELALQIQKV 108
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 109 V*ALAFH*DIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRR-RFRTDKIK*FILDEADE*LSSGFKEQIYQIF 187
Cdd:cd17941  82 LRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 11513344 188 TLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRILV 223
Cdd:cd17941 162 ENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
32-221 4.38e-34

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: 125.38  E-value: 4.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI---DTSVKAPQ--AL*LAPTRELALQIQ 106
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 107 KVV*ALAFH*DIKVHA--CIGGTSFVEDAEGLRD--AQIVVGTPGRVFDNIQRrrfRTDKIK*-----FILDEADE*LSS 177
Cdd:cd17960  81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFKRngPNILVGTPGRLEELLSR---KADKVKVkslevLVLDEADRLLDL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 11513344 178 GFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17960 158 GFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
23-218 7.41e-32

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: 119.82  E-value: 7.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEG--HDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQAL*LAPTRE 100
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 101 LALQIQKVV*ALA-FH*DIKVHACIGGTSfVEDAEGLRDaQIVVGTPGRVFD-NIQRRRFRTDKIK*FILDEADE*LSS- 177
Cdd:cd18047  83 LALQTGKVIEQMGkFYPELKLAYAVRGNK-LERGQKISE-QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIATq 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 11513344 178 GFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNP 218
Cdd:cd18047 161 GHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
32-221 2.88e-31

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: 117.90  E-value: 2.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAAL-----QRIDTSVKAPQAL*LAPTRELALQIQ 106
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 107 KVV*ALAFH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQ 185
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 11513344 186 IFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
32-221 5.00e-31

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: 117.09  E-value: 5.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDT-----SVKAPQAL*LAPTRELALQIQ 106
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAqppleRGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 107 KVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQ 185
Cdd:cd17966  81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLrRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 11513344 186 IFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
40-221 1.01e-30

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: 116.92  E-value: 1.01e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  40 GFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI---DTSVK---APQAL*LAPTRELALQIQKVV*AL- 112
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVDrsdGTLALVLVPTRELALQIYEVLEKLl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 113 -AFH*dIKVHACIGGTSfvEDAEGLR---DAQIVVGTPGRVFDNIQR-RRFRTDKIK*FILDEADE*LSSGFKEQIYQIF 187
Cdd:cd17949  90 kPFHW-IVPGYLIGGEK--RKSEKARlrkGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 11513344 188 TLL-------------PPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
40-221 2.43e-30

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: 115.25  E-value: 2.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  40 GFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV------KAPQAL*LAPTRELALQIQKVV*ALA 113
Cdd:cd17958   9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreqrNGPGVLVLTPTRELALQIEAECSKYS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 114 fH*DIKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLLPP 192
Cdd:cd17958  89 -YKGLKSVCVYGGGNRNEQIEDLSKgVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRP 167
                       170       180
                ....*....|....*....|....*....
gi 11513344 193 TTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd17958 168 DRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
23-219 2.54e-30

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 115.50  E-value: 2.54e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  23 FDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIdtsvkapQAL*LAPTRELA 102
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 103 LQIQKVV*ALAFH*D---IKVHACIGGTSFVEDAEGLRD-AQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSG 178
Cdd:cd17938  74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESgVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 11513344 179 FKEQIYQIFTLLPPTT------QVVLLSAT*PN-DVLEVTTKF*RNPV 219
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATLHSfEVKKLADKIMHFPT 201
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
58-202 6.07e-30

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: 112.50  E-value: 6.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  58 GHDVLAQAQSGTGKTGTFSIAALQRIDTsvKAPQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAE-GL 136
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKnKL 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11513344 137 RDAQIVVGTPGRVFDNIQR-RRFRTDKIK*FILDEADE*LSSGFKEQI--YQIFTLLPPTTQVVLLSAT 202
Cdd:cd00046  78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
47-216 2.99e-29

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: 112.63  E-value: 2.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  47 IQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV------KAPQAL*LAPTRELALQIQKVV*ALAfh*DIKV 120
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDIT--RKLSV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 121 HACIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIFTLL-----PPTT 194
Cdd:cd17944  94 ACFYGGTPYQQQIFAIRNGiDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDNP 173
                       170       180
                ....*....|....*....|..
gi 11513344 195 QVVLLSAT*PNDVLEVTTKF*R 216
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
32-181 4.11e-29

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: 113.10  E-value: 4.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*P-IIEGHDVLAQAQSGTGKTGTFSIAALQRI---------DTSVKAPQAL*LAPTREL 101
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 102 ALQIQKVV*ALAFH*DIKVHACIGGTSfVEDAEGL--RDAQIVVGTPGRVFDNIQRR-----RFRtdKIK*FILDEADE* 174
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKIASIVGGLA-VQKQERLlkKRPEIVVATPGRLWELIQEGnehlaNLK--SLRFLVLDEADRM 157

                ....*...
gi 11513344 175 LSSG-FKE 181
Cdd:cd17946 158 LEKGhFAE 165
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
22-217 6.40e-28

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: 110.13  E-value: 6.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI--DTSVKA---------- 89
Cdd:cd18051  22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeQGPGESlpsesgyygr 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  90 ----PQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSFVEDAEGL-RDAQIVVGTPGRVFDNIQRRRFRTDKIK 164
Cdd:cd18051 102 rkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLeRGCHLLVATPGRLVDMLERGKIGLDYCK 181
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11513344 165 *FILDEADE*LSSGFKEQIYQIFT--LLPPT--TQVVLLSAT*PNDVLEVTTKF*RN 217
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
15-221 7.41e-27

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: 107.02  E-value: 7.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  15 NYDKVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV-----KA 89
Cdd:cd18049  18 NCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  90 PQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSF---VEDAEglRDAQIVVGTPGRVFDNIQRRRFRTDKIK*F 166
Cdd:cd18049  98 PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKgpqIRDLE--RGVEICIATPGRLIDFLEAGKTNLRRCTYL 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 11513344 167 ILDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd18049 176 VLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
246-348 2.10e-26

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: 101.90  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   246 KYECLTDLYDSISVTQAVIFCNTRRKVEElTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDV 325
Cdd:pfam00271   2 KLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100
                  ....*....|....*....|...
gi 11513344   326 QQVSLVINYDLPANKENYIHRIG 348
Cdd:pfam00271  81 PDVDLVINYDLPWNPASYIQRIG 103
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
18-221 3.48e-26

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: 106.25  E-value: 3.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  18 KVVYKFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSV-----KAPQA 92
Cdd:cd18050  59 KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergDGPIC 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  93 L*LAPTRELALQIQKVV*ALAFH*DIKVHACIGGTSF---VEDAEglRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILD 169
Cdd:cd18050 139 LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKgpqIRDLE--RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLD 216
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 11513344 170 EADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PNDVLEVTTKF*RNPVRI 221
Cdd:cd18050 217 EADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
32-204 3.35e-24

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: 98.95  E-value: 3.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  32 LLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAA-LQRIDTSVKA-------PQAL*LAPTRELAL 103
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLpfikgegPYGLIVCPSRELAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 104 QIQKVV*ALAFH*DIKVHA------CIGGTSFVEDAEGLRDA-QIVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LS 176
Cdd:cd17951  81 QTHEVIEYYCKALQEGGYPqlrcllCIGGMSVKEQLEVIRKGvHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                       170       180
                ....*....|....*....|....*...
gi 11513344 177 SGFKEQIYQIFTLLPPTTQVVLLSAT*P 204
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMP 188
HELICc smart00490
helicase superfamily c-terminal domain;
273-347 4.13e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 4.13e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11513344    273 EELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKENYIHRI 347
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
38-213 5.14e-22

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: 93.59  E-value: 5.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  38 GYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI-------DTSVKAPQAL*LAPTRELALQIQKVV* 110
Cdd:cd17948   7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQIGSVAQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 111 ALAFH*DIKVHaCIGGTSFVEDAEGLRDAQ--IVVGTPGRVFDNIQRRRFRTDKIK*FILDEADE*LSSGFKEQIYQIF- 187
Cdd:cd17948  87 SLTEGLGLKVK-VITGGRTKRQIRNPHFEEvdILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLr 165
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 11513344 188 ------------TLLPPTTQVVLLSAT*PNDVLEVTTK 213
Cdd:cd17948 166 rfplasrrsentDGLDPGTQLVLVSATMPSGVGEVLSK 203
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
44-181 2.08e-17

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


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 80.75  E-value: 2.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  44 PSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRI-DTSVKAPQAL*LAPTRELALQIQKVV*ALAFH*DIKVHA 122
Cdd:cd17956  22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11513344 123 CIGGTSFVEDAEGLRD---------AQIVVGTPGRVFDNIQR-RRFRTDKIK*FILDEADE*LSSGFKE 181
Cdd:cd17956 102 LSGQKSFKKEQKLLLVdtsgrylsrVDILVATPGRLVDHLNStPGFTLKHLRFLVIDEADRLLNQSFQD 170
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
40-323 3.02e-14

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 74.16  E-value: 3.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  40 GFEE--PSaiQQRAI*P-IIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKApqaL*LAPTRELALQIQKVV*ALAFH* 116
Cdd:COG1204  19 GIEElyPP--QAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKA---LYIVPLRALASEKYREFKRDFEEL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 117 DIKVHACIGGtsFVEDAEGLRDAQIVVGTPGRvFDNIQRRRFRT-DKIK*FILDEA----DE*lSSGFK-EQIYQIFTLL 190
Cdd:COG1204  94 GIKVGVSTGD--YDSDDEWLGRYDILVATPEK-LDSLLRNGPSWlRDVDLVVVDEAhlidDE--SRGPTlEVLLARLRRL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 191 PPTTQVVLLSAT*PN--DVLE------VTTKF*RNPVRILVKKDEltlegikQFYVNVEEEEYKYECLTDLYDSISV-TQ 261
Cdd:COG1204 169 NPEAQIVALSATIGNaeEIAEwldaelVKSDWRPVPLNEGVLYDG-------VLRFDDGSRRSKDPTLALALDLLEEgGQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 262 AVIFCNTRRKVEELTTKLRN--------------DKFTVSAI-----------------------YSDLPQQERDTI*KE 304
Cdd:COG1204 242 VLVFVSSRRDAESLAKKLADelkrrltpeereelEELAEELLevseethtnekladclekgvafhHAGLPSELRRLVEDA 321
                       330
                ....*....|....*....
gi 11513344 305 FRSGSSRILISTDLLARGI 323
Cdd:COG1204 322 FREGLIKVLVATPTLAAGV 340
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
48-332 4.72e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.52  E-value: 4.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  48 QQRAI-----*PIIEGHDVLAQAQSGTGKTgTFSIAALQRIDTSVKApqaL*LAPTRELALQIQKvv*ALAFH*DIKVHa 122
Cdd:COG1061  85 QQEALeallaALERGGGRGLVVAPTGTGKT-VLALALAAELLRGKRV---LVLVPRRELLEQWAE--ELRRFLGDPLAG- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 123 ciGGTSFvedaeglRDAQIVVGTPGRVFDNIQRRRFRtDKIK*FILDEADE*LSSGFKeqiyQIFTLLPPTTqVVLLSAT 202
Cdd:COG1061 158 --GGKKD-------SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYR----RILEAFPAAY-RLGLTAT 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 203 *P--NDVLEVTTKF*RN-----------------PVRILVKKDELTLEgiKQFYVNVEE---------EEYKYECLTDLY 254
Cdd:COG1061 223 -PfrSDGREILLFLFDGivyeyslkeaiedgylaPPEYYGIRVDLTDE--RAEYDALSErlrealaadAERKDKILRELL 299
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11513344 255 DSI-SVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVI 332
Cdd:COG1061 300 REHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
47-205 2.54e-10

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 59.20  E-value: 2.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  47 IQQRAI*PII-EGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKapQAL*LAPTRELALQIQKVV*ALAFH*DIKVHACIG 125
Cdd:cd17921   5 IQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSGG--KAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 126 GTSfvEDAEGLRDAQIVVGTPGRvFDNIQRRR--FRTDKIK*FILDEAdE*LSSGFKEQIYQ-IFTLLP---PTTQVVLL 199
Cdd:cd17921  83 DPS--VNKLLLAEADILVATPEK-LDLLLRNGgeRLIQDVRLVVVDEA-HLIGDGERGVVLElLLSRLLrinKNARFVGL 158

                ....*.
gi 11513344 200 SAT*PN 205
Cdd:cd17921 159 SATLPN 164
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
28-343 1.07e-09

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 60.11  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   28 LDENLLRGVFGYGFEEPSaiQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRidtsvkapQAL*LAPTRELALQIQK 107
Cdd:PRK11057  12 LAKQVLQETFGYQQFRPG--QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL--------DGLTLVVSPLISLMKDQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  108 VV*ALAFH*DIkvhACIGGTSFVEDA----EGLRDAQI--VVGTPGRVFDNIQRRRFRTDKIK*FILDEAD--------- 172
Cdd:PRK11057  82 VDQLLANGVAA---ACLNSTQTREQQlevmAGCRTGQIklLYIAPERLMMDNFLEHLAHWNPALLAVDEAHcisqwghdf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  173 --E*LSSGfkeQIYQIFTLLPpttqVVLLSAT*PNdvlevTTKf*RNPVRILVKKDELTLegIKQF------YVNVEeee 244
Cdd:PRK11057 159 rpEYAALG---QLRQRFPTLP----FMALTATADD-----TTR--QDIVRLLGLNDPLIQ--ISSFdrpnirYTLVE--- 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  245 yKYECLTDLYDSISVTQ---AVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLAR 321
Cdd:PRK11057 220 -KFKPLDQLMRYVQEQRgksGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
                        330       340
                 ....*....|....*....|..
gi 11513344  322 GIDVQQVSLVINYDLPANKENY 343
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESY 320
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
263-343 3.52e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 58.23  E-value: 3.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 263 VIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKEN 342
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313

                .
gi 11513344 343 Y 343
Cdd:COG0514 314 Y 314
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
260-344 2.86e-08

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: 52.21  E-value: 2.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 260 TQAVIFCNTR----------RKVEELTTKLRNDKFT-----VSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGID 324
Cdd:cd18802  26 FRGIIFVERRatavvlsrllKEHPSTLAFIRCGFLIgrgnsSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGID 105
                        90       100
                ....*....|....*....|
gi 11513344 325 VQQVSLVINYDLPANKENYI 344
Cdd:cd18802 106 VPACNLVIRFDLPKTLRSYI 125
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
262-332 5.85e-08

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: 50.64  E-value: 5.85e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11513344 262 AVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDT---I*KEFRSGSSRILISTDLLARGIDVQQVSLVI 332
Cdd:cd18799   9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDealILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
264-337 1.72e-07

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 50.34  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 264 IFCNTRRKVEELTTKLRN---DKFTVSAIY---SDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLP 337
Cdd:cd18796  43 VFTNTRSQAERLAQRLRElcpDRVPPDFIAlhhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
262-339 3.06e-07

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 49.01  E-value: 3.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 262 AVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSS--RILISTDLLARGIDVQQVSLVINYDLPAN 339
Cdd:cd18793  30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
65-221 4.09e-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: 50.84  E-value: 4.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  65 AQSGTGKTGTF---SIAALQRIDTSVK--------------APQAL*LAPTRELALQIQKVV*ALA--FH*DIKVHACIG 125
Cdd:cd17965  68 AETGSGKTLAYlapLLDYLKRQEQEPFeeaeeeyesakdtgRPRSVILVPTHELVEQVYSVLKKLShtVKLGIKTFSSGF 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 126 GTSFVEDAEGLRDA-QIVVGTPGRVfDNIQRRRFRT-DKIK*FILDEADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT* 203
Cdd:cd17965 148 GPSYQRLQLAFKGRiDILVTTPGKL-ASLAKSRPKIlSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
                       170
                ....*....|....*...
gi 11513344 204 PNDVLEVTTKF*RNPVRI 221
Cdd:cd17965 227 PKEFDKTLRKLFPDVVRI 244
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
262-339 8.26e-07

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 50.99  E-value: 8.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 262 AVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSS--RILISTDLLARGIDVQQVSLVINYDLPAN 339
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
262-347 2.77e-06

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 46.43  E-value: 2.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 262 AVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKE 341
Cdd:cd18794  33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112

                ....*.
gi 11513344 342 NYIHRI 347
Cdd:cd18794 113 SYYQES 118
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
268-343 6.83e-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: 46.08  E-value: 6.83e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11513344 268 TRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDlpANKENY 343
Cdd:cd18790  36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKEGF 109
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
261-336 7.01e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 48.19  E-value: 7.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 261 QAVIFCNTRRKVEELTTKLRNDKFTV------SAIYSD--LPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVI 332
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434

                ....
gi 11513344 333 NYDL 336
Cdd:COG1111 435 FYEP 438
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
25-339 1.01e-05

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: 47.52  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  25 D*ELDENLLRGVFGYGFEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKApQAL*LAPTRELAL- 103
Cdd:COG1205  38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-TALYLYPTKALARd 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 104 QIQKVV*-ALAFH*DIKVHACIGGTSFVEDAEGLRDAQIVVGTPgrvfDNI------QRRRFRT--DKIK*FILDEAdE* 174
Cdd:COG1205 117 QLRRLRElAEALGLGVRVATYDGDTPPEERRWIREHPDIVLTNP----DMLhygllpHHTRWARffRNLRYVVIDEA-HT 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 175 LSSGFKEQIYQIFTLL----------PpttQVVLLSAT*PN-----------DVLEVTTK----------F*RNPVRILV 223
Cdd:COG1205 192 YRGVFGSHVANVLRRLrricrhygsdP---QFILASATIGNpaehaerltgrPVTVVDEDgsprgertfvLWNPPLVDDG 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 224 KKDELTLEGIKQFYVNVEEEeykyecltdlydsisvTQAVIFCNTRRKVEELTTKLRN------DKFTVSAIYSDLPQQE 297
Cdd:COG1205 269 IRRSALAEAARLLADLVREG----------------LRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEE 332
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 11513344 298 RDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYDLP------------AN 339
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPgtrasfwqqagrAG 386
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
68-316 1.56e-05

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: 47.00  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  68 GTGKTgtfsIAALqRIdtsvkapqAL*LA------------PTRELALQIQKVV*A------LAFH*DIKVHACIGGTSF 129
Cdd:COG1203 157 GGGKT----EAAL-LF--------ALRLAakhggrriiyalPFTSIINQTYDRLRDlfgedvLLHHSLADLDLLEEEEEY 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 130 VEDAEGLR------DAQIVVGTP----GRVFDNiQRRRFRtdKI-----K*FILDEA---DE*LSSGFKEQIYQIFTLlp 191
Cdd:COG1203 224 ESEARWLKllkelwDAPVVVTTIdqlfESLFSN-RKGQER--RLhnlanSVIILDEVqayPPYMLALLLRLLEWLKNL-- 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 192 pTTQVVLLSAT*PNDVLEvttkF*RNPVRILVKKDELTLEGIKQFY---VNVEEEEYKYEcltDLYDSI-----SVTQAV 263
Cdd:COG1203 299 -GGSVILMTATLPPLLRE----ELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDE---ELAELIlealhKGKSVL 370
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 11513344 264 IFCNTRRKVEELTTKLRNDKFTVSAIY--SDLPQQER----DTI*KEFRSGSSRILIST 316
Cdd:COG1203 371 VIVNTVKDAQELYEALKEKLPDEEVYLlhSRFCPADRseieKEIKERLERGKPCILVST 429
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
261-323 1.98e-05

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 44.47  E-value: 1.98e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11513344 261 QAVIFCNTRRKVEELTTKLRNdkftVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGI 323
Cdd:cd18795  45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
273-335 3.54e-05

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 43.87  E-value: 3.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11513344 273 EELTTKLRNdKFTVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVINYD 335
Cdd:cd18811  52 EYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
260-335 5.13e-05

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 42.73  E-value: 5.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344 260 TQAVIFCNTRRKVEELTTKLRNDKFTVSAI----------YSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVS 329
Cdd:cd18801  31 TRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigqasgksSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110

                ....*.
gi 11513344 330 LVINYD 335
Cdd:cd18801 111 LIICYD 116
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
43-145 8.29e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 42.79  E-value: 8.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  43 EPSAIQQRAI*PII------EGHDVLAQAQSGTGKTGTFSIAALqridTSVKAP-QAL*LAPTRELALQIQKVv*ALAFH 115
Cdd:cd17918  15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAAL----LAYKNGkQVAILVPTEILAHQHYEE--ARKFL 88
                        90       100       110
                ....*....|....*....|....*....|
gi 11513344 116 *DIKVHACIGGTSfvedAEGLRDAQIVVGT 145
Cdd:cd17918  89 PFINVELVTGGTK----AQILSGISLLVGT 114
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
55-205 1.06e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 42.71  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  55 IIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKApqaL*LAPTRelALQIQKVV*ALAFH-*DIKVHACIGgtSFVEDA 133
Cdd:cd18028  14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKA---LYLVPLR--ALASEKYEEFKKLEeIGLKVGISTG--DYDEDD 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11513344 134 EGLRDAQIVVGTPGRvFDNIQRrrFRTDKIK*---FILDE---ADE*LSSGFKEQIYQIFTLLPPTTQVVLLSAT*PN 205
Cdd:cd18028  87 EWLGDYDIIVATYEK-FDSLLR--HSPSWLRDvgvVVVDEihlISDEERGPTLESIVARLRRLNPNTQIIGLSATIGN 161
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
30-80 5.06e-04

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: 40.98  E-value: 5.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 11513344  30 ENLLRGVFGYgfEEPSAIQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAAL 80
Cdd:cd17920   1 EQILKEVFGY--DEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL 49
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
47-171 1.20e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 39.42  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  47 IQQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTsvKAPQAL*LAPTRELALQIQKVV*ALaFH*DIKVHACIGG 126
Cdd:cd18035   5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTK--KGGKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGE 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 11513344 127 TSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEA 171
Cdd:cd18035  82 VKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
PRK00254 PRK00254
ski2-like helicase; Provisional
22-332 4.85e-03

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 39.03  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344   22 KFDD*ELDENLLRGVFGYGFEEPSAIQQRAI*P-IIEGHDVLAQAQSGTGKTGTFSIAALQRIDTsvKAPQAL*LAPTRE 100
Cdd:PRK00254   2 KVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR--EGGKAVYLVPLKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  101 LALQIQKVV*ALAfH*DIKVHACIGGTSFVEDAEGLRDaqIVVGTPGRvFDNIQRRRFRTDK-IK*FILDEADE*LSSGF 179
Cdd:PRK00254  80 LAEEKYREFKDWE-KLGLRVAMTTGDYDSTDEWLGKYD--IIIATAEK-FDSLLRHGSSWIKdVKLVVADEIHLIGSYDR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  180 KEQIYQIFTLLPPTTQVVLLSAT*--PNDVLE-VTTKF*RN---PVRI---LVKKDELTLE--GIKQFYVNVEEEeykye 248
Cdd:PRK00254 156 GATLEMILTHMLGRAQILGLSATVgnAEELAEwLNAELVVSdwrPVKLrkgVFYQGFLFWEdgKIERFPNSWESL----- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  249 cltdLYDSISV-TQAVIFCNTRRKVE----ELTTKLR-----------------------NDKFT------VSAIYSDLP 294
Cdd:PRK00254 231 ----VYDAVKKgKGALVFVNTRRSAEkealELAKKIKrfltkpelralkeladsleenptNEKLKkalrggVAFHHAGLG 306
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 11513344  295 QQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVI 332
Cdd:PRK00254 307 RTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVII 344
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
68-171 6.47e-03

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 37.63  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  68 GTGKTgtfSIAAL-------QRIDTSVKAPQAL*LAPTRELALQiQkvV*ALAFH*DIKVHACIGG------TSFVEDAE 134
Cdd:cd18034  26 GSGKT---LIAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEmgvdkwTKERWKEE 99
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 11513344 135 gLRDAQIVVGTPGRVFDNIQRRRFRTDKIK*FILDEA 171
Cdd:cd18034 100 -LEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
260-332 7.02e-03

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: 36.84  E-value: 7.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11513344 260 TQAVIFCNTRRKVEELTTKLRndkftVSAIYSDLPQQERDTI*KEFRSGSSRILISTDLLARGIDVQQVSLVI 332
Cdd:cd18789  50 DKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAI 117
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
48-171 7.85e-03

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 37.18  E-value: 7.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11513344  48 QQRAI*PIIEGHDVLAQAQSGTGKTGTFSIAALQRIdTSVKAPQAL*LAPTRELALQIQKVV*ALA--FH*DIKVHACIG 125
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRELLeqLGLGIRVATYDG 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 11513344 126 GTSfVEDAEGLRD--AQIVVGTPGRV------FDNIQRRRFRtdKIK*FILDEA 171
Cdd:cd17923  84 DTP-REERRAIIRnpPRILLTNPDMLhyallpHHDRWARFLR--NLRYVVLDEA 134
 
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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