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Conserved domains on  [gi|119598578|gb|EAW78172|]
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eukaryotic translation initiation factor 4A, isoform 2, isoform CRA_a [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
21-407 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: 609.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  21 DGVIESNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFK 100
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 101 ETQALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMF 180
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKA-GVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 181 VLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWK 260
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 261 LDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 340
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 341 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI 407
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
21-407 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 609.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  21 DGVIESNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFK 100
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 101 ETQALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMF 180
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKA-GVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 181 VLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWK 260
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 261 LDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 340
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 341 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI 407
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
35-236 1.01e-150

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: 424.55  E-value: 1.01e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFK 194
Cdd:cd18046   81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119598578 195 DQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRIL 236
Cdd:cd18046  160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
34-401 1.47e-144

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 417.24  E-value: 1.47e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEF-KETQALVLAPTRE 112
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 113 LAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRG 192
Cdd:COG0513   83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 193 FKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEwKLDTLCDLYETLT 272
Cdd:COG0513  162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 273 ITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPT 352
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 119598578 353 NRENYIHRIgrggrfgrkgVAINFVTEEDKRILRDIETFYNTTVEEMPM 401
Cdd:COG0513  321 DPEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEXDc smart00487
DEAD-like helicases superfamily;
48-250 4.57e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 185.77  E-value: 4.57e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578    48 IYAYGFEKPSAIQQRAIIPCIKGY-DVIAQAQSGTGKTATFAISILQQLeIEFKETQALVLAPTRELAQQIQKVILALGD 126
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578   127 YMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQKLNT 206
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119598578   207 SIQVVLLSATMPTDVLEVTKKFMRDPIRILVkkEELTLEGIKQF 250
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
57-224 7.15e-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: 183.98  E-value: 7.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578   57 SAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILALGDYMGATCHACI 136
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  137 GGTNVRNEMQKLQaeAPHIVVGTPGRVFDML-NRRYLSPkwIKMFVLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSA 215
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLqERKLLKN--LKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 119598578  216 TMPTDVLEV 224
Cdd:pfam00270 157 TLPRNLEDL 165
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
21-407 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 609.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  21 DGVIESNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFK 100
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 101 ETQALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMF 180
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKA-GVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 181 VLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWK 260
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 261 LDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 340
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 341 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI 407
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
35-236 1.01e-150

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: 424.55  E-value: 1.01e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFK 194
Cdd:cd18046   81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119598578 195 DQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRIL 236
Cdd:cd18046  160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
34-401 1.47e-144

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 417.24  E-value: 1.47e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEF-KETQALVLAPTRE 112
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 113 LAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRG 192
Cdd:COG0513   83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 193 FKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEwKLDTLCDLYETLT 272
Cdd:COG0513  162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 273 ITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPT 352
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 119598578 353 NRENYIHRIgrggrfgrkgVAINFVTEEDKRILRDIETFYNTTVEEMPM 401
Cdd:COG0513  321 DPEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
37-236 2.00e-135

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: 385.91  E-value: 2.00e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  37 DMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQ 116
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 117 IQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQ 196
Cdd:cd17939   81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQ-YGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119598578 197 IYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRIL 236
Cdd:cd17939  160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
35-236 7.35e-106

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: 310.94  E-value: 7.35e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFK 194
Cdd:cd18045   81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLD-YGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119598578 195 DQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRIL 236
Cdd:cd18045  160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
35-397 9.71e-87

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 270.90  E-value: 9.71e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGAT-----ChaciGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEML 189
Cdd:PRK11776  86 DQVAKEIRRLARFIPNIkvltlC----GGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 190 SRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEElTLEGIKQFYINVEREEwKLDTLCDLYE 269
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDE-RLPALQRLLL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 270 TLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 349
Cdd:PRK11776 239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 119598578 350 LPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVE 397
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
44-235 2.29e-83

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: 253.13  E-value: 2.29e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL----EIEFKETQALVLAPTRELAQQIQK 119
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpepKKKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 120 VILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYE 199
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119598578 200 IFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
30-407 2.24e-75

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 246.30  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  30 EIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAP 109
Cdd:PRK11634   3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 110 TRELAQQIQKVILALGDYM-GATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEM 188
Cdd:PRK11634  83 TRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 189 LSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEwKLDTLCDLY 268
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 269 ETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 348
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119598578 349 DLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVEEMPMNVADLI 407
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
40-235 1.19e-65

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: 207.81  E-value: 1.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  40 LKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYD--VIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQI 117
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 118 QKVILALGDYMGATCHACIGGTNVRNEmQKLQAeapHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEML-SRGFKDQ 196
Cdd:cd17963   81 GEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQ 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119598578 197 IYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17963  157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
35-400 1.28e-64

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 214.01  E-value: 1.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL-------EIEFKETQALVL 107
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 108 APTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADE 187
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 188 MLSRGFKDQIYEIFQKL--NTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQ-FYINVEREEWKLdtL 264
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL--L 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 265 CDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSL 344
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 345 VINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETFYNTTVE-EMP 400
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
34-389 1.45e-63

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 210.18  E-value: 1.45e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLeIEF---KETQA--LVLA 108
Cdd:PRK11192   2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL-LDFprrKSGPPriLILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 109 PTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLqAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEM 188
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVF-SENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 189 LSRGFKDQIYEIFQKLNTSIQVVLLSATMPTD-VLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWKLDTLCDL 267
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 268 YETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 347
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 119598578 348 YDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIE 389
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
35-237 1.92e-61

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: 197.57  E-value: 1.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACI-GGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEML-SRG 192
Cdd:cd17950   84 FQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 119598578 193 FKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILV 237
Cdd:cd17950  164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
35-235 1.93e-61

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: 197.14  E-value: 1.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFK 194
Cdd:cd17940   81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLY-QTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 119598578 195 DQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17940  160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
34-389 2.10e-61

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 205.04  E-value: 2.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL---EIEFK---ETQALVL 107
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrQPHAKgrrPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 108 APTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADE 187
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRG-GVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 188 MLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEwKLDTLCDL 267
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 268 YETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 347
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 119598578 348 YDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIE 389
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIE 361
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
44-235 1.95e-59

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: 191.71  E-value: 1.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILA 123
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 124 LGDYM-GATCHACIGGTNVRNEMQKLQaeAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQ 202
Cdd:cd17943   81 IGKKLeGLKCEVFIGGTPVKEDKKKLK--GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 119598578 203 KLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17943  159 SLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
35-388 2.07e-57

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 196.16  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQ-------QLEIEFKETQALVL 107
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLAMVL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 108 APTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADE 187
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQ-QGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 188 MLSRGFKDQIYEIFQKLNTSiQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQFYINVEREEWKLDtlcdL 267
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----L 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 268 YETLTITQ-----AVIFLNTRRKVDWLTEKMH-ARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQ 341
Cdd:PLN00206 357 FDILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 119598578 342 VSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDI 388
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
DEXDc smart00487
DEAD-like helicases superfamily;
48-250 4.57e-57

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 185.77  E-value: 4.57e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578    48 IYAYGFEKPSAIQQRAIIPCIKGY-DVIAQAQSGTGKTATFAISILQQLeIEFKETQALVLAPTRELAQQIQKVILALGD 126
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578   127 YMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQKLNT 206
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119598578   207 SIQVVLLSATMPTDVLEVTKKFMRDPIRILVkkEELTLEGIKQF 250
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
57-224 7.15e-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: 183.98  E-value: 7.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578   57 SAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILALGDYMGATCHACI 136
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  137 GGTNVRNEMQKLQaeAPHIVVGTPGRVFDML-NRRYLSPkwIKMFVLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSA 215
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLqERKLLKN--LKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 119598578  216 TMPTDVLEV 224
Cdd:pfam00270 157 TLPRNLEDL 165
PTZ00110 PTZ00110
helicase; Provisional
32-388 2.29e-54

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 188.44  E-value: 2.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  32 VDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATF----AISILQQLEIEFKETQ-ALV 106
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFllpaIVHINAQPLLRYGDGPiVLV 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 107 LAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEAD 186
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALR-RGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 187 EMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRD-PIRILVKKEELTL-EGIKQfYINVEREEWKLDTL 264
Cdd:PTZ00110 288 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEEHEKRGKL 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 265 CDLYETLTI--TQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQV 342
Cdd:PTZ00110 367 KMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 119598578 343 SLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDI 388
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
34-391 2.84e-54

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 189.01  E-value: 2.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL-------EIEFKETQALV 106
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 107 LAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNR-RYLSPKWIKMFVLDEA 185
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQ-QGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 186 DEMLSRGFKDQIYEIFQKL--NTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQfYINVEREEWKLDT 263
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ-RIYFPADEEKQTL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 264 LCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVS 343
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 119598578 344 LVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETF 391
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAY 375
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
35-232 1.30e-50

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: 169.33  E-value: 1.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEaPHIVVGTPGRVFDMLNRRYLSPKW---IKMFVLDEADEMLSR 191
Cdd:cd17955   81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKR-PHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 119598578 192 GFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDP 232
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
35-235 1.68e-50

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: 169.03  E-value: 1.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELA 114
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGATCHACIGGTNVRNEMQKLqAEAPHIVVGTPGRVFDML-NRRYLSPKWIKMFVLDEADEMLSRGF 193
Cdd:cd17954   82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIAL-AKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDF 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119598578 194 KDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17954  161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
44-235 6.63e-50

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 167.05  E-value: 6.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKE---TQALVLAPTRELAQQIQKV 120
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKkaaTRVLVLVPTRELAMQCFSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 121 ILALGDYMGATCHACIGGTNVRNEMQKLQAeAPHIVVGTPGRVFDML-NRRYLSPKWIKMFVLDEADEMLSRGFKDQIYE 199
Cdd:cd17947   81 LQQLAQFTDITFALAVGGLSLKAQEAALRA-RPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119598578 200 IFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17947  160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
35-391 3.02e-49

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 172.08  E-value: 3.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAIS----ILQQLEIEFKET---QALVL 107
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVnqpRALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 108 APTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADE 187
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLE-SGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 188 MLSRGFKDQIYEIF-------QKLNtsiqvVLLSATMPTDVLEVTKKFMRDPIRILVKKEELTLEGIKQ--FYINVERee 258
Cdd:PRK04837 169 MFDLGFIKDIRWLFrrmppanQRLN-----MLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE-- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 259 wKLDTLCDLYETLTITQAVIFLNTRRKV----DWLTEKMHardfTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLA 334
Cdd:PRK04837 242 -KMRLLQTLIEEEWPDRAIIFANTKHRCeeiwGHLAADGH----RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 335 RGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINFVTEEDKRILRDIETF 391
Cdd:PRK04837 317 RGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETY 373
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
40-230 7.15e-49

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: 165.06  E-value: 7.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  40 LKESLLRGIYAYGFEKPSAIQQRAIIPCI-KGYDVIAQAQSGTGKTATFAISILQQLeIEFKE------TQALVLAPTRE 112
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSL-LNTKPagrrsgVSALIISPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 113 LAQQIQKVILALGDYM-GATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNrrylSPKWIKMF------VLDEA 185
Cdd:cd17964   80 LALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLE----NPGVAKAFtdldylVLDEA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119598578 186 DEMLSRGFKDQIYEIFQKLNTS----IQVVLLSATMPTDVLEVTKKFMR 230
Cdd:cd17964  156 DRLLDMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
40-233 5.44e-48

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: 162.37  E-value: 5.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  40 LKESLLRGIYAYGFEKPSAIQQRAIiPCI-KGYDVIAQAQSGTGKTATFAISILQQL------EIEFKETQALVLAPTRE 112
Cdd:cd17961    1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLAlEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 113 LAQQIQKVILALGDYmgatCHACIGGTNVRNEM-----QKLQAEAPHIVVGTPGRVFDMLNRRYLSPK-WIKMFVLDEAD 186
Cdd:cd17961   80 LAQQVSKVLEQLTAY----CRKDVRVVNLSASSsdsvqRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEAD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119598578 187 EMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPI 233
Cdd:cd17961  156 LVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
34-235 3.15e-47

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: 160.55  E-value: 3.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKET--QALVLAPTR 111
Cdd:cd17959    2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 112 ELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLqAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSR 191
Cdd:cd17959   82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEAL-ASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119598578 192 GFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17959  161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
247-362 9.80e-46

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: 153.82  E-value: 9.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 247 IKQFYINVEREEWKLDTLCDLYETLTITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRV 326
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119598578 327 LITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIG 362
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
44-237 7.12e-45

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: 153.90  E-value: 7.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIiPCI-KGYDVIAQAQSGTGKTATFAISILQQLEIEFKET--QALVLAPTRELAQQIQKV 120
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAI-PILlHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 121 ILALGDYMGATCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEI 200
Cdd:cd17957   80 LLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119598578 201 FQKL-NTSIQVVLLSATMPTDVLEVTKKFMRDPIRILV 237
Cdd:cd17957  160 LAACtNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
44-235 2.62e-44

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: 152.73  E-value: 2.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL---EIEFKETQ--ALVLAPTRELAQQIQ 118
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 119 KVILALGDYMGA--TCHACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRY--LSPKWIKMFVLDEADEMLSRGFK 194
Cdd:cd17960   81 EVLQSFLEHHLPklKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 119598578 195 DQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
35-231 3.05e-43

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: 150.33  E-value: 3.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIiPCI-KGYDVIAQAQSGTGKTATFAISILQQL-------EIEFKETQ--- 103
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIIlAGRDLMACAQTGSGKTAAFLLPIISKLledgppsVGRGRRKAyps 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 104 ALVLAPTRELAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEApHIVVGTPGRVFDMLNRRYLSPKWIKMFVLD 183
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGC-DILVATPGRLVDFIERGRISLSSIKFLVLD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119598578 184 EADEMLSRGFKDQIYEIFQKLN----TSIQVVLLSATMPTDVLEVTKKFMRD 231
Cdd:cd17967  160 EADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLKN 211
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
40-235 2.08e-41

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: 145.60  E-value: 2.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  40 LKESLLRGIYAYGFEKPSAIQQRAIiPCI-KGYDVIAQAQSGTGKTATFAI----SILQQLEIEFKETQ-ALVLAPTREL 113
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQAL-PAImSGRDVIGIAKTGSGKTLAFLLpmfrHIKDQRPVKPGEGPiGLIMAPTREL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 114 AQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQAEApHIVVGTPGRVFDML---NRRYLSPKWIKMFVLDEADEMLS 190
Cdd:cd17953   98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGA-EIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 119598578 191 RGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17953  177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
44-235 7.15e-41

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: 144.38  E-value: 7.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQ---QLEIEFKET-----QALVLAPTRELAQ 115
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisRLPPLDEETkddgpYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 116 QIQKVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKD 195
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLR-NGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 196 QIYEIFQKLNTSI--------------------QVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17945  160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
32-243 4.35e-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: 142.47  E-value: 4.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  32 VDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIiPCIKGY---DVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLA 108
Cdd:cd18048   17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 109 PTRELAQQIQKVIlalgDYMGATCHACIGGTNVR-NEMQKLQAEAPHIVVGTPGRVFD-MLNRRYLSPKWIKMFVLDEAD 186
Cdd:cd18048   96 PTFELALQTGKVV----EEMGKFCVGIQVIYAIRgNRPGKGTDIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEAD 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119598578 187 EMLS-RGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILVKKEELT 243
Cdd:cd18048  172 VMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
34-230 5.55e-40

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: 143.18  E-value: 5.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  34 NFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL------EIEFKETQ---A 104
Cdd:cd18052   44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltASSFSEVQepqA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 105 LVLAPTRELAQQIQKVILALGDymGATCHACI--GGTNVRNEMQKLQAEApHIVVGTPGRVFDMLNRRYLSPKWIKMFVL 182
Cdd:cd18052  124 LIVAPTRELANQIFLEARKFSY--GTCIRPVVvyGGVSVGHQIRQIEKGC-HILVATPGRLLDFIGRGKISLSKLKYLIL 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119598578 183 DEADEMLSRGFKDQIYEIFQKLN----TSIQVVLLSATMPTDVLEVTKKFMR 230
Cdd:cd18052  201 DEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
44-235 7.43e-39

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: 138.32  E-value: 7.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFA----ISILQQLEIEFKETQ-ALVLAPTRELAQQIQ 118
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIwpmlVHIMDQRELEKGEGPiAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 119 KVILALGDYMGATCHACIGGTNvRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIY 198
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGS-KWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119598578 199 EIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
44-235 5.36e-38

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: 135.75  E-value: 5.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTRELAQQIQKVILA 123
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 124 LGDYMGATCHA-CIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQ 202
Cdd:cd17962   81 LMKGLPPMKTAlLVGGLPLPPQLYRLQ-QGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 119598578 203 KLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17962  160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
44-235 2.22e-37

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: 134.42  E-value: 2.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISIL-----QQLEIEFKETQALVLAPTRELAQQIQ 118
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 119 KVILALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIY 198
Cdd:cd17966   81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLR-RGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119598578 199 EIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
45-237 3.14e-37

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: 133.95  E-value: 3.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  45 LRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIE-FKETQ---ALVLAPTRELAQQIQKV 120
Cdd:cd17941    2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErWTPEDglgALIISPTRELAMQIFEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 121 ILALGDYMGATCHACIGGTNVRNEMQKLQAEapHIVVGTPGRVFDMLNRR-YLSPKWIKMFVLDEADEMLSRGFKDQIYE 199
Cdd:cd17941   82 LRKVGKYHSFSAGLIIGGKDVKEEKERINRM--NILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119598578 200 IFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRILV 237
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
45-235 1.56e-36

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: 132.10  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  45 LRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL-EIEFKE---TQALVLAPTRELAQQIQKV 120
Cdd:cd17942    2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLyKLKFKPrngTGVIIISPTRELALQIYGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 121 ILALGDYMGATCHACIGGTNVRNEMQKLQAEAPhIVVGTPGRVFDML-NRRYLSPKWIKMFVLDEADEMLSRGFKDQIYE 199
Cdd:cd17942   82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVN-ILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119598578 200 IFQKLNTSIQVVLLSATMPTDVLEVTK-KFMRDPIRI 235
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
35-232 3.13e-36

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 131.29  E-value: 3.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQleiefkeTQALVLAPTRELA 114
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVILALGDYMGA---TCHACIGGTNVRNEMQKLQAEApHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSR 191
Cdd:cd17938   74 EQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGV-DIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119598578 192 GFKDQIYEIFQKL------NTSIQVVLLSATM-PTDVLEVTKKFMRDP 232
Cdd:cd17938  153 GNLETINRIYNRIpkitsdGKRLQVIVCSATLhSFEVKKLADKIMHFP 200
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
52-235 1.83e-35

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: 129.63  E-value: 1.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  52 GFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL---EIEFKETQ---ALVLAPTRELAQQIQKVILALG 125
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVDRSDgtlALVLVPTRELALQIYEVLEKLL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 126 DYmgatCHAC-----IGGTNVRNEMQKLQAEAPhIVVGTPGRVFDML-NRRYLSPKWIKMFVLDEADEMLSRGFKDQIYE 199
Cdd:cd17949   90 KP----FHWIvpgylIGGEKRKSEKARLRKGVN-ILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119598578 200 IFQKLNTSI-------------QVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17949  165 ILELLDDKRskaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
44-235 2.75e-35

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: 128.74  E-value: 2.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFA----ISILQQLEIEFKETQA--LVLAPTRELAQQI 117
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLlpgfIHLDLQPIPREQRNGPgvLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 118 QKVILALgDYMGATChACIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQI 197
Cdd:cd17958   81 EAECSKY-SYKGLKS-VCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119598578 198 YEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
26-233 4.09e-35

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: 129.77  E-value: 4.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  26 SNWNEIVDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL------EIEF 99
Cdd:cd18051   14 ENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 100 KETQ----------ALVLAPTRELAQQIqkvilalgdYMGATCHA-------CI--GGTNVRNEMQKLQaEAPHIVVGTP 160
Cdd:cd18051   94 SESGyygrrkqyplALVLAPTRELASQI---------YDEARKFAyrsrvrpCVvyGGADIGQQMRDLE-RGCHLLVATP 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 161 GRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIFQKLNT----SIQVVLLSATMPTDVLEVTKKFMRDPI 233
Cdd:cd18051  164 GRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpptgERQTLMFSATFPKEIQMLARDFLDNYI 240
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
44-235 9.11e-35

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: 127.46  E-value: 9.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIiPCI-KGYDVIAQAQSGTGKTATFAIS-ILQQLEIEFK-------ETQALVLAPTRELA 114
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGL-PTIlSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKlpfikgeGPYGLIVCPSRELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 115 QQIQKVI------LALGDYMGATCHACIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEM 188
Cdd:cd17951   80 RQTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIR-KGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119598578 189 LSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17951  159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
35-232 1.54e-33

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: 124.45  E-value: 1.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  35 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIiPCIKG---YDVIAQAQSGTGKTATFAISILQQLEIEFKETQALVLAPTR 111
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 112 ELAQQIQKVILALGD-YMGATCHACIGGtnvrNEMQKLQAEAPHIVVGTPGRVFD-MLNRRYLSPKWIKMFVLDEADEML 189
Cdd:cd18047   82 ELALQTGKVIEQMGKfYPELKLAYAVRG----NKLERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMI 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119598578 190 -SRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDP 232
Cdd:cd18047  158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
44-217 4.34e-32

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: 121.19  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIK-GYDVIAQAQSGTGKTATFAISILQQLEIEFKET---------QALVLAPTREL 113
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNgvggkqkplRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 114 AQQIQKVILALGDYMGATCHACIGGTNVRNEmQKLQAEAPHIVVGTPGRVFDMLNRR--YL-SPKWIKMFVLDEADEMLS 190
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQ-ERLLKKRPEIVVATPGRLWELIQEGneHLaNLKSLRFLVLDEADRMLE 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 119598578 191 RG-FKD--QIYEIFQK----LNTSIQVVLLSATM 217
Cdd:cd17946  160 KGhFAEleKILELLNKdragKKRKRQTFVFSATL 193
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
59-230 1.27e-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: 113.79  E-value: 1.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  59 IQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEFKET------QALVLAPTRELAQQIQKVILALGDYMGATC 132
Cdd:cd17944   16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 133 HacIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQIYEIF-----QKLNTS 207
Cdd:cd17944   96 F--YGGTPYQQQIFAIR-NGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDN 172
                        170       180
                 ....*....|....*....|...
gi 119598578 208 IQVVLLSATMPTDVLEVTKKFMR 230
Cdd:cd17944  173 PQTLLFSATCPDWVYNVAKKYMK 195
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
259-362 3.29e-29

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: 109.61  E-value: 3.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  259 WKLDTLCDLYETLTITQAVIFLNTRRKVD--WLTEKmhaRDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 336
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEK---EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100
                  ....*....|....*....|....*.
gi 119598578  337 IDVQQVSLVINYDLPTNRENYIHRIG 362
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIG 103
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
44-227 6.92e-28

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: 109.76  E-value: 6.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQL-------EIEFKETQALVLAPTRELAQQ 116
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 117 IQKVILALGDYMGATCHaCIGGTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEADEMLSRGFKDQ 196
Cdd:cd17948   81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119598578 197 IYEIFQK-------------LNTSIQVVLLSATMPTDVLEVTKK 227
Cdd:cd17948  160 LSHFLRRfplasrrsentdgLDPGTQLVLVSATMPSGVGEVLSK 203
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
32-235 4.40e-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: 107.79  E-value: 4.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  32 VDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATF----AISILQQLEIEFKETQ-ALV 106
Cdd:cd18049   23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYllpaIVHINHQPFLERGDGPiCLV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 107 LAPTRELAQQIQKVILALGD--YMGATChaCIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDE 184
Cdd:cd18049  103 LAPTRELAQQVQQVAAEYGRacRLKSTC--IYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119598578 185 ADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd18049  180 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
32-235 2.49e-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: 106.63  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  32 VDNFDDMNLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATF----AISILQQLEIEFKETQ-ALV 106
Cdd:cd18050   61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYllpaIVHINHQPYLERGDGPiCLV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 107 LAPTRELAQQIQKVILALG--DYMGATChaCIGGTNVRNEMQKLQaEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDE 184
Cdd:cd18050  141 LAPTRELAQQVQQVADDYGksSRLKSTC--IYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119598578 185 ADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd18050  218 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
HELICc smart00490
helicase superfamily c-terminal domain;
287-361 4.22e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 92.27  E-value: 4.22e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119598578   287 DWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRI 361
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
70-216 3.51e-22

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: 91.70  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  70 GYDVIAQAQSGTGKTATFAISILQQLEIefKETQALVLAPTRELAQQIQKVILALGDyMGATCHACIGGTNVrNEMQKLQ 149
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSA-EEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119598578 150 AEAPHIVVGTPGRVFDMLNR--RYLSPKWiKMFVLDEADEMLSRGFKDQIYE--IFQKLNTSIQVVLLSAT 216
Cdd:cd00046   77 LGDADIIIATPDMLLNLLLRedRLFLKDL-KLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
44-221 1.57e-20

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: 89.61  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  44 LLRGIYAYGFEKPSAIQQrAIIP-------CIKGY---DVIAQAQSGTGKTATFAISILQQLEIEFK-ETQALVLAPTRE 112
Cdd:cd17956    1 LLKNLQNNGITSAFPVQA-AVIPwllpsskSTPPYrpgDLCVSAPTGSGKTLAYVLPIVQALSKRVVpRLRALIVVPTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 113 LAQQIQKVILALGDYMGATCHACIGGTNVRNEMQKLQA-------EAPHIVVGTPGRVFDMLNR-RYLSPKWIKMFVLDE 184
Cdd:cd17956   80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylSRVDILVATPGRLVDHLNStPGFTLKHLRFLVIDE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 185 ADEMLSRGF--------------KDQIYEIFQKLNTSI------QVVLLSATMPTDV 221
Cdd:cd17956  160 ADRLLNQSFqdwletvmkalgrpTAPDLGSFGDANLLErsvrplQKLLFSATLTRDP 216
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
27-346 3.23e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 74.29  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  27 NWNEIVDNFDDMNLKESLLRGIYAYGFE-KPSAIQQRAI-----IPCIKGYDVIAQAQSGTGKTATFAISILQQLEIEfk 100
Cdd:COG1061   51 RRLPEEDTERELAEAEALEAGDEASGTSfELRPYQQEALeallaALERGGGRGLVVAPTGTGKTVLALALAAELLRGK-- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 101 etQALVLAPTRELAQQIQKVILALgdymgatchaciggTNVRNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWiKMF 180
Cdd:COG1061  129 --RVLVLVPRRELLEQWAEELRRF--------------LGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRF-GLV 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 181 VLDEADEMLSRGFKdqiyEIFQKLNTSIqVVLLSATmP--TD------------VLEVT-KKFMRD----PIRILVKKEE 241
Cdd:COG1061  192 IIDEAHHAGAPSYR----RILEAFPAAY-RLGLTAT-PfrSDgreillflfdgiVYEYSlKEAIEDgylaPPEYYGIRVD 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 242 LTLEGIKQFYIN-------VEREEWKLDTLCDLYETLT-ITQAVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERD 313
Cdd:COG1061  266 LTDERAEYDALSerlrealAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKERE 345
                        330       340       350
                 ....*....|....*....|....*....|...
gi 119598578 314 VIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 346
Cdd:COG1061  346 EILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
39-351 8.76e-14

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: 72.95  E-value: 8.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  39 NLKESLLRGIYAYGFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFAISILQQLeIEFKETQALVLAPTRELAQ-QI 117
Cdd:COG1205   40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 118 QKvILALGDYMGA--TCHACIGGTNvRNEMQKLQaEAPHIVVGTPgrvfDMLNRRYLS--PKWIKMF------VLDEADE 187
Cdd:COG1205  119 RR-LRELAEALGLgvRVATYDGDTP-PEERRWIR-EHPDIVLTNP----DMLHYGLLPhhTRWARFFrnlryvVIDEAHT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 188 MlsRG-FKDQIYEIFQKLN-------TSIQVVLLSATM--PT---------DVLEVTKK----------FMRDPIRILVK 238
Cdd:COG1205  192 Y--RGvFGSHVANVLRRLRricrhygSDPQFILASATIgnPAehaerltgrPVTVVDEDgsprgertfvLWNPPLVDDGI 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 239 KEELTLEGIKQFYINVEREewkLDTLCdlyetltitqaviFLNTRRKV----DWLTEKMHARDFT--VSALHGDMDQKER 312
Cdd:COG1205  270 RRSALAEAARLLADLVREG---LRTLV-------------FTRSRRGAellaRYARRALREPDLAdrVAAYRAGYLPEER 333
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 119598578 313 DVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 351
Cdd:COG1205  334 REIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYP 372
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
261-358 3.57e-11

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 60.68  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 261 LDTLCDLYETLTITQAVIFLNTRRKV----DWLTEKMHARDF-----------TVSALHGDMDQKERDVIMREFRSGSSR 325
Cdd:cd18802   13 IEILREYFPKTPDFRGIIFVERRATAvvlsRLLKEHPSTLAFircgfligrgnSSQRKRSLMTQRKQKETLDKFRDGELN 92
                         90       100       110
                 ....*....|....*....|....*....|...
gi 119598578 326 VLITTDLLARGIDVQQVSLVINYDLPTNRENYI 358
Cdd:cd18802   93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
260-353 2.39e-09

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: 55.18  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 260 KLDTLCDLYETLTITQ--AVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSS--RVLITTDLLAR 335
Cdd:cd18793   12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
                         90
                 ....*....|....*...
gi 119598578 336 GIDVQQVSLVINYDLPTN 353
Cdd:cd18793   92 GLNLTAANRVILYDPWWN 109
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
55-235 2.85e-09

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: 57.39  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  55 KPSAIQqRAIIPCIKG---YDVIAQ--------------AQSGTGKTATF---AISILQQLEIEFKET------------ 102
Cdd:cd17965   30 KPSPIQ-TLAIKKLLKtlmRKVTKQtsneepklevfllaAETGSGKTLAYlapLLDYLKRQEQEPFEEaeeeyesakdtg 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 103 --QALVLAPTRELAQQIQKVILALGDYMG---ATCHACIGGTNVRNemQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWI 177
Cdd:cd17965  109 rpRSVILVPTHELVEQVYSVLKKLSHTVKlgiKTFSSGFGPSYQRL--QLAFKGRIDILVTTPGKLASLAKSRPKILSRV 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119598578 178 KMFVLDEADEMLSRGFKDQIYEIFQKLNTSIQVVLLSATMPTDVLEVTKKFMRDPIRI 235
Cdd:cd17965  187 THLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI 244
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
32-337 5.65e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 57.98  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  32 VDNFDDMNLKESLLRGiyayGFEK--PSaiQQRAIIPCI-KGYDVIAQAQSGTGKTATFAISILQQLEIEFKetqALVLA 108
Cdd:COG1204    3 VAELPLEKVIEFLKER----GIEElyPP--QAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 109 PTRELAQQI------------QKVILALGDYmgatchaciggtnvrnEMQKLQAEAPHIVVGTPGRvFDMLNRRylSPKW 176
Cdd:COG1204   74 PLRALASEKyrefkrdfeelgIKVGVSTGDY----------------DSDDEWLGRYDILVATPEK-LDSLLRN--GPSW 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 177 IK---MFVLDEA----DEmlSRGFkdqIYEI----FQKLNTSIQVVLLSATM--PTDVLE-VTKKFMRDPIRIlVKKEEL 242
Cdd:COG1204  135 LRdvdLVVVDEAhlidDE--SRGP---TLEVllarLRRLNPEAQIVALSATIgnAEEIAEwLDAELVKSDWRP-VPLNEG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 243 TLEGIKQFYINVEREEwkLDTLCDL-YETLTI-TQAVIFLNTRRKVDWLTEKMHAR------------------------ 296
Cdd:COG1204  209 VLYDGVLRFDDGSRRS--KDPTLALaLDLLEEgGQVLVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevs 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119598578 297 -----DFTVSAL--------HGDMDQKERDVIMREFRSGSSRVLITTDLLARGI 337
Cdd:COG1204  287 eethtNEKLADClekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV 340
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
70-217 8.55e-09

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: 54.90  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  70 GYDVIAQAQSGTGKTATFAISILQQLeIEFKETQALVLAPTRELAQQIQKVILALGDYMGA--TCHACIGGTNvRNEMQK 147
Cdd:cd17923   15 GRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRELLEQLGLgiRVATYDGDTP-REERRA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 148 LQAEAPHIVVGTPgrvfDMLNRRYLSP--KWIKMF------VLDEAD----------EMLSRGFKDqiyeIFQKLNTSIQ 209
Cdd:cd17923   93 IIRNPPRILLTNP----DMLHYALLPHhdRWARFLrnlryvVLDEAHtyrgvfgshvALLLRRLRR----LCRRYGADPQ 164

                 ....*...
gi 119598578 210 VVLLSATM 217
Cdd:cd17923  165 FILTSATI 172
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
276-356 3.62e-08

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 55.62  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 276 AVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPTN 353
Cdd:COG0553  552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631

                 ....*
gi 119598578 354 --REN 356
Cdd:COG0553  632 paVEE 636
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
142-330 1.38e-07

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: 53.55  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 142 RNEMQKLQAEaphIVVGTPGRVFDML--NRRYLSPKWIKM----FVLDEAD----EMLsRGFKDQIYEIfQKLNTSiqVV 211
Cdd:COG1203  231 KLLKELWDAP---VVVTTIDQLFESLfsNRKGQERRLHNLansvIILDEVQayppYML-ALLLRLLEWL-KNLGGS--VI 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 212 LLSATMPTDVlevtKKFMRDPIRILVKKEELTLEGIKQFY---INVEREEWKLDTLCDLYETL--TITQAVIFLNTRRKV 286
Cdd:COG1203  304 LMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAELILEAlhKGKSVLVIVNTVKDA 379
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119598578 287 DWLTEKMHARDFTVSA--LHGDMDQKER----DVIMREFRSGSSRVLITT 330
Cdd:COG1203  380 QELYEALKEKLPDEEVylLHSRFCPADRseieKEIKERLERGKPCILVST 429
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
277-357 4.07e-07

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 52.02  E-value: 4.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 277 VIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 356
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319

                 .
gi 119598578 357 Y 357
Cdd:PRK11057 320 Y 320
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
70-224 1.69e-06

DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 47.58  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  70 GYDVIAQAQSGTGKTATFAISILQQL-EIEFKETQALVLAPTRELAQQIQKVILALGDYMGATCHACI--GGTNvRNEMQ 146
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhGDTS-QSEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 147 KLQAEAPHIVVGTPGRVFDMLNRRYLSPKW--IKMFVLDEADEMLS--RG--FKDQIYEIFQKLNTSIQVVLLSATM--P 218
Cdd:cd17922   80 KQLKNPPGILITTPESLELLLVNKKLRELFagLRYVVVDEIHALLGskRGvqLELLLERLRKLTGRPLRRIGLSATLgnL 159

                 ....*.
gi 119598578 219 TDVLEV 224
Cdd:cd17922  160 EEAAAF 165
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
266-349 6.93e-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: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 266 DLYETLtitQAVIFLNTRRKVDWLTEKMhARDFT---------VSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 336
Cdd:cd18790   15 DLLGEI---RKRVARGERVLVTTLTKRM-AEDLTeylqelgvkVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREG 90
                         90
                 ....*....|...
gi 119598578 337 IDVQQVSLVINYD 349
Cdd:cd18790   91 LDLPEVSLVAILD 103
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
72-185 8.47e-06

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.11  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  72 DVIAQAQSGTGKTAtfaISIL-------QQLEIEFKETQALVLAPTRELAQQIQKVIlalGDYMGATCHACIGGTNV--- 141
Cdd:cd18034   18 NTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAI---RSHTDLKVGEYSGEMGVdkw 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119598578 142 RNEMQKLQAEAPHIVVGTPGRVFDMLNRRYLSPKWIKMFVLDEA 185
Cdd:cd18034   92 TKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
289-349 9.74e-06

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: 45.41  E-value: 9.74e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119598578 289 LTEKMHArDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 349
Cdd:cd18811   54 LKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
61-218 1.13e-05

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: 45.72  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  61 QRAIIPCIKGYD--VIAQAQSGTGKTATFAISILQQL-EIEFKetqALVLAPTRELAQQI------------QKVILALG 125
Cdd:cd17921    6 QREALRALYLSGdsVLVSAPTSSGKTLIAELAILRALaTSGGK---AVYIAPTRALVNQKeadlrerfgplgKNVGLLTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 126 DYmgatchaciggtnvrnEMQKLQAEAPHIVVGTPGRvFDMLNRRyLSPKWIK---MFVLDEA----DEmlSRGfkdQIY 198
Cdd:cd17921   83 DP----------------SVNKLLLAEADILVATPEK-LDLLLRN-GGERLIQdvrLVVVDEAhligDG--ERG---VVL 139
                        170       180
                 ....*....|....*....|....
gi 119598578 199 EI----FQKLNTSIQVVLLSATMP 218
Cdd:cd17921  140 ELllsrLLRINKNARFVGLSATLP 163
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
277-361 1.55e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 47.06  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 277 VIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 356
Cdd:COG0514  234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313

                 ....*
gi 119598578 357 YIHRI 361
Cdd:COG0514  314 YYQEI 318
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
278-351 2.15e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 44.18  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 278 IFLNTRRKVDWLTEKMHAR------DFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 351
Cdd:cd18796   43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
275-350 3.99e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 45.88  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 275 QAVIFLNTRRKVDWLTEKMHARDFTV------SALHGD--MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 346
Cdd:COG1111  355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434

                 ....
gi 119598578 347 NYDL 350
Cdd:COG1111  435 FYEP 438
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
275-337 6.22e-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: 42.93  E-value: 6.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119598578 275 QAVIFLNTRRKvdwlTEKMhARDFT-VSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGI 337
Cdd:cd18795   45 PVLVFCSSRKE----CEKT-AKDLAgIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
208-339 9.88e-05

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 43.96  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 208 IQVVLLSATMPtdvlEVTKKFMRDpIRILVKKEELTLEGIKQFYINVEREEWKLD--TLCDLYETL-TITQAVIFLNTRR 284
Cdd:cd09639  155 VPILLMSATLP----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEisSLERLLEFIkKGGSVAIIVNTVD 229
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119598578 285 KV----DWLTEKMHarDFTVSALHGDMDQKER----DVIMREFRSGSSRVLITTDLLARGIDV 339
Cdd:cd09639  230 RAqefyQQLKEKGP--EEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI 290
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
276-361 1.75e-04

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: 41.04  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 276 AVIFLNTRRKVDWLTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRE 355
Cdd:cd18794   33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112

                 ....*.
gi 119598578 356 NYIHRI 361
Cdd:cd18794  113 SYYQES 118
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
291-330 3.60e-04

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 42.73  E-value: 3.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119598578 291 EKMHAR------DFTVSALHGDMDQKERDVIMREFRSGSSRVLITT 330
Cdd:COG1200  491 EETYEElreafpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
289-345 4.54e-04

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 42.34  E-value: 4.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119598578 289 LTEKMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLV 345
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
307-349 1.18e-03

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: 38.88  E-value: 1.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 119598578 307 MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 349
Cdd:cd18801   74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD 116
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
292-349 1.23e-03

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 39.17  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119598578 292 KMHARDFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 349
Cdd:cd18792   55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
52-233 1.66e-03

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


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 39.44  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578  52 GFEKPSAIQQRAIIPCIKGYDVIAQAQSGTGKTATFaisilqQLEIEFKETQALVLAPTRELAQ-QIQKVILalgdyMGA 130
Cdd:cd17920    9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISLMQdQVDRLQQ-----LGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598578 131 TChACIGGT----NVRNEMQKLQAEAPHIVVGTP-----GRVFDMLNRRYlSPKWIKMFVLDEA-----------DEMLs 190
Cdd:cd17920   78 RA-AALNSTlspeEKREVLLRIKNGQYKLLYVTPerllsPDFLELLQRLP-ERKRLALIVVDEAhcvsqwghdfrPDYL- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119598578 191 rgfkdQIYEIFQKLNtSIQVVLLSATMP----TDVLEVTKkfMRDPI 233
Cdd:cd17920  155 -----RLGRLRRALP-GVPILALTATATpevrEDILKRLG--LRNPV 193
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
297-339 1.97e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 40.52  E-value: 1.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 119598578 297 DFTVSALHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDV 339
Cdd:PRK10917 505 ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDV 547
 
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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