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Conserved domains on  [gi|224036361|pdb|3EIQ|D]
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Chain D, Eukaryotic initiation factor 4A-I

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 ...
28-414 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: 617.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        28 EGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLK 107
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       108 ATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMF 187
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLK-AGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       188 VLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWK 267
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       268 LDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 347
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D       348 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 414
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
28-414 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 617.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        28 EGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLK 107
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       108 ATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMF 187
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLK-AGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       188 VLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWK 267
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       268 LDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 347
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D       348 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 414
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 ...
42-243 3.04e-149

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: 421.08  E-value: 3.04e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 121
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 243
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
41-408 2.98e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 419.55  E-value: 2.98e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL-KATQALVLAPTRE 119
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      120 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRG 199
Cdd:COG0513  83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      200 FKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDLYETLT 279
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDED 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      280 ITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPT 359
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
3EIQ_D      360 NRENYIHRIgrggrfgrkgVAINMVTEEDKRTLRDIETFYNTSIEEMPL 408
Cdd:COG0513 321 DPEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
64-231 3.71e-57

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 185.14  E-value: 3.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D         64 SAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACI 143
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        144 GGTNVRAEVQKLQmeAPHIIVGTPGRVFDML-NRRYLspKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSA 222
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLqERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
3EIQ_D        223 TMPSDVLEV 231
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
55-257 6.22e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 183.08  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D          55 IYAYGFEKPSAIQQRAILPCIKGY-DVIAQAQSGTGKTATFAISILQQIeLDLKATQALVLAPTRELAQQIQKVVMALGD 133
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D         134 YMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNS 213
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
3EIQ_D         214 NTQVVLLSATMPSDVLEVTKKFMRDPIRILVkkEELTLEGIRQF 257
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
 
Name Accession Description Interval E-value
PTZ00424 PTZ00424
helicase 45; Provisional
28-414 0e+00

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 617.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        28 EGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLK 107
Cdd:PTZ00424  16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       108 ATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMF 187
Cdd:PTZ00424  96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLK-AGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       188 VLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWK 267
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       268 LDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 347
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D       348 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 414
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 ...
42-243 3.04e-149

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: 421.08  E-value: 3.04e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 121
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd18046  81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 243
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
41-408 2.98e-145

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 419.55  E-value: 2.98e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL-KATQALVLAPTRE 119
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      120 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRG 199
Cdd:COG0513  83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      200 FKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDLYETLT 279
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDED 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      280 ITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPT 359
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
3EIQ_D      360 NRENYIHRIgrggrfgrkgVAINMVTEEDKRTLRDIETFYNTSIEEMPL 408
Cdd:COG0513 321 DPEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
44-243 6.02e-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: 384.75  E-value: 6.02e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       44 DMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQ 123
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      124 IQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQ 203
Cdd:cd17939  81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQY-GPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
3EIQ_D      204 IYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 243
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
42-243 2.00e-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: 312.48  E-value: 2.00e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 121
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd18045  81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLD-YGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 243
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
41-409 8.24e-87

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 271.29  E-value: 8.24e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 120
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       121 AQQIQKVVMALGDYMG-----ASChaciGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 195
Cdd:PRK11776  85 ADQVAKEIRRLARFIPnikvlTLC----GGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       196 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEElTLEGIRQFYINVEREEwKLDTLCDLY 275
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDE-RLPALQRLL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       276 ETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 355
Cdd:PRK11776 238 LHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
3EIQ_D       356 DLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLN 409
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
51-242 3.48e-85

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: 258.14  E-value: 3.48e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL----KATQALVLAPTRELAQQIQK 126
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      127 VVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 206
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*.
3EIQ_D      207 IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
37-414 1.36e-76

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 249.77  E-value: 1.36e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        37 EIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAP 116
Cdd:PRK11634   3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       117 TRELAQQIQKVVMALGDYM-GASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 195
Cdd:PRK11634  83 TRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       196 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDLY 275
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       276 ETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 355
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
3EIQ_D       356 DLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 414
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
47-242 3.21e-67

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: 212.05  E-value: 3.21e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       47 LSESLLRGIYAYGFEKPSAIQQRAiLPCIKG---YDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQ 123
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETA-LPLILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      124 IQKVVMALGDYMGASCHACIGGTNVRAevqKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEML-SRGFKD 202
Cdd:cd17963  80 IGEVVEKMGKFTGVKVALAVPGNDVPR---GKKITA-QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
3EIQ_D      203 QIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
42-242 4.23e-64

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: 204.07  E-value: 4.23e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 121
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd17940  81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLY-QTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
42-407 2.28e-63

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 210.92  E-value: 2.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALVL 114
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       115 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVraEVQKLQMEAPH--IIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA 192
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDF--DKQLKQLEARFcdILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       193 DEMLSRGFKDQIYDIFQKL--NSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQ-FYINVEREEWKLd 269
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL- 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       270 tLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQV 349
Cdd:PRK01297 326 -LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
3EIQ_D       350 SLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIE-EMP 407
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
42-396 2.60e-61

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 204.41  E-value: 2.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeLDL---KATQA--LVLAP 116
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL-LDFprrKSGPPriLILTP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       117 TRELAQQIQKVVMALGDYMGASCHACIGGTNV--RAEVQKlqmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 194
Cdd:PRK11192  82 TRELAMQVADQARELAKHTHLDIATITGGVAYmnHAEVFS---ENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       195 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSD-VLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCD 273
Cdd:PRK11192 159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       274 LYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
3EIQ_D       354 NYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIE 396
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
41-408 3.15e-61

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 205.04  E-value: 3.15e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELD------LKATQALVL 114
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       115 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 194
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLR-GGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       195 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDL 274
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       275 YETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 354
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
3EIQ_D       355 YDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPL 408
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAI 373
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
51-242 2.29e-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: 2.29e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMA 130
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      131 LGDYM-GASCHACIGGTNVRAEVQKLQmeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ 209
Cdd:cd17943  81 IGKKLeGLKCEVFIGGTPVKEDKKKLK--GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
                       170       180       190
                ....*....|....*....|....*....|...
3EIQ_D      210 KLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17943 159 SLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
41-244 4.76e-58

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: 188.71  E-value: 4.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 120
Cdd:cd17950   3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      121 AQQIQKVVMALGDYMGASCHACI-GGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEML-SR 198
Cdd:cd17950  83 AFQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQL 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3EIQ_D      199 GFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 244
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
41-395 2.40e-57

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 196.16  E-value: 2.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIEL-------DLKATQALV 113
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAMV 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       114 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 193
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQ-QGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       194 EMLSRGFKDQIYDIFQKLnSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDtlcd 273
Cdd:PLN00206 281 CMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK---- 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       274 LYETLTITQ-----AVIFINTRRKVDWLTEKMH-ARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 347
Cdd:PLN00206 356 LFDILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
3EIQ_D       348 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDI 395
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
64-231 3.71e-57

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 185.14  E-value: 3.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D         64 SAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACI 143
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        144 GGTNVRAEVQKLQmeAPHIIVGTPGRVFDML-NRRYLspKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSA 222
Cdd:pfam00270  81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLqERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
3EIQ_D        223 TMPSDVLEV 231
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
55-257 6.22e-56

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 183.08  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D          55 IYAYGFEKPSAIQQRAILPCIKGY-DVIAQAQSGTGKTATFAISILQQIeLDLKATQALVLAPTRELAQQIQKVVMALGD 133
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D         134 YMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNS 213
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
3EIQ_D         214 NTQVVLLSATMPSDVLEVTKKFMRDPIRILVkkEELTLEGIRQF 257
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
41-408 2.37e-53

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 186.69  E-value: 2.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALV 113
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       114 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNR-RYLSPKYIKMFVLDEA 192
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQ-QGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       193 DEMLSRGFKDQIYDIFQKLNSNT--QVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQfYINVEREEWKLDT 270
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ-RIYFPADEEKQTL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       271 LCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVS 350
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
3EIQ_D       351 LVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPL 408
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
PTZ00110 PTZ00110
helicase; Provisional
39-368 7.94e-53

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 184.59  E-value: 7.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        39 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATF----AISILQQIELDL-KATQALV 113
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFllpaIVHINAQPLLRYgDGPIVLV 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       114 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 193
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALR-RGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       194 EMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRD-PIRILVKKEELTL-EGIRQfYINVEREEWKLDTL 271
Cdd:PTZ00110 288 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEEHEKRGKL 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       272 CDLYETLTI--TQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQV 349
Cdd:PTZ00110 367 KMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
                        330
                 ....*....|....*....
3EIQ_D       350 SLVINYDLPTNRENYIHRI 368
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRI 465
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
42-239 4.10e-52

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 173.18  E-value: 4.10e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 121
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKY---IKMFVLDEADEMLSR 198
Cdd:cd17955  81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELS-KRPHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDEADRLLTG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EIQ_D      199 GFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDP 239
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 ...
41-242 4.28e-52

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: 173.27  E-value: 4.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 120
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      121 AQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLqMEAPHIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRG 199
Cdd:cd17954  81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIAL-AKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMD 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
3EIQ_D      200 FKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
47-237 4.79e-51

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: 170.84  E-value: 4.79e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       47 LSESLLRGIYAYGFEKPSAIQQRAILPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKATQ-----ALVLAPTREL 120
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      121 AQQIQKVVMALGDYM-GASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLnRRYLSPKY---IKMFVLDEADEML 196
Cdd:cd17964  81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHL-ENPGVAKAftdLDYLVLDEADRLL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3EIQ_D      197 SRGFKDQIYDIFQKLN----SNTQVVLLSATMPSDVLEVTKKFMR 237
Cdd:cd17964 160 DMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
42-403 4.45e-50

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 174.39  E-value: 4.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKT-----ATFAISILQQIELDLKATQ--ALVL 114
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFHYLLSHPAPEDRKVNQprALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       115 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 194
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLE-SGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       195 MLSRGFKDQIYDIFQKLNSNTQ--VVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQ--FYINVEReewKLDT 270
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       271 LCDLYETLTITQAVIFINTRRKV----DWLTEKMHardfTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDV 346
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCeeiwGHLAADGH----RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D       347 QQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSI 403
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
51-242 1.06e-48

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: 163.96  E-value: 1.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI---ELDLKATQALVLAPTRELAQQIQKV 127
Cdd:cd17947   1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      128 VMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 206
Cdd:cd17947  81 LQQLAQFTDITFALAVGGLSLKAQEAALR-ARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
                       170       180       190
                ....*....|....*....|....*....|....*.
3EIQ_D      207 IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
47-240 7.12e-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: 7.12e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       47 LSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIeLDLKA-------TQALVLAPTR 118
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLAlEGKDILARARTGSGKTAAYALPIIQKI-LKAKAesgeeqgTRALILVPTR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      119 ELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQK-LQMEAPHIIVGTPGRVFDMLNRRYLSPK-YIKMFVLDEADEML 196
Cdd:cd17961  79 ELAQQVSKVLEQLTAYCRKDVRVVNLSASSSDSVQRaLLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
3EIQ_D      197 SRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPI 240
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
41-242 2.02e-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: 160.93  E-value: 2.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQieldLKA------TQALVL 114
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK----LKAhsptvgARALIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      115 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLqMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 194
Cdd:cd17959  78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEAL-ASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3EIQ_D      195 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17959 157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
41-238 2.37e-45

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: 156.11  E-value: 2.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIELD---------LKAT- 109
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIIlAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsvgrgrRKAYp 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      110 QALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAevQKLQMEAP-HIIVGTPGRVFDMLNRRYLSPKYIKMFV 188
Cdd:cd17967  80 SALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVH--QQLQLLRGcDILVATPGRLVDFIERGRISLSSIKFLV 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
3EIQ_D      189 LDEADEMLSRGFKDQIYDIFQKLNS----NTQVVLLSATMPSDVLEVTKKFMRD 238
Cdd:cd17967 158 LDEADRMLDMGFEPQIRKIVEHPDMppkgERQTLMFSATFPREIQRLAADFLKN 211
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
254-369 2.91e-45

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: 152.66  E-value: 2.91e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      254 IRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRV 333
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                        90       100       110
                ....*....|....*....|....*....|....*.
3EIQ_D      334 LITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIG 369
Cdd:cd18787  81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
51-244 5.93e-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: 154.28  E-value: 5.93e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKAT--QALVLAPTRELAQQIQKV 127
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAI-PILlHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      128 VMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDI 207
Cdd:cd17957  80 LLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
                       170       180       190
                ....*....|....*....|....*....|....*...
3EIQ_D      208 FQKL-NSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 244
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, ...
51-242 2.53e-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: 2.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-----ELDLKATQALVLAPTRELAQQIQ 125
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      126 KVVMALGDYMGA--SCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRY--LSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd17960  81 EVLQSFLEHHLPklKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
47-242 1.58e-42

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: 148.68  E-value: 1.58e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       47 LSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQI--ELDLKATQ---ALVLAPTREL 120
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQAL-PAImSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPGEgpiGLIMAPTREL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      121 AQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDML---NRRYLSPKYIKMFVLDEADEMLS 197
Cdd:cd17953  98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGA-EIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFD 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3EIQ_D      198 RGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
39-250 5.15e-41

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: 145.16  E-value: 5.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       39 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAiLPCIKGY---DVIAQAQSGTGKTATFAISILQQIELDLKATQALVLA 115
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENA-LPMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      116 PTRELAQQIQKVVMALGDY-MGASCHACIGGTNVRaevQKLQMEApHIIVGTPGRVFD-MLNRRYLSPKYIKMFVLDEAD 193
Cdd:cd18048  96 PTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPG---KGTDIEA-QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEAD 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
3EIQ_D      194 EMLS-RGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELT 250
Cdd:cd18048 172 VMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
51-242 6.16e-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: 144.77  E-value: 6.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI----ELDLKATQ----ALVLAPTRELAQ 122
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlpPLDEETKDdgpyALILAPTRELAQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      123 QIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKD 202
Cdd:cd17945  81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGC-EILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      203 QIYDIFQKLNSNT--------------------QVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
41-237 1.35e-39

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: 142.41  E-value: 1.35e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQ-IELDLKAT--------QA 111
Cdd:cd18052  44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTASsfsevqepQA 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      112 LVLAPTRELAQQIQKVVMALGDymGASCHACI--GGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVL 189
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSY--GTCIRPVVvyGGVSVGHQIRQIEKGC-HILVATPGRLLDFIGRGKISLSKLKYLIL 200
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
3EIQ_D      190 DEADEMLSRGFKDQIYDIFQKLNS----NTQVVLLSATMPSDVLEVTKKFMR 237
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEPGMpskeDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
51-242 4.75e-39

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: 138.84  E-value: 4.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMA 130
Cdd:cd17962   1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      131 LGDYMGASCHA-CIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ 209
Cdd:cd17962  81 LMKGLPPMKTAlLVGGLPLPPQLYRLQ-QGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
                       170       180       190
                ....*....|....*....|....*....|...
3EIQ_D      210 KLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17962 160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
51-242 5.85e-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: 138.70  E-value: 5.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeLDLKATQ------ALVLAPTRELAQQI 124
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      125 QKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQI 204
Cdd:cd17952  80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQ-EGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
                       170       180       190
                ....*....|....*....|....*....|....*...
3EIQ_D      205 YDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
51-242 4.76e-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: 133.65  E-value: 4.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeldlKATQ---------ALVLAPTRELA 121
Cdd:cd17966   1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI----NAQPplergdgpiVLVLAPTRELA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 201
Cdd:cd17966  77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLR-RGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFE 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EIQ_D      202 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17966 156 PQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
52-244 5.98e-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: 133.18  E-value: 5.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       52 LRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI------ELDlkATQALVLAPTRELAQQIQ 125
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtPED--GLGALIISPTRELAMQIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      126 KVVMALGDYMGASCHACIGGTNVRAEvqKLQMEAPHIIVGTPGRVFDMLNRR-YLSPKYIKMFVLDEADEMLSRGFKDQI 204
Cdd:cd17941  80 EVLRKVGKYHSFSAGLIIGGKDVKEE--KERINRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
3EIQ_D      205 YDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 244
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
42-239 9.38e-37

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


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 132.83  E-value: 9.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       42 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQqieldlkATQALVLAPTRELA 121
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVVMALGDYMGA---SCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSR 198
Cdd:cd17938  74 EQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGV-DIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3EIQ_D      199 GFKDQIYDIFQKLNSNT------QVVLLSATMPS-DVLEVTKKFMRDP 239
Cdd:cd17938 153 GNLETINRIYNRIPKITsdgkrlQVIVCSATLHSfEVKKLADKIMHFP 200
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
33-240 1.25e-36

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: 134.01  E-value: 1.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       33 SNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI------ELDL 106
Cdd:cd18051  14 ENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLP 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      107 KATQ----------ALVLAPTRELAQQIqkvvmalgdYMGASCHA-------CI--GGTNVRAEVQKLQmEAPHIIVGTP 167
Cdd:cd18051  94 SESGyygrrkqyplALVLAPTRELASQI---------YDEARKFAyrsrvrpCVvyGGADIGQQMRDLE-RGCHLLVATP 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D      168 GRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLN----SNTQVVLLSATMPSDVLEVTKKFMRDPI 240
Cdd:cd18051 164 GRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTmpptGERQTLMFSATFPKEIQMLARDFLDNYI 240
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
52-242 1.30e-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: 132.48  E-value: 1.30e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       52 LRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISIlqqIELDLK-------ATQALVLAPTRELAQQI 124
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPA---IELLYKlkfkprnGTGVIIISPTRELALQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      125 QKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPhIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQ 203
Cdd:cd17942  79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVN-ILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
3EIQ_D      204 IYDIFQKLNSNTQVVLLSATMPSDVLEVTK-KFMRDPIRI 242
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
51-242 3.21e-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: 3.21e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILqqIELDLKATQ--------ALVLAPTRELAQ 122
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPreqrngpgVLVLTPTRELAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      123 QIQKVVMALgDYMGASChACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKD 202
Cdd:cd17958  79 QIEAECSKY-SYKGLKS-VCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEP 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
3EIQ_D      203 QIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17958 157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
59-242 1.52e-34

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: 127.32  E-value: 1.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       59 GFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-ELDLKATQ-----ALVLAPTRELAQQIQKVVMALg 132
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRsdgtlALVLVPTRELALQIYEVLEKL- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      133 dymGASCHAC-----IGGTNVRAEVQKLQMEAPhIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 206
Cdd:cd17949  89 ---LKPFHWIvpgylIGGEKRKSEKARLRKGVN-ILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
3EIQ_D      207 IFQKLNSNT-------------QVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17949 165 ILELLDDKRskaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
51-242 4.19e-33

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: 123.22  E-value: 4.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISIL-----QQIELDLKATQ---ALVLAPTRELA 121
Cdd:cd17951   1 ILKGLKKKGIKKPTPIQMQGL-PTIlSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      122 QQIQKVV------MALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 195
Cdd:cd17951  80 RQTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIR-KGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
3EIQ_D      196 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
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 ...
41-239 1.60e-32

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 121.75  E-value: 1.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       41 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAiLPCIKG---YDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPT 117
Cdd:cd18047   2 SFEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      118 RELAQQIQKVVMALGD-YMGASCHACIGGTNVRAEVQKlqmeAPHIIVGTPGRVFD-MLNRRYLSPKYIKMFVLDEADEM 195
Cdd:cd18047  81 YELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVM 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3EIQ_D      196 L-SRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDP 239
Cdd:cd18047 157 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
51-224 2.60e-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: 121.96  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIK-GYDVIAQAQSGTGKTATFAISILQQIeLDLKAT----------QALVLAPTRE 119
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERL-LSQKSSngvggkqkplRALILTPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      120 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEvQKLQMEAPHIIVGTPGRVFDMLNRR--YL-SPKYIKMFVLDEADEML 196
Cdd:cd17946  80 LAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQ-ERLLKKRPEIVVATPGRLWELIQEGneHLaNLKSLRFLVLDEADRML 158
                       170       180       190
                ....*....|....*....|....*....|....*
3EIQ_D      197 SRGFKDQIYDIFQKLNSNT-------QVVLLSATM 224
Cdd:cd17946 159 EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
66-237 3.26e-32

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: 120.72  E-value: 3.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       66 IQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL------KATQALVLAPTRELAQQIQKVVMALGDYMGASC 139
Cdd:cd17944  16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      140 HacIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ---KLNS--N 214
Cdd:cd17944  96 F--YGGTPYQQQIFAIR-NGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsyKKDSedN 172
                       170       180
                ....*....|....*....|...
3EIQ_D      215 TQVVLLSATMPSDVLEVTKKFMR 237
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
51-234 5.17e-31

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: 118.62  E-value: 5.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALVLAPTRELAQQ 123
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      124 IQKVVMALGDYMGASCHaCIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQ 203
Cdd:cd17948  81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
3EIQ_D      204 IYDIFQK-------------LNSNTQVVLLSATMPSDVLEVTKK 234
Cdd:cd17948 160 LSHFLRRfplasrrsentdgLDPGTQLVLVSATMPSGVGEVLSK 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
266-369 7.16e-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: 108.84  E-value: 7.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D        266 WKLDTLCDLYETLTITQAVIFINTRRKVD--WLTEKmhaRDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 343
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEK---EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100
                  ....*....|....*....|....*.
3EIQ_D        344 IDVQQVSLVINYDLPTNRENYIHRIG 369
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIG 103
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
39-242 1.40e-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: 109.33  E-value: 1.40e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       39 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQA-----LV 113
Cdd:cd18049  23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      114 LAPTRELAQQIQKVVmalGDYmGASCH---ACI-GGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVL 189
Cdd:cd18049 103 LAPTRELAQQVQQVA---AEY-GRACRlksTCIyGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
3EIQ_D      190 DEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
39-242 1.38e-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: 107.40  E-value: 1.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       39 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQA-----LV 113
Cdd:cd18050  61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLV 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      114 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 193
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
3EIQ_D      194 EMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd18050 220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
77-223 8.47e-25

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: 99.01  E-value: 8.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       77 GYDVIAQAQSGTGKTATFAISILQqiELDLKATQALVLAPTRELAQQIQKVVMALGDyMGASCHACIGGTNVRAEVQKLQ 156
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALL--LLLKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      157 MEAPhIIVGTPGRVFDMLNRRYLSPKY-IKMFVLDEADEMLSRGFKDQIYD--IFQKLNSNTQVVLLSAT 223
Cdd:cd00046  78 GDAD-IIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
HELICc smart00490
helicase superfamily c-terminal domain;
294-368 6.81e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.50  E-value: 6.81e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3EIQ_D         294 DWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRI 368
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
51-228 7.45e-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: 87.69  E-value: 7.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       51 LLRGIYAYGFEKPSAIQQR---AILPCIKGY------DVIAQAQSGTGKTATFAISILQQIeLDLKATQ--ALVLAPTRE 119
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAvipWLLPSSKSTppyrpgDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRlrALIVVPTKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      120 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEvQKLQMEAPH--------IIVGTPGRVFDMLNR-RYLSPKYIKMFVLD 190
Cdd:cd17956  80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKE-QKLLLVDTSgrylsrvdILVATPGRLVDHLNStPGFTLKHLRFLVID 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
3EIQ_D      191 EADEMLSRGF--------------KDQIYDIFQKLN------SNTQVVLLSATMPSDV 228
Cdd:cd17956 159 EADRLLNQSFqdwletvmkalgrpTAPDLGSFGDANllersvRPLQKLLFSATLTRDP 216
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
46-358 9.47e-15

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: 76.03  E-value: 9.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       46 NLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATqALVLAPTRELAQ-QI 124
Cdd:COG1205  40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-ALYLYPTKALARdQL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      125 QKvVMALGDYMGA--SCHACIGGT--NVRAEVQklqmEAPHIIVGTPgrvfDMLNRRYLS--PKYIKMF------VLDEA 192
Cdd:COG1205 119 RR-LRELAEALGLgvRVATYDGDTppEERRWIR----EHPDIVLTNP----DMLHYGLLPhhTRWARFFrnlryvVIDEA 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      193 DEMlsRG-FKDQIYDIFQKLN-------SNTQVVLLSATM--PS---------DVLEVTKK----------FMRDPIRIL 243
Cdd:COG1205 190 HTY--RGvFGSHVANVLRRLRricrhygSDPQFILASATIgnPAehaerltgrPVTVVDEDgsprgertfvLWNPPLVDD 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      244 VKKEELTLEGIRQFYINVEREewkLDTLCdlyetltitqaviFINTRRKV----DWLTEKMHARDFT--VSAMHGDMDQK 317
Cdd:COG1205 268 GIRRSALAEAARLLADLVREG---LRTLV-------------FTRSRRGAellaRYARRALREPDLAdrVAAYRAGYLPE 331
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
3EIQ_D      318 ERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 358
Cdd:COG1205 332 ERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYP 372
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
67-353 8.56e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 8.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       67 QQRAI-----LPCIKGYDVIAQAQSGTGKTaTFAISILQQIELDLKAtqaLVLAPTRELAQQIQKvvmalgdymgaschA 141
Cdd:COG1061  85 QQEALeallaALERGGGRGLVVAPTGTGKT-VLALALAAELLRGKRV---LVLVPRRELLEQWAE--------------E 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      142 CIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYiKMFVLDEADEMLSRGFKdQIYDIFQKlnsnTQVVLLS 221
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRF-GLVIIDEAHHAGAPSYR-RILEAFPA----AYRLGLT 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      222 ATmP--SD------------VLEVT-KKFMRD----PIRILVKKEELTLEGIRQFYIN-------VEREEWKLDTLCDLY 275
Cdd:COG1061 221 AT-PfrSDgreillflfdgiVYEYSlKEAIEDgylaPPEYYGIRVDLTDERAEYDALSerlrealAADAERKDKILRELL 299
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3EIQ_D      276 ETLT-ITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:COG1061 300 REHPdDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
268-365 1.64e-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: 61.84  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      268 LDTLCDLYETLTITQAVIFINTRRKV----DWLTEKMHARD-FTVSAMHG----------DMDQKERDVIMREFRSGSSR 332
Cdd:cd18802  13 IEILREYFPKTPDFRGIIFVERRATAvvlsRLLKEHPSTLAfIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
                        90       100       110
                ....*....|....*....|....*....|...
3EIQ_D      333 VLITTDLLARGIDVQQVSLVINYDLPTNRENYI 365
Cdd:cd18802  93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
267-360 1.43e-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: 55.95  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      267 KLDTLCDLYETLTITQ--AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSS--RVLITTDLLAR 342
Cdd:cd18793  12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
                        90
                ....*....|....*...
3EIQ_D      343 GIDVQQVSLVINYDLPTN 360
Cdd:cd18793  92 GLNLTAANRVILYDPWWN 109
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
80-242 1.70e-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: 58.16  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       80 VIAqAQSGTGKTATFAISILQQI-----------------ELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHAC 142
Cdd:cd17965  65 LLA-AETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyesAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      143 IGGTNVRaeVQKLQMEAPH---IIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVL 219
Cdd:cd17965 144 SSGFGPS--YQRLQLAFKGridILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
                       170       180
                ....*....|....*....|...
3EIQ_D      220 LSATMPSDVLEVTKKFMRDPIRI 242
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
67-344 2.34e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 59.14  E-value: 2.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       67 QQRAILPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKAtqaLVLAPTRELAQQI------------QKVVMALGD 133
Cdd:COG1204  27 QAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGGKA---LYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      134 YmgaschaciggTNVRAEVQKlqmeaPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA----DEmlSRGFK-DQIYDIF 208
Cdd:COG1204 104 Y-----------DSDDEWLGR-----YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      209 QKLNSNTQVVLLSATMPS--DVLE-VTKKFMRDPIRIlVKKEELTLEGIRQFYINVEREEwkLDTLCDL-YETLTI-TQA 283
Cdd:COG1204 166 RRLNPEAQIVALSATIGNaeEIAEwLDAELVKSDWRP-VPLNEGVLYDGVLRFDDGSRRS--KDPTLALaLDLLEEgGQV 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      284 VIFINTRRKVDWLTEKMHAR-----------------------------DFTVSAM--------HGDMDQKERDVIMREF 326
Cdd:COG1204 243 LVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevseethtNEKLADClekgvafhHAGLPSELRRLVEDAF 322
                       330
                ....*....|....*...
3EIQ_D      327 RSGSSRVLITTDLLARGI 344
Cdd:COG1204 323 REGLIKVLVATPTLAAGV 340
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
67-224 3.98e-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: 55.67  E-value: 3.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       67 QQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDlKATQALVLAPTRELAQQIQKVVMALGDYMGASCH-ACIGG 145
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRvATYDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      146 TNVRAEVQKLQMEAPHIIVGTPgrvfDMLN----------RRYLSP-KYIkmfVLDEAD----------EMLSRGFKdqi 204
Cdd:cd17923  84 DTPREERRAIIRNPPRILLTNP----DMLHyallphhdrwARFLRNlRYV---VLDEAHtyrgvfgshvALLLRRLR--- 153
                       170       180
                ....*....|....*....|
3EIQ_D      205 yDIFQKLNSNTQVVLLSATM 224
Cdd:cd17923 154 -RLCRRYGADPQFILTSATI 172
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
154-337 9.55e-08

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 53.93  E-value: 9.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      154 KLQMEAPhIIVGTPGRVFDML--NRRYLSPKYIKM----FVLDEAD----EMLSrgfkdQIYDIFQKLNS-NTQVVLLSA 222
Cdd:COG1203 234 KELWDAP-VVVTTIDQLFESLfsNRKGQERRLHNLansvIILDEVQayppYMLA-----LLLRLLEWLKNlGGSVILMTA 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      223 TMPSDVlevtKKFMRDPIRILVKKEELTLEGIRQFY---INVEREEWKLDTLCD-LYETLTITQAVIFI-NTRRKVDWLT 297
Cdd:COG1203 308 TLPPLL----REELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAElILEALHKGKSVLVIvNTVKDAQELY 383
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3EIQ_D      298 EKMHARDFTVSAM--HGDMDQKER----DVIMREFRSGSSRVLITT 337
Cdd:COG1203 384 EALKEKLPDEEVYllHSRFCPADRseieKEIKERLERGKPCILVST 429
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
79-192 1.24e-07

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: 51.88  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       79 DVIAQAQSGTGKTAtfaISIL-------QQIELDLKATQALVLAPTRELAQQiQkvVMALGDYMGASCHACIGGTNV--- 148
Cdd:cd18034  18 NTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVdkw 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3EIQ_D      149 RAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA 192
Cdd:cd18034  92 TKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
283-363 3.36e-07

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 52.53  E-value: 3.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      283 AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPTN 360
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631

                ....*
3EIQ_D      361 --REN 363
Cdd:COG0553 632 paVEE 636
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
284-364 4.24e-07

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 52.02  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       284 VIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 363
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319

                 .
3EIQ_D       364 Y 364
Cdd:PRK11057 320 Y 320
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
77-231 2.08e-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: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       77 GYDVIAQAQSGTGKTATFAISILQQI-ELDLKATQALVLAPTRELAQQIQKVVMALGDYMGAschaciggtNVRAEV--- 152
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDL---------EIPVAVrhg 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      153 -----QKLQM--EAPHIIVGTPGRVFDMLNRRYLSPKY--IKMFVLDEADEMLS--RG--FKDQIYDIFQKLNSNTQVVL 219
Cdd:cd17922  72 dtsqsEKAKQlkNPPGILITTPESLELLLVNKKLRELFagLRYVVVDEIHALLGskRGvqLELLLERLRKLTGRPLRRIG 151
                       170
                ....*....|....
3EIQ_D      220 LSATM--PSDVLEV 231
Cdd:cd17922 152 LSATLgnLEEAAAF 165
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
68-225 3.51e-06

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 47.26  E-value: 3.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       68 QRAILPCIKGYD--VIAQAQSGTGKT--ATFAI--SILQQIELdlkatqALVLAPTRELAQQI------------QKVVM 129
Cdd:cd17921   6 QREALRALYLSGdsVLVSAPTSSGKTliAELAIlrALATSGGK------AVYIAPTRALVNQKeadlrerfgplgKNVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      130 ALGDYmgaschaciggtnvraEVQKLQMEAPHIIVGTPGRvFDML--NRRYLSPKYIKMFVLDEA----DEmlSRGFK-D 202
Cdd:cd17921  80 LTGDP----------------SVNKLLLAEADILVATPEK-LDLLlrNGGERLIQDVRLVVVDEAhligDG--ERGVVlE 140
                       170       180
                ....*....|....*....|...
3EIQ_D      203 QIYDIFQKLNSNTQVVLLSATMP 225
Cdd:cd17921 141 LLLSRLLRINKNARFVGLSATLP 163
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
296-356 4.52e-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: 46.57  E-value: 4.52e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3EIQ_D      296 LTEKMHArDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18811  54 LKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
273-356 6.63e-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: 6.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      273 DLYETLtitQAVIFINTRRKVDWLTEKMhARDFT---------VSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 343
Cdd:cd18790  15 DLLGEI---RKRVARGERVLVTTLTKRM-AEDLTeylqelgvkVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREG 90
                        90
                ....*....|...
3EIQ_D      344 IDVQQVSLVINYD 356
Cdd:cd18790  91 LDLPEVSLVAILD 103
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
285-358 1.40e-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: 44.95  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      285 IFINTRRKVDWLTEKMHAR------DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 358
Cdd:cd18796  43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
284-368 1.79e-05

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 46.67  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      284 VIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 363
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313

                ....*
3EIQ_D      364 YIHRI 368
Cdd:COG0514 314 YYQEI 318
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
282-357 3.11e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 46.26  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      282 QAVIFINTRRKVDWLTEKMHARDFTV------SAMHGD--MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434

                ....
3EIQ_D      354 NYDL 357
Cdd:COG1111 435 FYEP 438
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
282-344 6.73e-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: 6.73e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3EIQ_D      282 QAVIFINTRRKvdwlTEKMhARDFT-VSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGI 344
Cdd:cd18795  45 PVLVFCSSRKE----CEKT-AKDLAgIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
114-233 6.84e-05

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 43.47  E-value: 6.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      114 LAPTREL-AQQIQkvvmALGDYMGASCHACIGGT-NVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDE 191
Cdd:cd18033  52 MAPTKPLvSQQIE----ACYKITGIPSSQTAELTgSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDE 127
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3EIQ_D      192 ADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTK 233
Cdd:cd18033 128 AHRATGNYAYCQVVRELMRYNSHFRILALTATPGSKLEAVQQ 169
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
283-368 1.55e-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: 41.43  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      283 AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRE 362
Cdd:cd18794  33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112

                ....*.
3EIQ_D      363 NYIHRI 368
Cdd:cd18794 113 SYYQES 118
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
296-352 3.63e-04

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 42.73  E-value: 3.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
3EIQ_D       296 LTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLV 352
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
214-346 4.10e-04

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 42.03  E-value: 4.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      214 NTQVVLLSATMPsdvlEVTKKFMRDpIRILVKKEELTLEGIRQFYINVEREEWKLD--TLCDLYETLT-ITQAVIFINTR 290
Cdd:cd09639 154 DVPILLMSATLP----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEisSLERLLEFIKkGGSVAIIVNTV 228
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3EIQ_D      291 RKV----DWLTEKMHarDFTVSAMHGDMDQKER----DVIMREFRSGSSRVLITTDLLARGIDV 346
Cdd:cd09639 229 DRAqefyQQLKEKGP--EEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI 290
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
299-356 6.06e-04

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


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 40.33  E-value: 6.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
3EIQ_D      299 KMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18792  55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
298-337 6.13e-04

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 41.96  E-value: 6.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
3EIQ_D      298 EKMHAR------DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITT 337
Cdd:COG1200 491 EETYEElreafpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
59-240 1.03e-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: 40.21  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D       59 GFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFaisilqQIELDLKATQALVLAPTRELaQQIQkvVMALGDyMGAS 138
Cdd:cd17920   9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISL-MQDQ--VDRLQQ-LGIR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EIQ_D      139 ChACIGGT----NVRAEVQKLQMEAPHIIVGTP-----GRVFDMLNRRYlSPKYIKMFVLDEA-----------DEMLsr 198
Cdd:cd17920  79 A-AALNSTlspeEKREVLLRIKNGQYKLLYVTPerllsPDFLELLQRLP-ERKRLALIVVDEAhcvsqwghdfrPDYL-- 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3EIQ_D      199 gfkdQIYDIFQKLNsNTQVVLLSATMP----SDVLEVTKkfMRDPI 240
Cdd:cd17920 155 ----RLGRLRRALP-GVPILALTATATpevrEDILKRLG--LRNPV 193
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
314-356 1.07e-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: 39.26  E-value: 1.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
3EIQ_D      314 MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18801  74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD 116
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
304-346 2.35e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 40.13  E-value: 2.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
3EIQ_D       304 DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDV 346
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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