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Conserved domains on  [gi|4826686|ref|NP_004930|]
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ATP-dependent RNA helicase DDX1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
284-625 1.18e-94

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 300.53  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  284 PNAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:COG0513  69 PRAPQALILAPTRELALQVAEELRKLAKYLG---LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  364 VRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVDLKGEDSVPDTVhh 443
Cdd:COG0513 146 VETLVLDEADRMLDMGFIEDIERILKLLP------KERQTLLFSATMPP-EIRKLAKRYLKNPVRIEVAPENATAETI-- 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  444 vvvpvnpkTDRLWErlgkshirtddVHAKDntrpganspemwseaikilKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLE 523
Cdd:COG0513 217 --------EQRYYL-----------VDKRD-------------------KLELLRRLLRDEDPERAIVFCNTKRGADRLA 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:COG0513 259 EKLQKRG---------ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRI 329
                       330       340
                ....*....|....*....|..
gi 4826686  604 GRVGRAERMGLAISLVaTEKEK 625
Cdd:COG0513 330 GRTGRAGAEGTAISLV-TPDER 350
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
93-245 1.82e-82

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


:

Pssm-ID: 293933  Cd Length: 155  Bit Score: 258.66  E-value: 1.82e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   93 MNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLM-KGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTG 171
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKgKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  172 KKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEE 245
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNSALFPAVCLKNAEVEFNFGDK 154
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
4-64 1.43e-39

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 cd17938:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 204  Bit Score: 144.77  E-value: 1.43e-39
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV 61
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
284-625 1.18e-94

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 300.53  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  284 PNAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:COG0513  69 PRAPQALILAPTRELALQVAEELRKLAKYLG---LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  364 VRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVDLKGEDSVPDTVhh 443
Cdd:COG0513 146 VETLVLDEADRMLDMGFIEDIERILKLLP------KERQTLLFSATMPP-EIRKLAKRYLKNPVRIEVAPENATAETI-- 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  444 vvvpvnpkTDRLWErlgkshirtddVHAKDntrpganspemwseaikilKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLE 523
Cdd:COG0513 217 --------EQRYYL-----------VDKRD-------------------KLELLRRLLRDEDPERAIVFCNTKRGADRLA 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:COG0513 259 EKLQKRG---------ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRI 329
                       330       340
                ....*....|....*....|..
gi 4826686  604 GRVGRAERMGLAISLVaTEKEK 625
Cdd:COG0513 330 GRTGRAGAEGTAISLV-TPDER 350
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
288-430 3.80e-90

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: 280.75  E-value: 3.80e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFL 367
Cdd:cd17938  62 VALILEPSRELAEQTYNCIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFF 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  368 VLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVD 430
Cdd:cd17938 142 VLDEADRLLSQGNLETINRIYNRIPKITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWVD 204
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
93-245 1.82e-82

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 258.66  E-value: 1.82e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   93 MNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLM-KGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTG 171
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKgKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  172 KKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEE 245
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNSALFPAVCLKNAEVEFNFGDK 154
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
286-620 1.18e-54

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 194.63  E-value: 1.18e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   286 APKALIVEPSRELAEQTLNNIKQFKKYIDNPKLreLLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:PRK11776  72 RVQALVLCPTRELADQVAKEIRRLARFIPNIKV--LTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALN 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   366 FLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATlhsF--DVKKLSEKIMHFPTWVDLkgeDSVPDtvhh 443
Cdd:PRK11776 150 TLVLDEADRMLDMGFQDAIDAIIRQAP------ARRQTLLFSAT---YpeGIAAISQRFQRDPVEVKV---ESTHD---- 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   444 vvvpvnpktdrlwerlgKSHIRTDDVHAKDNTRpganspemwSEAIKILkgeyavraIKEHKMDQAIIFCRTKIDCDNLE 523
Cdd:PRK11776 214 -----------------LPAIEQRFYEVSPDER---------LPALQRL--------LLHHQPESCVVFCNTKKECQEVA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:PRK11776 260 DALNAQG---------FSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330
                        330
                 ....*....|....*..
gi 4826686   604 GRVGRAERMGLAISLVA 620
Cdd:PRK11776 331 GRTGRAGSKGLALSLVA 347
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
4-64 1.43e-39

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: 144.77  E-value: 1.43e-39
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV 61
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
493-609 1.01e-31

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: 119.24  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    493 KGEYAVRAIKEHKMDQAIIFCRTKIDCDnlEQYFIQQGGgpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICT 572
Cdd:pfam00271   2 KLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG--------IKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 4826686    573 DVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRA 609
Cdd:pfam00271  72 DVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRA 108
DEXDc smart00487
DEAD-like helicases superfamily;
285-430 1.84e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 1.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     285 NAPKALIVEPSRELAEQTLNnikQFKKYIDNPKLRELLIIGGVAARDQLSVLENGV-DIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:smart00487  53 KGGRVLVLVPTRELAEQWAE---ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSN 129
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826686     364 VRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVD 430
Cdd:smart00487 130 VDLVILDEAHRLLDGGFGDQLEKLLKLLP------KNVQLLLLSATPPE-EIENLLELFLNDPVFID 189
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
130-243 2.40e-21

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 90.05  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     130 KGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFG-----FGGTGKKSHNKQFDNYGEEFTMH-DTIGCYLDIDKGHV 203
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKgswgyDGDGGKKYHNSTGPEYGLPLQEPgDVIGCFLDLEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4826686     204 KFSKNGKDL-GLAFEippHMK-NQALFPACVLKNAE-LKFNFG 243
Cdd:smart00449  81 SFYKNGKYLhGLAFF---DVKfSGPLYPAFSLGSGNsVRLNFG 120
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
132-243 2.18e-20

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 87.40  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    132 KHYYEVSCH--DQGLCRVGWSTMQASLDLGTDKFGFG-----FGGTGKKSHNKQFDNYGEE-FTMHDTIGCYLDIDKGHV 203
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESgswgyDGWTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4826686    204 KFSKNGKDLGLAFEIPPHMKnqALFPACVL-KNAELKFNFG 243
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPFAG--PLFPAVSLgAGEGLKFNFG 119
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-62 5.89e-18

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 86.74  E-value: 5.89e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686    1 MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ 62
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
3-72 3.38e-12

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 69.88  E-value: 3.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     3 AFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ 76
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
26-72 6.25e-11

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: 61.49  E-value: 6.25e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 4826686     26 TDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ 47
DEXDc smart00487
DEAD-like helicases superfamily;
17-71 8.58e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 53.26  E-value: 8.58e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686      17 VEEMDWLLPTDIQAESIPLIL-GGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQ 71
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEALKRGKGGR 56
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
284-625 1.18e-94

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 300.53  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  284 PNAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:COG0513  69 PRAPQALILAPTRELALQVAEELRKLAKYLG---LRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSG 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  364 VRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVDLKGEDSVPDTVhh 443
Cdd:COG0513 146 VETLVLDEADRMLDMGFIEDIERILKLLP------KERQTLLFSATMPP-EIRKLAKRYLKNPVRIEVAPENATAETI-- 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  444 vvvpvnpkTDRLWErlgkshirtddVHAKDntrpganspemwseaikilKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLE 523
Cdd:COG0513 217 --------EQRYYL-----------VDKRD-------------------KLELLRRLLRDEDPERAIVFCNTKRGADRLA 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:COG0513 259 EKLQKRG---------ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRI 329
                       330       340
                ....*....|....*....|..
gi 4826686  604 GRVGRAERMGLAISLVaTEKEK 625
Cdd:COG0513 330 GRTGRAGAEGTAISLV-TPDER 350
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
288-430 3.80e-90

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: 280.75  E-value: 3.80e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFL 367
Cdd:cd17938  62 VALILEPSRELAEQTYNCIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFF 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  368 VLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVD 430
Cdd:cd17938 142 VLDEADRLLSQGNLETINRIYNRIPKITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWVD 204
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
93-245 1.82e-82

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 258.66  E-value: 1.82e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   93 MNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLM-KGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTG 171
Cdd:cd12873   1 MNPYDRDAALAISPDGLLCQSREEKGWQGCRATKGVKgKGKYYYEVTVTDEGLCRVGWSTEDASLDLGTDKFGFGYGGTG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  172 KKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEE 245
Cdd:cd12873  81 KKSHGRQFDDYGEPFGLGDVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRNSALFPAVCLKNAEVEFNFGDK 154
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
286-620 1.18e-54

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 194.63  E-value: 1.18e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   286 APKALIVEPSRELAEQTLNNIKQFKKYIDNPKLreLLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:PRK11776  72 RVQALVLCPTRELADQVAKEIRRLARFIPNIKV--LTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALN 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   366 FLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATlhsF--DVKKLSEKIMHFPTWVDLkgeDSVPDtvhh 443
Cdd:PRK11776 150 TLVLDEADRMLDMGFQDAIDAIIRQAP------ARRQTLLFSAT---YpeGIAAISQRFQRDPVEVKV---ESTHD---- 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   444 vvvpvnpktdrlwerlgKSHIRTDDVHAKDNTRpganspemwSEAIKILkgeyavraIKEHKMDQAIIFCRTKIDCDNLE 523
Cdd:PRK11776 214 -----------------LPAIEQRFYEVSPDER---------LPALQRL--------LLHHQPESCVVFCNTKKECQEVA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:PRK11776 260 DALNAQG---------FSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330
                        330
                 ....*....|....*..
gi 4826686   604 GRVGRAERMGLAISLVA 620
Cdd:PRK11776 331 GRTGRAGSKGLALSLVA 347
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
288-626 1.41e-53

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 191.95  E-value: 1.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   288 KALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFL 367
Cdd:PRK10590  77 RALILTPTRELAAQIGENVRDYSKYLN---IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEIL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   368 VLDEADGLLSQGYSDFINRMHNQIPqvtsdGKRlQVIVCSATLhSFDVKKLSEKIMHFPTWVDLKgedsvpdtvhhvvvp 447
Cdd:PRK10590 154 VLDEADRMLDMGFIHDIRRVLAKLP-----AKR-QNLLFSATF-SDDIKALAEKLLHNPLEIEVA--------------- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   448 vnpktdrlwERLGKSHIRTDDVHAKDNTRpganspemwseaikilKGEYAVRAIKEHKMDQAIIFCRTKIDCDNL-EQYf 526
Cdd:PRK10590 212 ---------RRNTASEQVTQHVHFVDKKR----------------KRELLSQMIGKGNWQQVLVFTRTKHGANHLaEQL- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   527 iqqgggpDKKGhqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRV 606
Cdd:PRK10590 266 -------NKDG--IRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRT 336
                        330       340
                 ....*....|....*....|
gi 4826686   607 GRAERMGLAISLVATEKEKV 626
Cdd:PRK10590 337 GRAAATGEALSLVCVDEHKL 356
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
498-619 9.96e-49

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: 167.68  E-value: 9.96e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  498 VRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAAR 577
Cdd:cd18787  19 LLLLEKLKPGKAIIFVNTKKRVDRLAELLEELG---------IKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAAR 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4826686  578 GIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLV 619
Cdd:cd18787  90 GLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
284-619 7.57e-46

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 169.74  E-value: 7.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   284 PNAPKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:PRK11192  71 SGPPRILILTPTRELAMQVADQARELAKHT---HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   364 VRFLVLDEADGLLSQGYSDFINRMHNQIPQvtsdgkRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSvpdtvhh 443
Cdd:PRK11192 148 VETLILDEADRMLDMGFAQDIETIAAETRW------RKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRR------- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   444 vvvpvnpktdrlwERlGKSH---IRTDDVHAKdntrpganspemwseaIKILKgeyavRAIKEHKMDQAIIFCRTKIDCD 520
Cdd:PRK11192 215 -------------ER-KKIHqwyYRADDLEHK----------------TALLC-----HLLKQPEVTRSIVFVRTRERVH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   521 NLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYV 600
Cdd:PRK11192 260 ELAGWLRKAG---------INCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYL 330
                        330
                 ....*....|....*....
gi 4826686   601 HRIGRVGRAERMGLAISLV 619
Cdd:PRK11192 331 HRIGRTGRAGRKGTAISLV 349
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
279-430 8.53e-43

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: 153.75  E-value: 8.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  279 QTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYidnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGK 358
Cdd:cd00268  55 EPKKKGRGPQALVLAPTRELAMQIAEVARKLGKG---TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686  359 LNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLhSFDVKKLSEKIMHFPTWVD 430
Cdd:cd00268 132 LDLSNVKYLVLDEADRMLDMGFEEDVEKILSALP------KDRQTLLFSATL-PEEVKELAKKFLKNPVRIE 196
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
287-617 2.20e-42

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 160.85  E-value: 2.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   287 PKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLE-NGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:PRK01297 163 PRALIIAPTRELVVQIAKDAAALTKYTG---LNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   366 FLVLDEADGLLSQGysdFINRMHNQIPQVTSDGKRlQVIVCSATLhSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVhhvv 445
Cdd:PRK01297 240 VMVLDEADRMLDMG---FIPQVRQIIRQTPRKEER-QTLLFSATF-TDDVMNLAKQWTTDPAIVEIEPENVASDTV---- 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   446 vpvnpktdrlwerlgKSHIRTddVHAKDNTRPGANspemwseaikilkgeyavrAIKEHKMDQAIIFCRTKIDCDNLEQY 525
Cdd:PRK01297 311 ---------------EQHVYA--VAGSDKYKLLYN-------------------LVTQNPWERVMVFANRKDEVRRIEER 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   526 FIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGR 605
Cdd:PRK01297 355 LVKDG---------INAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGR 425
                        330
                 ....*....|..
gi 4826686   606 VGRAERMGLAIS 617
Cdd:PRK01297 426 TGRAGASGVSIS 437
PTZ00424 PTZ00424
helicase 45; Provisional
285-645 1.02e-41

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 156.91  E-value: 1.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   285 NAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:PTZ00424  95 NACQALILAPTRELAQQIQKVVLALGDYLK---VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDL 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   365 RFLVLDEADGLLSQGYSDFINRMHNQIPQvtsdgkRLQVIVCSATLHSfDVKKLSEKIMHFPTWVdlkgedsvpdtvhhv 444
Cdd:PTZ00424 172 KLFILDEADEMLSRGFKGQIYDVFKKLPP------DVQVALFSATMPN-EILELTTKFMRDPKRI--------------- 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   445 vvpvNPKTDRL-WERLGKSHIRTDDVHAKDNTrpganspemwseaikiLKGEYAVRAIKehkmdQAIIFCRTKIDCDNLE 523
Cdd:PTZ00424 230 ----LVKKDELtLEGIRQFYVAVEKEEWKFDT----------------LCDLYETLTIT-----QAIIYCNTRRKVDYLT 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   524 QYFIQQgggpdkkghQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:PTZ00424 285 KKMHER---------DFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRI 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 4826686   604 GRVGRAERMGLAISLVATEKEkvwyhVCSSRGKGCYNTRLKE 645
Cdd:PTZ00424 356 GRSGRFGRKGVAINFVTPDDI-----EQLKEIERHYNTQIEE 392
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
284-618 1.60e-41

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 157.06  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   284 PNAPKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:PRK04837  81 VNQPRALIMAPTRELAVQIHADAEPLAQAT---GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   364 VRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSdgkRLQVIVcSATLhSFDVKKLSEKIMHFPTWVDLKGEDsvpdtvhh 443
Cdd:PRK04837 158 IQVVVLDEADRMFDLGFIKDIRWLFRRMPPANQ---RLNMLF-SATL-SYRVRELAFEHMNNPEYVEVEPEQ-------- 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   444 vvvpvnpKTD-RLWERLgkshirtddvhakdntrpgaNSPEMwSEAIKILkgeyaVRAIKEHKMDQAIIFCRTKIDCDNL 522
Cdd:PRK04837 225 -------KTGhRIKEEL--------------------FYPSN-EEKMRLL-----QTLIEEEWPDRAIIFANTKHRCEEI 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   523 EQYFiqqgggpDKKGHQFSCvcLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHR 602
Cdd:PRK04837 272 WGHL-------AADGHRVGL--LTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHR 342
                        330
                 ....*....|....*.
gi 4826686   603 IGRVGRAERMGLAISL 618
Cdd:PRK04837 343 IGRTGRAGASGHSISL 358
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
4-64 1.43e-39

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: 144.77  E-value: 1.43e-39
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV 61
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
286-619 3.96e-39

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 153.85  E-value: 3.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   286 APKALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:PRK11634  74 APQILVLAPTRELAVQVAEAMTDFSKHM--RGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   366 FLVLDEADGLLSQGYSDFINRMHNQIPQvtsdgkRLQVIVCSATLHSfDVKKLSEKIMHFPTWVDLkgEDSVpdtvhhvv 445
Cdd:PRK11634 152 GLVLDEADEMLRMGFIEDVETIMAQIPE------GHQTALFSATMPE-AIRRITRRFMKEPQEVRI--QSSV-------- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   446 vpvnpktdrlwerlgkshirtddvhakdNTRPGAnSPEMWSeAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQY 525
Cdd:PRK11634 215 ----------------------------TTRPDI-SQSYWT-VWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEA 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   526 FIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGR 605
Cdd:PRK11634 265 LERNG---------YNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGR 335
                        330
                 ....*....|....
gi 4826686   606 VGRAERMGLAISLV 619
Cdd:PRK11634 336 TGRAGRAGRALLFV 349
PTZ00110 PTZ00110
helicase; Provisional
287-626 2.74e-38

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 150.31  E-value: 2.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   287 PKALIVEPSRELAEQTLNNIKQFKKyidNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:PTZ00110 204 PIVLVLAPTRELAEQIREQCNKFGA---SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTY 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   367 LVLDEADGLLSQGYSDFINRMHNQI-PQvtsdgkrLQVIVCSATLHSfDVKKLSEkimhfptwvDLKGEDSVpdtvhhvv 445
Cdd:PTZ00110 281 LVLDEADRMLDMGFEPQIRKIVSQIrPD-------RQTLMWSATWPK-EVQSLAR---------DLCKEEPV-------- 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   446 vpvnpktdrlwerlgksHIRTD--DVHAKDNTRPGANSPEmwsEAIKILKGEYAVRAIKEHKmDQAIIFCRTKIDCDNLE 523
Cdd:PTZ00110 336 -----------------HVNVGslDLTACHNIKQEVFVVE---EHEKRGKLKMLLQRIMRDG-DKILIFVETKKGADFLT 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   524 QYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRI 603
Cdd:PTZ00110 395 KELRLDG---------WPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
                        330       340
                 ....*....|....*....|...
gi 4826686   604 GRVGRAERMGLAISLVATEKEKV 626
Cdd:PTZ00110 466 GRTGRAGAKGASYTFLTPDKYRL 488
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
284-618 6.68e-32

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 131.23  E-value: 6.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   284 PNAPKALIVEPSRELAEQTLNNIKQFKKyidNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKL-NLS 362
Cdd:PRK04537  82 PEDPRALILAPTRELAIQIHKDAVKFGA---DLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLH 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   363 QVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDgkrlQVIVCSATLhSFDVKKLSEKIMHFPtwvdlkgEDSVPDTVH 442
Cdd:PRK04537 159 ACEICVLDEADRMFDLGFIKDIRFLLRRMPERGTR----QTLLFSATL-SHRVLELAYEHMNEP-------EKLVVETET 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   443 HVvvpvnpkTDRLWERLgksHIRTDDvhakdntrpganspemwsEAIKILKGeyavrAIKEHKMDQAIIFCRTKIDCDNL 522
Cdd:PRK04537 227 IT-------AARVRQRI---YFPADE------------------EKQTLLLG-----LLSRSEGARTMVFVNTKAFVERV 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   523 EQYFiqqgggpDKKGHQFSCvcLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHR 602
Cdd:PRK04537 274 ARTL-------ERHGYRVGV--LSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHR 344
                        330
                 ....*....|....*.
gi 4826686   603 IGRVGRAERMGLAISL 618
Cdd:PRK04537 345 IGRTARLGEEGDAISF 360
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
493-609 1.01e-31

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: 119.24  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    493 KGEYAVRAIKEHKMDQAIIFCRTKIDCDnlEQYFIQQGGgpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICT 572
Cdd:pfam00271   2 KLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG--------IKVARLHGDLSQEEREEILEDFRKGKIDVLVAT 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 4826686    573 DVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRA 609
Cdd:pfam00271  72 DVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRA 108
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
119-246 1.69e-29

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 115.38  E-value: 1.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  119 WHGCRATKGLMKGKHYYEV-------------SCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEE 185
Cdd:cd12884  33 WAGARATYGVTKGKVCFEVkvtenlpvkhlptEETDPHVVRVGWSVDSSSLQLGEEEFSYGYGSTGKKSTNCKFEDYGEP 112
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  186 FTMHDTIGCYLDIDKGHVK--FSKNGKDLGLAFEIPPH-MKNQALFPACVLKNAELKFNFGEEE 246
Cdd:cd12884 113 FGENDVIGCYLDFESEPVEisFSKNGKDLGVAFKISKEeLGGKALFPHVLTKNCAVEVNFGQKE 176
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
287-622 4.17e-28

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 119.12  E-value: 4.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   287 PKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:PLN00206 197 PLAMVLTPTRELCVQVEDQAKVLGKGL---PFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSV 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   367 LVLDEADGLLSQGYSDfinrmhnQIPQVTSDGKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVDlkgedsvpdtvhhvvv 446
Cdd:PLN00206 274 LVLDEVDCMLERGFRD-------QVMQIFQALSQPQVLLFSATVSP-EVEKFASSLAKDIILIS---------------- 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   447 pvnpktdrlwerLGKSHIRTDDVHakdntrpganSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYF 526
Cdd:PLN00206 330 ------------IGNPNRPNKAVK----------QLAIWVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAI 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   527 IQQGGgpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRV 606
Cdd:PLN00206 388 TVVTG--------LKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRA 459
                        330
                 ....*....|....*.
gi 4826686   607 GRAERMGLAISLVATE 622
Cdd:PLN00206 460 SRMGEKGTAIVFVNEE 475
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
281-418 5.49e-28

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: 110.41  E-value: 5.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    281 KFLPNAPKALIVEPSRELAEQTLNNikqFKKYIDNPKLRELLIIGGVAARDQLSVLEnGVDIVVGTPGRLDDLVSTGKLn 360
Cdd:pfam00270  40 DKLDNGPQALVLAPTRELAEQIYEE---LKKLGKGLGLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL- 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686    361 LSQVRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKL 418
Cdd:pfam00270 115 LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP------KKRQILLLSATLPR-NLEDL 165
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
287-384 4.28e-27

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: 109.35  E-value: 4.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIDN---PKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:cd17951  67 PYGLIVCPSRELARQTHEVIEYYCKALQEggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDI 146
                        90       100
                ....*....|....*....|.
gi 4826686  364 VRFLVLDEADGLLSQGYSDFI 384
Cdd:cd17951 147 CRYLCLDEADRMIDMGFEEDI 167
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
287-410 8.87e-27

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: 108.73  E-value: 8.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNnikQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd17967  79 PSALILAPTRELAIQIYE---EARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4826686  367 LVLDEADGLLSQGYSDFINRM--HNQIPQVtsdGKRlQVIVCSATL 410
Cdd:cd17967 156 LVLDEADRMLDMGFEPQIRKIveHPDMPPK---GER-QTLMFSATF 197
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
279-431 6.47e-26

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: 105.74  E-value: 6.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  279 QTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIdNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGK 358
Cdd:cd17961  61 AESGEEQGTRALILVPTRELAQQVSKVLEQLTAYC-RKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGS 139
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  359 L-NLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLhSFDVKKLSEKIMHFPTWVDL 431
Cdd:cd17961 140 LlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLP------KNYQTFLMSATL-SEDVEALKKLVLHNPAILKL 206
DEXDc smart00487
DEAD-like helicases superfamily;
285-430 1.84e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 1.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     285 NAPKALIVEPSRELAEQTLNnikQFKKYIDNPKLRELLIIGGVAARDQLSVLENGV-DIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:smart00487  53 KGGRVLVLVPTRELAEQWAE---ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSN 129
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826686     364 VRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVD 430
Cdd:smart00487 130 VDLVILDEAHRLLDGGFGDQLEKLLKLLP------KNVQLLLLSATPPE-EIENLLELFLNDPVFID 189
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
279-392 2.58e-24

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: 101.11  E-value: 2.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  279 QTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDnPKLRELLIIGGVAA-RDQLSVLENGVDIVVGTPGRLDDLVS-- 355
Cdd:cd17960  56 KANLKKGQVGALIISPTRELATQIYEVLQSFLEHHL-PKLKCQLLIGGTNVeEDVKKFKRNGPNILVGTPGRLEELLSrk 134
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4826686  356 TGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIP 392
Cdd:cd17960 135 ADKVKVKSLEVLVLDEADRLLDLGFEADLNRILSKLP 171
HELICc smart00490
helicase superfamily c-terminal domain;
536-609 3.03e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.90  E-value: 3.03e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686     536 KGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRA 609
Cdd:smart00490   8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
285-427 4.84e-24

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: 100.48  E-value: 4.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd17939  64 RETQALVLAPTRELAQQIQKVVKALGDYM---GVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKI 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  365 RFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLhSFDVKKLSEKIMHFPT 427
Cdd:cd17939 141 KMFVLDEADEMLSRGFKDQIYDIFQFLP------PETQVVLFSATM-PHEVLEVTKKFMRDPV 196
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
288-410 1.08e-23

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: 99.69  E-value: 1.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFL 367
Cdd:cd17959  73 RALILSPTRELALQTLKVTKELGKFTD---LRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYV 149
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4826686  368 VLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATL 410
Cdd:cd17959 150 VFDEADRLFEMGFAEQLHEILSRLP------ENRQTLLFSATL 186
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
287-421 1.30e-23

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: 100.01  E-value: 1.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKL---NLSQ 363
Cdd:cd17946  69 LRALILTPTRELAVQVKDHLKAIAKYTN---IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKS 145
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686  364 VRFLVLDEADGLLSQGYS-------DFINRMHnqipqvTSDGKRLQVIVCSATL---HSFDVKKLSEK 421
Cdd:cd17946 146 LRFLVLDEADRMLEKGHFaelekilELLNKDR------AGKKRKRQTFVFSATLtldHQLPLKLNSKK 207
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
287-409 5.51e-23

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: 99.27  E-value: 5.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKkyiDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd18052 121 PQALIVAPTRELANQIFLEARKFS---YGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKY 197
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQiPQVTSDGKRlQVIVCSAT 409
Cdd:cd18052 198 LILDEADRMLDMGFGPEIRKLVSE-PGMPSKEDR-QTLMFSAT 238
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
285-426 9.11e-23

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: 96.75  E-value: 9.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd18046  66 KATQALVLAPTRELAQQIQKVVMALGDYMG---IKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYI 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686  365 RFLVLDEADGLLSQGYSDFINRMHNQIPQVTsdgkrlQVIVCSATLHSfDVKKLSEKIMHFP 426
Cdd:cd18046 143 KMFVLDEADEMLSRGFKDQIYDIFQKLPPDT------QVVLLSATMPN-DVLEVTTKFMRDP 197
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
289-426 1.17e-22

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: 96.21  E-value: 1.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  289 ALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLV 368
Cdd:cd17940  70 ALILVPTRELALQTSQVCKELGKHM---GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLV 146
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686  369 LDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSFdVKKLSEKIMHFP 426
Cdd:cd17940 147 LDEADKLLSQDFQPIIEKILNFLP------KERQILLFSATFPLT-VKNFMDRHMHNP 197
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
287-391 2.71e-22

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: 95.13  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLnniKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd17966  64 PIVLVLAPTRELAQQIQ---QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTY 140
                        90       100
                ....*....|....*....|....*
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQI 391
Cdd:cd17966 141 LVLDEADRMLDMGFEPQIRKIVDQI 165
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
287-426 5.38e-22

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: 94.19  E-value: 5.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNnikQFKKYIDNPKLRELLIIGGVAAR-DQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:cd17957  61 LRALILAPTRELASQIYR---ELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVE 137
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  366 FLVLDEADGLLSQGysdFInrmhNQIPQVTS--DGKRLQVIVCSATLhSFDVKKLSEKIMHFP 426
Cdd:cd17957 138 YLVLDEADKLFEPG---FR----EQTDEILAacTNPNLQRSLFSATI-PSEVEELARSVMKDP 192
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
287-429 7.92e-22

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: 93.87  E-value: 7.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLeNGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd17943  59 PQVLILAPTREIAVQIHDVFKKIGKKL--EGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRL 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSFDVKKLSeKIMHFPTWV 429
Cdd:cd17943 136 FVLDEADKLMEGSFQKDVNWIFSSLP------KNKQVIAFSATYPKNLDNLLA-RYMRKPVLV 191
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
289-430 8.53e-22

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: 94.19  E-value: 8.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  289 ALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRL-DDLVSTGKLNLSQVRFL 367
Cdd:cd17949  68 ALVLVPTRELALQIYEVLEKLLKPF--HWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLlDHLKNTQSFDVSNLRWL 145
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  368 VLDEADGLLSQGY----SDFINRMHNQIPQV---TSDGKRLQVIVCSATLHSfDVKKLSEKIMHFPTWVD 430
Cdd:cd17949 146 VLDEADRLLDMGFekdiTKILELLDDKRSKAggeKSKPSRRQTVLVSATLTD-GVKRLAGLSLKDPVYID 214
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
287-426 2.24e-21

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: 92.53  E-value: 2.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd18045  68 TQALILSPTRELAVQIQKVLLALGDYMN---VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKM 144
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQIPQVTsdgkrlQVIVCSATLhSFDVKKLSEKIMHFP 426
Cdd:cd18045 145 LVLDEADEMLNKGFKEQIYDVYRYLPPAT------QVVLVSATL-PQDILEMTNKFMTDP 197
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
130-243 2.40e-21

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 90.05  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     130 KGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFG-----FGGTGKKSHNKQFDNYGEEFTMH-DTIGCYLDIDKGHV 203
Cdd:smart00449   1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFALLGEDKgswgyDGDGGKKYHNSTGPEYGLPLQEPgDVIGCFLDLEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4826686     204 KFSKNGKDL-GLAFEippHMK-NQALFPACVLKNAE-LKFNFG 243
Cdd:smart00449  81 SFYKNGKYLhGLAFF---DVKfSGPLYPAFSLGSGNsVRLNFG 120
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
288-423 2.47e-21

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: 93.03  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLEN-GVDIVVGTPGRLDDLVST--GKLNLSQV 364
Cdd:cd17964  70 SALIISPTRELALQIAAEAKKLLQGL--RKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENpgVAKAFTDL 147
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686  365 RFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGkrLQVIVCSATLhSFDVKKLSEKIM 423
Cdd:cd17964 148 DYLVLDEADRLLDMGFRPDLEQILRHLPEKNADP--RQTLLFSATV-PDEVQQIARLTL 203
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
288-426 3.51e-21

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: 93.08  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLnniKQFKKYIDNPKLRELLIIGGVAARD---QLSV-----LENGVDIVVGTPGRL-DDLVSTGK 358
Cdd:cd17956  70 RALIVVPTKELVQQVY---KVFESLCKGTGLKVVSLSGQKSFKKeqkLLLVdtsgrYLSRVDILVATPGRLvDHLNSTPG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  359 LNLSQVRFLVLDEADGLLSQGYSDF-------INRMHNQIPQVTSDG-------KRLQVIVCSATLhSFDVKKLSEKIMH 424
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFQDWletvmkaLGRPTAPDLGSFGDAnllersvRPLQKLLFSATL-TRDPEKLSSLKLH 225

                ..
gi 4826686  425 FP 426
Cdd:cd17956 226 RP 227
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
132-243 2.18e-20

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 87.40  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    132 KHYYEVSCH--DQGLCRVGWSTMQASLDLGTDKFGFG-----FGGTGKKSHNKQFDNYGEE-FTMHDTIGCYLDIDKGHV 203
Cdd:pfam00622   1 RHYFEVEIFgqDGGGWRVGWATKSVPRKGERFLGDESgswgyDGWTGKKYWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4826686    204 KFSKNGKDLGLAFEIPPHMKnqALFPACVL-KNAELKFNFG 243
Cdd:pfam00622  81 SFTKNGKSLGYAFRDVPFAG--PLFPAVSLgAGEGLKFNFG 119
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
287-426 5.22e-20

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: 89.36  E-value: 5.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVST--GKL-NLSQ 363
Cdd:cd17953  86 PIGLIMAPTRELALQIYVECKKFSKALG---LRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnnGRVtNLRR 162
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686  364 VRFLVLDEADGLLSQGYSDFINRMHNQI-PQvtsdgkrLQVIVCSATLHSfDVKKLSEKIMHFP 426
Cdd:cd17953 163 VTYVVLDEADRMFDMGFEPQIMKIVNNIrPD-------RQTVLFSATFPR-KVEALARKVLHKP 218
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
287-392 6.06e-20

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: 88.92  E-value: 6.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQtlnnI-KQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:cd17945  67 PYALILAPTRELAQQ----IeEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCT 142
                        90       100
                ....*....|....*....|....*..
gi 4826686  366 FLVLDEADGLLSQGYSDFINRMHNQIP 392
Cdd:cd17945 143 YVVLDEADRMIDMGFEPQVTKILDAMP 169
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
286-426 1.46e-19

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: 87.22  E-value: 1.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  286 APKALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:cd17962  58 NPSALILTPTRELAVQIEDQAKELMKGL--PPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIK 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686  366 FLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLhSFDVKKLSEKIMHFP 426
Cdd:cd17962 136 IVVVDEADTMLKMGFQQQVLDILENIS------HDHQTILVSATI-PRGIEQLAGQLLQNP 189
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
284-426 1.88e-19

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: 87.28  E-value: 1.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  284 PNAPKALIVEPSRELAEQTLNnikQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTG---KLN 360
Cdd:cd17955  65 PYGIFALVLTPTRELAYQIAE---QFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKV 141
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686  361 LSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQvtsdgKRlQVIVCSATLHSFdVKKLSEKIMHFP 426
Cdd:cd17955 142 LSRVKFLVLDEADRLLTGSFEDDLATILSALPP-----KR-QTLLFSATLTDA-LKALKELFGNKP 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
285-423 1.95e-19

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: 86.86  E-value: 1.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKQFKKYidnPKLRELLIIGGVAARDQLSVLENgvdIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd17963  63 KSPQALCLAPTRELARQIGEVVEKMGKF---TGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKI 136
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  365 RFLVLDEADGLL-SQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLSEKIM 423
Cdd:cd17963 137 KILVLDEADVMLdTQGHGDQSIRIKRMLP------RNCQILLFSATFPD-SVRKFAEKIA 189
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
131-241 2.18e-19

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 84.40  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  131 GKHYYEVSCHDQ--GLCRVGWSTMQASLDLGTDKFGFGF-----GGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHV 203
Cdd:cd11709   1 GKWYWEVRVDSGngGLIQVGWATKSFSLDGEGGVGDDEEswgydGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEGTL 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4826686  204 KFSKNGKDLGLAFEIPPHmKNQALFPACVL-KNAELKFN 241
Cdd:cd11709  81 SFSLNGKDLGVAFTNLFL-KGGGLYPAVSLgSGQGVTIN 118
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
286-382 2.44e-19

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: 86.83  E-value: 2.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  286 APKALIVEPSRELAEQTLNNIKQFKKyidnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVR 365
Cdd:cd17944  64 APKVLVLAPTRELANQVTKDFKDITR-----KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLK 138
                        90
                ....*....|....*..
gi 4826686  366 FLVLDEADGLLSQGYSD 382
Cdd:cd17944 139 HVVLDEVDQMLDMGFAE 155
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
4-62 2.57e-19

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: 86.99  E-value: 2.57e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQ 60
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
287-426 2.82e-19

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: 86.70  E-value: 2.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd17952  64 PIAVIVAPTRELAQQIYLEAKKFGKAY---NLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTY 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  367 LVLDEADGLLSQGysdFINRMHNQIPQVTSDGkrlQVIVCSATLHSfDVKKLSEKIMHFP 426
Cdd:cd17952 141 LVLDEADRMFDMG---FEYQVRSIVGHVRPDR---QTLLFSATFKK-KIEQLARDILSDP 193
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
285-410 1.36e-18

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: 85.50  E-value: 1.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd17948  64 NAPRGLVITPSRELAEQIGSVAQSLTEGLG---LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQL 140
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4826686  365 RFLVLDEADGLLSQGY----SDFINRMHNQIPQVTSDGKR---LQVIVCSATL 410
Cdd:cd17948 141 RHLVLDEADTLLDDSFneklSHFLRRFPLASRRSENTDGLdpgTQLVLVSATM 193
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
288-419 2.11e-18

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: 83.84  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLENGVDIVVGTPGRL-DDLVSTGKLNLSQVRF 366
Cdd:cd17947  63 RVLVLVPTRELAMQCFSVLQQLAQFTD---ITFALAVGGLSLKAQEAALRARPDIVIATPGRLiDHLRNSPSFDLDSIEI 139
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKLS 419
Cdd:cd17947 140 LVLDEADRMLEEGFADELKEILRLCP------RTRQTMLFSATMTD-EVKDLA 185
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
279-427 5.13e-18

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: 83.16  E-value: 5.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  279 QTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIdnPKLRELLIIGGVAARDQLSVLENGV-DIVVGTPGRLDDLVSTG 357
Cdd:cd17950  63 QLEPVDGQVSVLVICHTRELAFQISNEYERFSKYM--PNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREK 140
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  358 KLNLSQVRFLVLDEADGLLSQgysdfINrMHNQIPQV---TSDGKrlQVIVCSATLhSFDVKKLSEKIMHFPT 427
Cdd:cd17950 141 KLKLSHVKHFVLDECDKMLEQ-----LD-MRRDVQEIfraTPHDK--QVMMFSATL-SKEIRPVCKKFMQDPL 204
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-62 5.89e-18

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 86.74  E-value: 5.89e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686    1 MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:COG0513   1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQ 62
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
13-74 7.44e-18

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: 82.49  E-value: 7.44e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEG 74
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG 62
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
285-429 1.51e-17

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: 81.36  E-value: 1.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKqfkKYIDNpKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd17958  63 NGPGVLVLTPTRELALQIEAECS---KYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSI 138
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686  365 RFLVLDEADGLLSQGYSdfinrmhNQIPQVTSDGK-RLQVIVCSATLHSfDVKKLSEKIMHFPTWV 429
Cdd:cd17958 139 TYLVLDEADRMLDMGFE-------PQIRKILLDIRpDRQTIMTSATWPD-GVRRLAQSYLKDPMIV 196
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
285-423 2.03e-17

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: 81.98  E-value: 2.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQtlnnIKQFK-KYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:cd18049  96 DGPICLVLAPTRELAQQ----VQQVAaEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRR 171
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686  364 VRFLVLDEADGLLSQGYSDFINRMHNQI-PQvtsdgkrLQVIVCSATLHSfDVKKLSEKIM 423
Cdd:cd18049 172 CTYLVLDEADRMLDMGFEPQIRKIVDQIrPD-------RQTLMWSATWPK-EVRQLAEDFL 224
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
287-409 3.76e-17

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: 81.62  E-value: 3.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFKkYidNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd18051 106 PLALVLAPTRELASQIYDEARKFA-Y--RSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKY 182
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4826686  367 LVLDEADGLLSQGYSDFINRMHNQ--IPQVtsdGKRlQVIVCSAT 409
Cdd:cd18051 183 LVLDEADRMLDMGFEPQIRRIVEQdtMPPT---GER-QTLMFSAT 223
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
285-423 2.87e-16

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: 79.67  E-value: 2.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  285 NAPKALIVEPSRELAEQTLNNIKQFKKyidNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQV 364
Cdd:cd18050 134 DGPICLVLAPTRELAQQVQQVADDYGK---SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRC 210
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  365 RFLVLDEADGLLSQGYSDFINRMHNQI-PQvtsdgkrLQVIVCSATLHSfDVKKLSEKIM 423
Cdd:cd18050 211 TYLVLDEADRMLDMGFEPQIRKIVDQIrPD-------RQTLMWSATWPK-EVRQLAEDFL 262
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
289-429 4.73e-16

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: 77.33  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  289 ALIVEPSRELAEQTLNNIKQFKKYIDnpkLRELLIIGGVAARDQLSVLeNGVDIVVGTPGR-LDDLVSTGKLNLSQVRFL 367
Cdd:cd17941  65 ALIISPTRELAMQIFEVLRKVGKYHS---FSAGLIIGGKDVKEEKERI-NRMNILVCTPGRlLQHMDETPGFDTSNLQML 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686  368 VLDEADGLLSQGYSDFINRMHNQIPQvtsdgKRlQVIVCSATLhSFDVKKLSEKIMHFPTWV 429
Cdd:cd17941 141 VLDEADRILDMGFKETLDAIVENLPK-----SR-QTLLFSATQ-TKSVKDLARLSLKNPEYI 195
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
277-409 7.54e-16

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: 76.63  E-value: 7.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  277 VTQTKFLP-NAPKALIVEPSRELAEQTLNNIKQFKKYidnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGR-LDDLV 354
Cdd:cd17942  52 LYKLKFKPrNGTGVIIISPTRELALQIYGVAKELLKY---HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRlLDHLQ 128
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4826686  355 STGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSAT 409
Cdd:cd17942 129 NTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLLP------KRRQTMLFSAT 177
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
11-76 7.80e-16

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: 76.85  E-value: 7.80e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686   11 PEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQivyETLKDQQEGKK 76
Cdd:cd17961   3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQ---KILKAKAESGE 65
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
289-418 1.23e-15

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: 76.20  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  289 ALIVEPSRELAEQTlnnIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRL-DDLVSTGKLNLSQVRFL 367
Cdd:cd17954  71 ALVLAPTRELAQQI---SEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLvDHLENTKGFSLKSLKFL 147
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4826686  368 VLDEADGLLSQGYSDFINRMHNQIPqvtsdgKRLQVIVCSATLHSfDVKKL 418
Cdd:cd17954 148 VMDEADRLLNMDFEPEIDKILKVIP------RERTTYLFSATMTT-KVAKL 191
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
286-427 2.22e-14

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: 73.56  E-value: 2.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  286 APKALIVEPSRELAEQTLNNIKQFKKYIdnpKLRELLIIGGVAARDQLSVL--ENGVDIVVGTPGRLDDLVSTGKLNLSQ 363
Cdd:cd17965 109 RPRSVILVPTHELVEQVYSVLKKLSHTV---KLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPGKLASLAKSRPKILSR 185
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686  364 VRFLVLDEADGLLSQGYsdfinrmhnqIPQVTSDGKRL----QVIVCSATL-HSFDvKKLSEKimhFPT 427
Cdd:cd17965 186 VTHLVVDEADTLFDRSF----------LQDTTSIIKRApklkHLILCSATIpKEFD-KTLRKL---FPD 240
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
283-606 8.16e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 74.68  E-value: 8.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  283 LPNAPKALIVEPSRELAEQTLNNIKQFkkyidnpklreLLIIGGVAARDqlsvlENGVDIVVGTpgrLDDLVSTGKLNLS 362
Cdd:COG1061 124 LLRGKRVLVLVPRRELLEQWAEELRRF-----------LGDPLAGGGKK-----DSDAPITVAT---YQSLARRAHLDEL 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  363 QVRF--LVLDEADGLLSQGYSDFINRMHNQI-------PqVTSDGKRLQVIVCSATLHSFDVKKLSE-----KIMHFPTW 428
Cdd:COG1061 185 GDRFglVIIDEAHHAGAPSYRRILEAFPAAYrlgltatP-FRSDGREILLFLFDGIVYEYSLKEAIEdgylaPPEYYGIR 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  429 VDLKGEDSVPDTVhhvvvpvnpkTDRLWERLgkshirtddvhAKDNTRpganspemwseAIKILKgEYAVRAIKEHKmdq 508
Cdd:COG1061 264 VDLTDERAEYDAL----------SERLREAL-----------AADAER-----------KDKILR-ELLREHPDDRK--- 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  509 AIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVI 588
Cdd:COG1061 308 TLVFCSSVDHAEALAELLNEAG---------IRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
                       330
                ....*....|....*...
gi 4826686  589 NVTLPDEKQNYVHRIGRV 606
Cdd:COG1061 379 LLRPTGSPREFIQRLGRG 396
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
104-247 1.94e-13

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 68.31  E-value: 1.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  104 IGSDGLCCQSRevKEWHGCRATKGLMKGKHYYEV-----SCHDQGLCRVGWSTMQASL--------------DLGTDKFg 164
Cdd:cd12872   3 LSEDRLTVTGE--KGYRMARANHGVREGKWYFEVkilegGGTETGHVRVGWSRREASLqapvgydkysyairDKDGSKF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  165 fgfggtgkksHNKQFDNYGE-EFTMHDTIGCYLDIdkGHVKFSKNGKDLGLAFE-IPPhmkNQALFPACVL-KNAELKFN 241
Cdd:cd12872  80 ----------HQSRGKPYGEpGFKEGDVIGFLITL--PKIEFFKNGKSQGVAFEdIYG---TGGYYPAVSLyKGATVTIN 144

                ....*.
gi 4826686  242 FGEEEF 247
Cdd:cd12872 145 FGPDFK 150
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
4-62 6.18e-13

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: 68.49  E-value: 6.18e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17959   3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIE 61
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
4-66 1.77e-12

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: 66.86  E-value: 1.77e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYE 66
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSE 63
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
13-62 2.35e-12

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: 66.46  E-value: 2.35e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17957   1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQ 50
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
3-72 3.38e-12

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 69.88  E-value: 3.38e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     3 AFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQ 76
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
16-65 3.83e-12

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: 65.84  E-value: 3.83e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4826686   16 AVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVY 65
Cdd:cd17942   4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLY 53
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
13-82 5.11e-12

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: 66.11  E-value: 5.11e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGG-DVLMAAETGSGKTGAFSIPVIqivyETLKDQQEGKKGKTTIK 82
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPIL----ERLLSQKSSNGVGGKQK 67
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
4-62 9.69e-12

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 67.66  E-value: 9.69e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686     4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQ 61
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
4-72 1.35e-11

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: 64.24  E-value: 1.35e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ 69
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
3-82 1.35e-11

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 67.53  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686     3 AFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIvyetLKDQQEGKKGKTTIK 82
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH----LITRQPHAKGRRPVR 77
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
1-62 1.36e-11

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 67.52  E-value: 1.36e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826686     1 MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:PRK11776   3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQ 64
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
4-62 2.81e-11

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: 63.66  E-value: 2.81e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDvLMA-AETGSGKTGAFSIPVIQ 62
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRD-LMAcAQTGSGKTAAFLLPIIS 60
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
123-243 3.29e-11

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 61.19  E-value: 3.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  123 RATKGLMKGKHYYEVSCHDQGLCRVGWSTMQ----ASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDI 198
Cdd:cd12882   3 RANACVYKGKWMYEVTLGTKGIMQIGWATIScrftQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDL 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4826686  199 DKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAE-LKFNFG 243
Cdd:cd12882  83 DKGTISFYRNGRSLGVAFDNVRRGPGLAYFPAVSLSFGErLELNFG 128
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
13-65 3.97e-11

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: 62.69  E-value: 3.97e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVY 65
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY 53
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
282-409 5.52e-11

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 61.27  E-value: 5.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  282 FLPNAPKALIVEPSRELAEQTLNNIKQFKKyidnPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRL-DDLVSTGKLN 360
Cdd:cd00046  26 LLKKGKKVLVLVPTKALALQTAERLRELFG----PGIRVAVLVGGSSAEEREKNKLGDADIIIATPDMLlNLLLREDRLF 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4826686  361 LSQVRFLVLDEADGLLsqGYSDFINRMHNQIpqVTSDGKRLQVIVCSAT 409
Cdd:cd00046 102 LKDLKLIIVDEAHALL--IDSRGALILDLAV--RKAGLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
26-72 6.25e-11

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: 61.49  E-value: 6.25e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 4826686     26 TDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ 47
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
16-62 9.56e-11

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: 61.89  E-value: 9.56e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4826686   16 AVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17947   4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILE 50
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
502-608 1.44e-10

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: 59.53  E-value: 1.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  502 KEHKMDQAIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDI 581
Cdd:cd18794  26 VEHLGGSGIIYCLSRKECEQVAARLQSKG---------ISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDK 96
                        90       100
                ....*....|....*....|....*..
gi 4826686  582 HGVPYVINVTLPDEKQNYVHRIGRVGR 608
Cdd:cd18794  97 PDVRFVIHYSLPKSMESYYQESGRAGR 123
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
25-63 1.71e-10

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: 61.45  E-value: 1.71e-10
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4826686   25 PTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQI 63
Cdd:cd17949  14 PTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQR 52
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
13-62 2.23e-10

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: 61.23  E-value: 2.23e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17948   1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQ 50
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
13-74 5.00e-10

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: 60.03  E-value: 5.00e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYE----TLKDQQEG 74
Cdd:cd17945   1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEETKDDG 66
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
13-77 7.23e-10

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: 59.13  E-value: 7.23e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVyetLKDQQEGKKG 77
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIL---LKRKANLKKG 62
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
3-62 2.74e-09

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: 58.83  E-value: 2.74e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    3 AFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd18052  44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLT 103
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
258-435 5.19e-09

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: 57.34  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  258 LSKAPDGYIVKSQhSGN--------AQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAA 329
Cdd:cd18048  53 LADPPQNLIAQSQ-SGTgktaafvlAMLSRVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  330 RDQLSVlengvDIVVGTPGRLDDLVSTGKL-NLSQVRFLVLDEADGLLS-QGYSDFINRMHNQIPqvtsdgKRLQVIVCS 407
Cdd:cd18048 132 GTDIEA-----QIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMINvQGHSDHSVRVKRSMP------KECQMLLFS 200
                       170       180
                ....*....|....*....|....*...
gi 4826686  408 ATLHSfDVKKLSEKIMHFPTWVDLKGED 435
Cdd:cd18048 201 ATFED-SVWAFAERIVPDPNIIKLKKEE 227
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
175-243 7.36e-09

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 54.59  E-value: 7.36e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686  175 HNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHmknQALFP--ACVLKNAELKFNFG 243
Cdd:cd12885  65 GGGEGENYGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVK---GRLYPtvGLGSPGVKVRVNFG 132
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
498-608 8.91e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 58.61  E-value: 8.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  498 VRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTdVA-A 576
Cdd:COG0514 222 LDFLKEHPGGSGIVYCLSRKKVEELAEWLREAG---------IRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfG 291
                        90       100       110
                ....*....|....*....|....*....|..
gi 4826686  577 RGIDIHGVPYVINVTLPDEKQNYVHRIGRVGR 608
Cdd:COG0514 292 MGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
493-613 2.14e-08

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: 53.25  E-value: 2.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  493 KGEYAVRAIKEHKM--DQAIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGDRKPHERKQNLERFKK--GDVRF 568
Cdd:cd18793  12 KLEALLELLEELREpgEKVLIFSQFTDTLDILEEALRERG---------IKYLRLDGSTSSKERQKLVDRFNEdpDIRVF 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4826686  569 LICTDVAARGIDIHGVPYVINVTLP----DEKQnyvhrigRVGRAERMG 613
Cdd:cd18793  83 LLSTKAGGVGLNLTAANRVILYDPWwnpaVEEQ-------AIDRAHRIG 124
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
13-81 3.83e-08

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: 53.96  E-value: 3.83e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYetlkDQQEGKKGKTTI 81
Cdd:cd17952   1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM----DQRELEKGEGPI 65
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
4-61 3.92e-08

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 56.72  E-value: 3.92e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686     4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVI 61
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPII 180
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
4-66 4.06e-08

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: 55.05  E-value: 4.06e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYE 66
Cdd:cd18051  23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYE 85
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
4-81 5.81e-08

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: 53.92  E-value: 5.81e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVyetlKDQQEGKKGKTTI 81
Cdd:cd17953  14 WSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI----KDQRPVKPGEGPI 87
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
479-613 5.89e-08

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 56.39  E-value: 5.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  479 ANSPEMWSEAIKIL-----KGEYAVRAIKE-----HKmdqAIIFCRTKIDCDNLEQYFIQQGggpdkkghqFSCVCLHGD 548
Cdd:COG0553 515 CSHPALLLEEGAELsgrsaKLEALLELLEEllaegEK---VLVFSQFTDTLDLLEERLEERG---------IEYAYLHGG 582
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4826686  549 RKPHERKQNLERFKKGD--VRFLICTDVAARGIDIHGVPYVINVTLPD----EKQnyvhrigRVGRAERMG 613
Cdd:COG0553 583 TSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWnpavEEQ-------AIDRAHRIG 646
DEXDc smart00487
DEAD-like helicases superfamily;
17-71 8.58e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 53.26  E-value: 8.58e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686      17 VEEMDWLLPTDIQAESIPLIL-GGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQ 71
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEALKRGKGGR 56
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
4-56 2.77e-07

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 53.44  E-value: 2.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4826686     4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAF 56
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF 62
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
11-75 3.35e-07

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: 51.43  E-value: 3.35e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686   11 PEIAQAVEEMDWLLPTDIQAESIPLILGGG-DVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGK 75
Cdd:cd17964   3 PSLLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG 68
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
24-61 7.76e-07

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: 50.24  E-value: 7.76e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4826686   24 LPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVI 61
Cdd:cd17962  12 VPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI 49
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
481-620 9.27e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 52.42  E-value: 9.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  481 SPEMwSEAIKILKGEyavraIKEHKMDQAIIFCRTKIDCDNLEQY----------FIQQGGGPDKKGhqfscvclhgdRK 550
Cdd:COG1111 334 HPKL-SKLREILKEQ-----LGTNPDSRIIVFTQYRDTAEMIVEFlsepgikagrFVGQASKEGDKG-----------LT 396
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686  551 PHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVIN---VtlPDEKQnYVHRIGRVGRAERmGLAISLVA 620
Cdd:COG1111 397 QKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFyepV--PSEIR-SIQRKGRTGRKRE-GRVVVLIA 465
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
568-610 1.09e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 46.93  E-value: 1.09e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4826686  568 FLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAE 610
Cdd:cd18785  25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
4-72 2.19e-06

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: 49.00  E-value: 2.19e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQ 69
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
182-244 2.21e-06

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 47.90  E-value: 2.21e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4826686  182 YGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKnqaLFPACVLK--NAELKFNFGE 244
Cdd:cd12909  83 YGPTFTTGDVIGCGINFRDNTAFYTKNGVNLGIAFRDIKKGN---LYPTVGLRtpGEHVEANFGQ 144
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
489-610 3.22e-06

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: 47.20  E-value: 3.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  489 IKILKGEYAVRAIKehkmdQAIIFCRTKIDCDNLE---------------QYFIQQGGGPDKKghqfscvclhgdRKPHE 553
Cdd:cd18802  13 IEILREYFPKTPDF-----RGIIFVERRATAVVLSrllkehpstlafircGFLIGRGNSSQRK------------RSLMT 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  554 RKQN---LERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRvGRAE 610
Cdd:cd18802  76 QRKQketLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAP 134
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
4-62 3.31e-06

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: 48.50  E-value: 3.31e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQ 62
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
190-243 5.86e-06

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 46.19  E-value: 5.86e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4826686  190 DTIGCYLDIDKGHVKFSKNGKDLGLAFEiPPHMKNQALFPACVLKNAE-LKFNFG 243
Cdd:cd12883  68 DVLGCLLDLNKKQMIFSLNGNRLPPERQ-VFTSAKSGFFAAASFMSFQqCEFNFG 121
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
485-622 6.86e-06

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: 49.45  E-value: 6.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  485 WSEAIKILKgeyavRAIKEHKmdQAIIFCR--------TKIdcdnLEQYFIQQGGGPDKKGHqfscvclHGDRKPHERKQ 556
Cdd:COG1205 274 LAEAARLLA-----DLVREGL--RTLVFTRsrrgaellARY----ARRALREPDLADRVAAY-------RAGYLPEERRE 335
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4826686  557 nLER-FKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAIsLVATE 622
Cdd:COG1205 336 -IERgLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGD 400
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
13-74 8.77e-06

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: 47.07  E-value: 8.77e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686   13 IAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIP-VIQIVYE-TLKDQQEG 74
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQpIPREQRNG 64
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
9-61 1.22e-05

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: 46.59  E-value: 1.22e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4826686    9 VMPEIAqaveEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVI 61
Cdd:cd17966   1 VMDELK----RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI 49
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
28-64 1.58e-05

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: 46.86  E-value: 1.58e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 4826686   28 IQAESIPLILGG---------GDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd17956  16 VQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL 61
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
25-64 2.72e-05

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: 45.72  E-value: 2.72e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4826686   25 PTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd17943  13 PSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL 52
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
175-217 3.37e-05

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 45.23  E-value: 3.37e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 4826686  175 HNKQFDNYGEEFTMHDT-IGCYLDIDKGHVKFSKNGKDLGLAFE 217
Cdd:cd12876 100 HDGQSRPYTSPFGNQGTiIGVHLDMWRGTLTFYKNGKPLGVAFT 143
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
11-66 4.10e-05

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 47.14  E-value: 4.10e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686   11 PEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYE 66
Cdd:COG1205  43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE 98
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
4-61 4.17e-05

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: 45.77  E-value: 4.17e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVI 61
Cdd:cd18049  26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 83
SPRY_SOCS_Fbox cd12875
SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family ...
94-232 5.78e-05

SPRY domain in Fbxo45 and suppressors of cytokine signaling (SOCS) proteins; This family consists of the SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) as well as F-box protein 45 (Fbxo45), a novel synaptic E3 and ubiquitin ligase. The SPSB protein is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. SPSB1, SPSB2, and SPSB4 interact with prostate apoptosis response protein 4 (Par-4) and are negative regulators that recruit the ECS E3 ubiquitin ligase complex to polyubiquitinate inducible nitric-oxide synthase (iNOS), resulting in its proteasomal degradation. Fbxo45 is related to this family; it is located N-terminal to the SPRY domain, and known to induce the degradation of a synaptic vesicle-priming factor, Munc13-1, via the SPRY domain, thus playing an important role in the regulation of neurotransmission by modulating Munc13-1 at the synapse. Suppressor of cytokine signaling (SOCS) proteins negatively regulate signaling from JAK-associated cytokine receptor complexes, and play key roles in the regulation of immune homeostasis.


Pssm-ID: 293935  Cd Length: 169  Bit Score: 44.37  E-value: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   94 NPYDRGSAFAIGSDGLCCQSREV-KEWHGCRATKGLMKGKHYYEVSC---------------HDQGLCRVGWSTMQAS-- 155
Cdd:cd12875   4 NPADCSKNIYIKEDGLTFHRRPVaQSTDAIRGKKGYTRGLHAWEVKWisrprgshavvgvatKDAPLQCDGYVTLLGSns 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  156 ----LDLGTDKFGFGFGGTgkkshNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEippHMKNQALFPAC 231
Cdd:cd12875  84 eswgWDLGDNKLYHNGKKV-----IGSYPAKSENYQVPDRILVILDMEDGTLAFEANGEYLGVAFR---GLPGKLLYPAV 155

                .
gi 4826686  232 V 232
Cdd:cd12875 156 S 156
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
130-243 9.65e-05

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 42.67  E-value: 9.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  130 KGKHYYEVSCHDQGLCRVGWS--TMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSK 207
Cdd:cd12878  13 SGKWYFEFEVLTSGYMRVGWArpGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCMLDLVDRTISFTL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4826686  208 NGK----DLG--LAFE-IPphmKNQALFPACVLKNAEL-KFNFG 243
Cdd:cd12878  93 NGEllidSSGseVAFKdIE---IGEGFVPACSLGVGQKgRLNLG 133
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
25-72 1.06e-04

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: 43.85  E-value: 1.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4826686   25 PTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:cd17939  20 PSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ 67
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
192-231 1.19e-04

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs.


Pssm-ID: 293937  Cd Length: 151  Bit Score: 43.06  E-value: 1.19e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4826686  192 IGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKnqaLFPAC 231
Cdd:cd12879 100 IGCLIDTATGLLTFTANGKETSTRFQVEPGTK---LFPAV 136
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
4-72 1.28e-04

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: 43.59  E-value: 1.28e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQ 69
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
11-72 1.43e-04

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: 43.33  E-value: 1.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826686   11 PEIAQAVEEMDWLLPTDIQAESIPLILGGGDV-LMA-AETGSGKTGAFSIPVIQIVYETLKDQQ 72
Cdd:cd17963   3 PELLKGLYAMGFNKPSKIQETALPLILSDPPEnLIAqSQSGTGKTAAFVLAMLSRVDPTLKSPQ 66
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
29-62 1.59e-04

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: 42.96  E-value: 1.59e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 4826686   29 QAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQ 62
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILE 38
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
22-53 1.98e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 44.71  E-value: 1.98e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 4826686   22 WLLPTDIQAESIPLILGGGDVLMAAETGSGKT 53
Cdd:COG1201  22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKT 53
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
25-61 2.47e-04

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: 43.46  E-value: 2.47e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4826686   25 PTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVI 61
Cdd:cd18050  85 PTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAI 121
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
287-386 4.32e-04

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 41.14  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  287 PKALIVEPSRELAEQTLNNIKQFkkyidNPKlRELLIIGGVAARDQlsvleNGVDIVVGTPGRLDDLVSTGKLNLSQVRF 366
Cdd:cd17926  45 LRTLIVVPTDALLDQWKERFEDF-----LGD-SSIGLIGGGKKKDF-----DDANVVVATYQSLSNLAEEEKDLFDQFGL 113
                        90       100
                ....*....|....*....|
gi 4826686  367 LVLDEADGLLSQGYSDFINR 386
Cdd:cd17926 114 LIVDEAHHLPAKTFSEILKE 133
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
27-79 6.51e-04

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: 41.76  E-value: 6.51e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4826686   27 DIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYEtlkDQQEGKKGKT 79
Cdd:cd17944  15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQE---DQQPRKRGRA 64
PRK13766 PRK13766
Hef nuclease; Provisional
552-641 8.70e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.94  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686   552 HERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVI---NVtlPDEKQNyVHRIGRVGRAeRMGLAISLVA--TEKEKv 626
Cdd:PRK13766 410 KEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIfyePV--PSEIRS-IQRKGRTGRQ-EEGRVVVLIAkgTRDEA- 484
                         90
                 ....*....|....*
gi 4826686   627 WYHVCSSRGKGCYNT 641
Cdd:PRK13766 485 YYWSSRRKEKKMKEE 499
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
551-620 8.71e-04

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 40.32  E-value: 8.71e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  551 PHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAIsLVA 620
Cdd:cd18797  78 AEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI-LVA 146
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
476-608 8.71e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 42.96  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686    476 RPGANSPEMWSEAIKILKG--EYAVRAIKEHKMDQ-AIIFCRTKIDCDNLEQYFiqqgggpDKKGHQfsCVCLHGDRKPH 552
Cdd:PLN03137  647 RQSFNRPNLWYSVVPKTKKclEDIDKFIKENHFDEcGIIYCLSRMDCEKVAERL-------QEFGHK--AAFYHGSMDPA 717
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4826686    553 ERKQNLERFKKGDVRfLICTDVA-ARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGR 608
Cdd:PLN03137  718 QRAFVQKQWSKDEIN-IICATVAfGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGR 773
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
553-608 1.22e-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: 40.03  E-value: 1.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4826686  553 ERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGR 608
Cdd:cd18801  78 EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SPRY_HERC1 cd12881
SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to ...
186-233 1.81e-03

SPRY domain in HERC1; This SPRY domain is found in the HERC1, a large protein related to chromosome condensation regulator RCC1. It is widely expressed in many tissues, playing an important role in intracellular membrane trafficking in the cytoplasm as well as Golgi apparatus. HERC1 also interacts with tuberous sclerosis 2 (TSC2, tuberin), which suppresses cell growth, and results in the destabilization of TSC2. However, the biological function of HERC1 has yet to be defined.


Pssm-ID: 293939  Cd Length: 162  Bit Score: 39.64  E-value: 1.81e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 4826686  186 FTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFE-IPPHmknqALFPaCVL 233
Cdd:cd12881 104 FHQGDYITVVLDMEEGTLSFGKNGEEPGVAFEdVDAT----ELYP-CVM 147
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
4-64 2.64e-03

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: 39.70  E-value: 2.64e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4826686    4 FSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGG--GDVLMAAETGSGKTGAFSIPVIQIV 64
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV 65
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
501-611 3.25e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.77  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  501 IKEHKM-DQAIIFCrtkidcDNLEQ----------YFIqqgggpdkkghqfscvclHGDRKPHERKQNLERFKKGDVRFL 569
Cdd:cd18789  43 LKRHEQgDKIIVFT------DNVEAlyryakrllkPFI------------------TGETPQSEREEILQNFREGEYNTL 98
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4826686  570 ICTDVAARGIDI--HGVPYVINVTLPDEKQnYVHRIGRVGRAER 611
Cdd:cd18789  99 VVSKVGDEGIDLpeANVAIQISGHGGSRRQ-EAQRLGRILRPKK 141
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
288-372 5.99e-03

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 38.65  E-value: 5.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826686  288 KALIVEPSRELAEQTLNNIKQFKKYIDnpklrELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFL 367
Cdd:cd18035  47 KVLILAPSRPLVEQHAENLKRVLNIPD-----KITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLL 121

                ....*
gi 4826686  368 VLDEA 372
Cdd:cd18035 122 IFDEA 126
 
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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