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Conserved domains on  [gi|311908065|gb|ADQ18506|]
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DEAD/DEAH box helicase domain protein [Leadbetterella byssophila DSM 17132]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-408 0e+00

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 512.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKsKSLRCLVMVPT 80
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP-RAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  81 HELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDL 160
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 161 GFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLERMITENP 240
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 241 QQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPD 320
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 321 VAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELEYQETLIFSNESSRTFKDVMKEIADFES 400
Cdd:COG0513  321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400

                 ....*...
gi 311908065 401 NTKKRKKK 408
Cdd:COG0513  401 RPGPKGER 408
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-408 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 512.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKsKSLRCLVMVPT 80
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP-RAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  81 HELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDL 160
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 161 GFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLERMITENP 240
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 241 QQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPD 320
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 321 VAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELEYQETLIFSNESSRTFKDVMKEIADFES 400
Cdd:COG0513  321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400

                 ....*...
gi 311908065 401 NTKKRKKK 408
Cdd:COG0513  401 RPGPKGER 408
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
1-360 7.57e-108

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 325.22  E-value: 7.57e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASE----KKSKSLRCLV 76
Cdd:PRK10590   1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphaKGRRPVRALI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  77 MVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADR 156
Cdd:PRK10590  81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 157 MLDLGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLERMI 236
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 237 TENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINY 316
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 311908065 317 DLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYL 360
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL 364
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
12-205 4.56e-93

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: 277.79  E-value: 4.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEK--KSKSLRCLVMVPTHELAQQIAD 89
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  90 VFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDV 169
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 311908065 170 KKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
25-193 1.13e-56

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 183.60  E-value: 1.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   25 TDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLKIMA 104
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL--DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  105 LYGSTDQEPQIKALqKGVDVLVTTPGRMFDLQAQGHLsLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPKRHQTLFFSA 184
Cdd:pfam00270  79 LLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 311908065  185 TLDEKIKKL 193
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
16-218 6.23e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.98  E-value: 6.23e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065    16 IADLGYKKPTDIQYKVLPKVLAGE-DIMGIAQTGTGKTAAFAIPVLHLLaseKKSKSLRCLVMVPTHELAQQIADVFKSL 94
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL---KRGKGGRVLVLVPTRELAEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065    95 AKNTRLKIMALYGSTDQEPQIKALQKGV-DVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRI 173
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 311908065   174 PKRHQTLFFSATLDEKIKKLAYSTVKNAIRiqISPDDPVSKNIDH 218
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVF--IDVGFTPLEPIEQ 200
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
241-313 1.88e-03

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 40.36  E-value: 1.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311908065  241 QQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYV 313
Cdd:TIGR00631 442 NERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 514
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1-408 0e+00

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 512.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKsKSLRCLVMVPT 80
Cdd:COG0513    2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP-RAPQALILAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  81 HELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDL 160
Cdd:COG0513   81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 161 GFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLERMITENP 240
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 241 QQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPD 320
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 321 VAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELEYQETLIFSNESSRTFKDVMKEIADFES 400
Cdd:COG0513  321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400

                 ....*...
gi 311908065 401 NTKKRKKK 408
Cdd:COG0513  401 RPGPKGER 408
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
1-360 7.57e-108

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 325.22  E-value: 7.57e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASE----KKSKSLRCLV 76
Cdd:PRK10590   1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphaKGRRPVRALI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  77 MVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADR 156
Cdd:PRK10590  81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 157 MLDLGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLERMI 236
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 237 TENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINY 316
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 311908065 317 DLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYL 360
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL 364
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
2-364 2.96e-102

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 309.59  E-value: 2.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   2 KFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLAS-----EKKSKSLRCLV 76
Cdd:PRK04837   9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLShpapeDRKVNQPRALI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  77 MVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADR 156
Cdd:PRK04837  89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 157 MLDLGFYQDIIDVKKRIPKRHQ--TLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLER 234
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 235 MITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVI 314
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 311908065 315 NYDLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTI 364
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
1-408 1.46e-95

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 293.00  E-value: 1.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL-HLLA-SEKKSKSLRCLVMV 78
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALqHLLDfPRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  79 PTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRML 158
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 159 DLGFYQDIidvkKRIPK----RHQTLFFSATLD-EKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMV-SMEDKRFFL 232
Cdd:PRK11192 161 DMGFAQDI----ETIAAetrwRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRAdDLEHKTALL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 233 ERMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEY 312
Cdd:PRK11192 237 CHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSH 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 313 VINYDLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELEYQetlifSNESSR--TFKD 390
Cdd:PRK11192 317 VINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPK-----TKAPSEkkTGKP 391
                        410
                 ....*....|....*...
gi 311908065 391 VMKEIADFESNTKKRKKK 408
Cdd:PRK11192 392 SKKVLAKRAEKKEKEKEK 409
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
19-373 3.51e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 290.16  E-value: 3.51e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  19 LGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasekKSKSLRC--LVMVPTHELAQQIADVFKSLAK 96
Cdd:PRK11776  22 LGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL----DVKRFRVqaLVLCPTRELADQVAKEIRRLAR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  97 NTR-LKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPK 175
Cdd:PRK11776  98 FIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 176 RHQTLFFSATLDEKIKKLAYSTVKNAIRIQI--SPDDPvskNIDHSVVMVSMEDKRFFLERMITENPQQKIIVFVRTKVR 253
Cdd:PRK11776 178 RRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLP---AIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKE 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 254 AERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPDVAENYVHRIGRTG 333
Cdd:PRK11776 255 CQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 311908065 334 RGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELE 373
Cdd:PRK11776 335 RAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLS 374
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
12-205 4.56e-93

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: 277.79  E-value: 4.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEK--KSKSLRCLVMVPTHELAQQIAD 89
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkKGRGPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  90 VFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDV 169
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 311908065 170 KKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
2-368 6.16e-90

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 279.87  E-value: 6.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   2 KFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLL-----ASEKKSKSLRCLV 76
Cdd:PRK01297  88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMGEPRALI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  77 MVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQ-KGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEAD 155
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 156 RMLDLGFYQDIIDVKKRIPKR--HQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFLE 233
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 234 RMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYV 313
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311908065 314 INYDLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQT 368
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEM 462
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
11-373 5.83e-88

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 279.04  E-value: 5.83e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  11 EIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLrcLVMVPTHELAQQIADV 90
Cdd:PRK11634  16 PILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQI--LVLAPTRELAVQVAEA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  91 FKSLAKNTR-LKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDV 169
Cdd:PRK11634  94 MTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 170 KKRIPKRHQTLFFSATLDEKIKKLAYSTVKNA--IRIQIS----PDdpvsknIDHSVVMVSMEDKRFFLERMITENPQQK 243
Cdd:PRK11634 174 MAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRIQSSvttrPD------ISQSYWTVWGMRKNEALVRFLEAEDFDA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 244 IIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPDVAE 323
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 311908065 324 NYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTLSELE 373
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-372 1.60e-80

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 258.34  E-value: 1.60e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLAS-----EKKSKSLRCL 75
Cdd:PRK04537   9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpalaDRKPEDPRAL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  76 VMVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHL-SLEDIKFLILDEA 154
Cdd:PRK04537  89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 155 DRMLDLGFYQDIIDVKKRIPKR--HQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRFFL 232
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 233 ERMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEY 312
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311908065 313 VINYDLPDVAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDYLGYTIASQTL-SEL 372
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVtAEL 389
PTZ00110 PTZ00110
helicase; Provisional
3-344 3.93e-80

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 256.62  E-value: 3.93e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYrILPEIKRAiadlGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIP-VLHLLASE--KKSKSLRCLVMVP 79
Cdd:PTZ00110 137 FPDY-ILKSLKNA----GFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPllRYGDGPIVLVLAP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  80 THELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLD 159
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLD 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 160 LGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKN-AIRIQI-SPDDPVSKNIDHSVVMVSMEDKR----FFLE 233
Cdd:PTZ00110 292 MGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRgklkMLLQ 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 234 RMITENPqqKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYV 313
Cdd:PTZ00110 372 RIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
                        330       340       350
                 ....*....|....*....|....*....|.
gi 311908065 314 INYDLPDVAENYVHRIGRTGRGTQKGKAVSF 344
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTF 480
PTZ00424 PTZ00424
helicase 45; Provisional
3-359 1.14e-72

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 232.79  E-value: 1.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHE 82
Cdd:PTZ00424  30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--DYDLNACQALILAPTRE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:PTZ00424 108 LAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKRF--FLERMITENP 240
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFdtLCDLYETLTI 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 241 QQKIIvFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPD 320
Cdd:PTZ00424 268 TQAII-YCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 311908065 321 VAENYVHRIGRTGRGTQKGKAVSFCSDEELPLLESIEDY 359
Cdd:PTZ00424 347 SPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH 385
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
3-205 4.92e-61

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: 196.00  E-value: 4.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKksKSLRCLVMVPTHE 82
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP--QRFFALVLAPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDEADRMLDLG 161
Cdd:cd17954   80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRLLNMD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 311908065 162 FYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd17954  160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
14-205 8.69e-60

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: 192.85  E-value: 8.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  14 RAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLH-LLASEKKSKSLRCLVMVPTHELAQQIADVFK 92
Cdd:cd17947    3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILErLLYRPKKKAATRVLVLVPTRELAMQCFSVLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  93 SLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGH-LSLEDIKFLILDEADRMLDLGFYQDIIDVKK 171
Cdd:cd17947   83 QLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEILR 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 311908065 172 RIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd17947  163 LCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
1-348 2.52e-59

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 201.17  E-value: 2.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLH---LLASEKKSKSLRCLVM 77
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNPLAM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  78 V--PTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEAD 155
Cdd:PLN00206 201 VltPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 156 RMLDLGFYQDIIDVKKRIPKRhQTLFFSATLDEKIKKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSMEDKR--FFLE 233
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKqkLFDI 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 234 RMITENPQQKIIVFVRTKVRAERVAAAMARVN-IKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEY 312
Cdd:PLN00206 360 LKSKQHFKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 311908065 313 VINYDLPDVAENYVHRIGRTGRGTQKGKAVSFCSDE 348
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
12-194 2.93e-59

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: 192.32  E-value: 2.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAiadlGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLR--------CLVMVPTHEL 83
Cdd:cd17967   15 IKRA----GYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRgrrkaypsALILAPTREL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  84 AQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFY 163
Cdd:cd17967   91 AIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFE 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 311908065 164 QDIidvkKRI------PKR--HQTLFFSATLDEKIKKLA 194
Cdd:cd17967  171 PQI----RKIvehpdmPPKgeRQTLMFSATFPREIQRLA 205
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
25-193 1.13e-56

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 183.60  E-value: 1.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   25 TDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLKIMA 104
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL--DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  105 LYGSTDQEPQIKALqKGVDVLVTTPGRMFDLQAQGHLsLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPKRHQTLFFSA 184
Cdd:pfam00270  79 LLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 311908065  185 TLDEKIKKL 193
Cdd:pfam00270 157 TLPRNLEDL 165
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
16-205 5.01e-55

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: 180.26  E-value: 5.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  16 IADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL-HLLASE--KKSKSLRCLVMVPTHELAQQIADVFK 92
Cdd:cd17966    5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvHINAQPplERGDGPIVLVLAPTRELAQQIQQEAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  93 SLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKR 172
Cdd:cd17966   85 KFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQ 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 311908065 173 IPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd17966  165 IRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
216-345 2.96e-54

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: 176.16  E-value: 2.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 216 IDHSVVMVSMEDKRFFL-ERMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWV 294
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 311908065 295 LIATDVSARGVDIPLVEYVINYDLPDVAENYVHRIGRTGRGTQKGKAVSFC 345
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
3-205 2.66e-53

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: 176.34  E-value: 2.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLRCLVMVPTHE 82
Cdd:cd17959    3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd17959   83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGF 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd17959  163 AEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
16-206 8.10e-53

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: 174.70  E-value: 8.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  16 IADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLRCLVMVPTHELAQQIADVFKSLA 95
Cdd:cd17957    5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  96 KNTRLKIMALYGST-DQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRIP 174
Cdd:cd17957   85 KGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 311908065 175 -KRHQTLFFSATLDEKIKKLAYSTVKNAIRIQI 206
Cdd:cd17957  165 nPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
14-201 9.82e-53

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: 174.72  E-value: 9.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  14 RAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEkkSKSLRCLVMVPTHELAQQIADVFKS 93
Cdd:cd17955   12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED--PYGIFALVLTPTRELAYQIAEQFRA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  94 LAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDL---QAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVK 170
Cdd:cd17955   90 LGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHlrsSDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATIL 169
                        170       180       190
                 ....*....|....*....|....*....|.
gi 311908065 171 KRIPKRHQTLFFSATLDEKIKKLAYSTVKNA 201
Cdd:cd17955  170 SALPPKRQTLLFSATLTDALKALKELFGNKP 200
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
12-188 2.59e-52

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: 174.73  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLA-GEDIMGIAQTGTGKTAAFAIPVLHLLASEKKS-------KSLRCLVMVPTHEL 83
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  84 AQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHL---SLEDIKFLILDEADRMLDL 160
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEK 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 311908065 161 GFYQDIIDVKKRIPKRH-------QTLFFSATLDE 188
Cdd:cd17946  161 GHFAELEKILELLNKDRagkkrkrQTFVFSATLTL 195
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
1-194 4.10e-52

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: 175.16  E-value: 4.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASE-------KKSKSLR 73
Cdd:cd18052   43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfSEVQEPQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  74 CLVMVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDE 153
Cdd:cd18052  123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 311908065 154 ADRMLDLGFYQDIidvKKRI------PK-RHQTLFFSATLDEKIKKLA 194
Cdd:cd18052  203 ADRMLDMGFGPEI---RKLVsepgmpSKeDRQTLMFSATFPEEIQRLA 247
DEXDc smart00487
DEAD-like helicases superfamily;
16-218 6.23e-51

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 169.98  E-value: 6.23e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065    16 IADLGYKKPTDIQYKVLPKVLAGE-DIMGIAQTGTGKTAAFAIPVLHLLaseKKSKSLRCLVMVPTHELAQQIADVFKSL 94
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL---KRGKGGRVLVLVPTRELAEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065    95 AKNTRLKIMALYGSTDQEPQIKALQKGV-DVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRI 173
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 311908065   174 PKRHQTLFFSATLDEKIKKLAYSTVKNAIRiqISPDDPVSKNIDH 218
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVF--IDVGFTPLEPIEQ 200
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
3-194 1.23e-50

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: 169.42  E-value: 1.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasekkskslRCLVMVPTHE 82
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV---------VALILEPSRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAK---NTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLD 159
Cdd:cd17938   72 LAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 160 LGFYQDIIDVKKRIPK------RHQTLFFSATL-DEKIKKLA 194
Cdd:cd17938  152 QGNLETINRIYNRIPKitsdgkRLQVIVCSATLhSFEVKKLA 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
3-204 2.79e-50

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: 168.25  E-value: 2.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSksLRCLVMVPTHE 82
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV--IQALILVPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd17940   79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17940  159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
12-204 1.25e-48

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: 164.00  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKS--LRCLVMVPTHELAQQIAD 89
Cdd:cd17941    1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdgLGALIISPTRELAMQIFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  90 VFKSLAKNTRLKIMALYGSTDQEPQIKALQkGVDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDEADRMLDLGFYQDIID 168
Cdd:cd17941   81 VLRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 311908065 169 VKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17941  160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
12-204 1.74e-48

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: 164.42  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL----HL--LASEKKSKSLRCLVMVPTHELAQ 85
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLvyisRLppLDEETKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  86 QIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQD 165
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 311908065 166 IIDVKKRIP--------------------KRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17945  161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
10-199 3.28e-48

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: 163.14  E-value: 3.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  10 PEIKRAIADLGYKKPTDIQYKVLPKVLA-GEDIMGIAQTGTGKTAAFAIPVLHLLASEK---KSKSLRCLVMVPTHELAQ 85
Cdd:cd17964    3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKpagRRSGVSALIISPTRELAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  86 QIADVFKSLAKN-TRLKIMALYGSTDQEPQIKALQK-GVDVLVTTPGRMFD-LQAQGHL-SLEDIKFLILDEADRMLDLG 161
Cdd:cd17964   83 QIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDhLENPGVAkAFTDLDYLVLDEADRLLDMG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 162 FYQDIIDVKKRIPKRH----QTLFFSATLDEKIKKLAYSTVK 199
Cdd:cd17964  163 FRPDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
15-204 1.03e-47

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: 161.43  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  15 AIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL-HLLASE--KKSKSLRCLVMVPTHELAQQIADVF 91
Cdd:cd17952    4 AIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvHIMDQRelEKGEGPIAVIVAPTRELAQQIYLEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  92 KSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKK 171
Cdd:cd17952   84 KKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVG 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 311908065 172 RIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17952  164 HVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
10-202 8.82e-47

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: 159.29  E-value: 8.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  10 PEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKS----LRCLVMVPTHELAQ 85
Cdd:cd17961    3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGeeqgTRALILVPTRELAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  86 QIADVFKSLAK--NTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd17961   83 QVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSYGY 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAI 202
Cdd:cd17961  163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
15-205 4.50e-46

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: 157.92  E-value: 4.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  15 AIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL-HLLASE--KKSKSLRCLVMVPTHELAQQIADVF 91
Cdd:cd17953   26 LIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrHIKDQRpvKPGEGPIGLIMAPTRELALQIYVEC 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  92 KSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGH---LSLEDIKFLILDEADRMLDLGFYQDIID 168
Cdd:cd17953  106 KKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMGFEPQIMK 185
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 311908065 169 VKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQ 205
Cdd:cd17953  186 IVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
21-202 2.85e-45

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: 156.74  E-value: 2.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  21 YKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLR--------------CLVMVPTHELAQQ 86
Cdd:cd18051   41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPsesgyygrrkqyplALVLAPTRELASQ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  87 IADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDI 166
Cdd:cd18051  121 IYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311908065 167 --IDVKKRIPKR--HQTLFFSATLDEKIKKLAYSTVKNAI 202
Cdd:cd18051  201 rrIVEQDTMPPTgeRQTLMFSATFPKEIQMLARDFLDNYI 240
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
14-204 3.62e-45

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: 154.79  E-value: 3.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  14 RAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSksLRCLVMVPTHELAQQIADVFKS 93
Cdd:cd17939   10 RGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE--TQALVLAPTRELAQQIQKVVKA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  94 LAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRI 173
Cdd:cd17939   88 LGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFL 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 311908065 174 PKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17939  168 PPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
12-194 6.00e-45

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: 154.44  E-value: 6.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEK--KSKSLRCLVMVPTHELAQQIAD 89
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkPRNGTGVIIISPTRELALQIYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  90 VFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDEADRMLDLGFYQDIID 168
Cdd:cd17942   81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                        170       180
                 ....*....|....*....|....*.
gi 311908065 169 VKKRIPKRHQTLFFSATLDEKIKKLA 194
Cdd:cd17942  161 IIKLLPKRRQTMLFSATQTRKVEDLA 186
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
18-204 8.50e-45

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: 154.28  E-value: 8.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  18 DLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASE----KKSKSLRCLVMVPTHELAQQIADVFKS 93
Cdd:cd17949    8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvDRSDGTLALVLVPTRELALQIYEVLEK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  94 LAKNTR-LKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDEADRMLDLGFYQDI----- 166
Cdd:cd17949   88 LLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDItkile 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 311908065 167 -IDVKKRI-------PKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17949  168 lLDDKRSKaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
16-206 5.16e-44

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: 154.40  E-value: 5.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  16 IADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVL----HLLASEKKSKSLrCLVMVPTHELAQQIADVF 91
Cdd:cd18050   77 LLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinHQPYLERGDGPI-CLVLAPTRELAQQVQQVA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  92 KSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKK 171
Cdd:cd18050  156 DDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 235
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 311908065 172 RIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQI 206
Cdd:cd18050  236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
20-204 8.35e-44

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: 151.16  E-value: 8.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  20 GYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSlrCLVMVPTHELAQQIADVFKSLAKNT- 98
Cdd:cd17962    9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS--ALILTPTRELAVQIEDQAKELMKGLp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  99 RLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPKRHQ 178
Cdd:cd17962   87 PMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQ 166
                        170       180
                 ....*....|....*....|....*.
gi 311908065 179 TLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17962  167 TILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
8-204 8.51e-44

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: 151.08  E-value: 8.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   8 ILPEIKRAiadlGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIP-VLHLL---ASEKKSKSLRCLVMVPTHEL 83
Cdd:cd17958    1 IMKEIKKQ----GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDlqpIPREQRNGPGVLVLTPTREL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  84 AQQI-ADVFKSLAKNtrLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd17958   77 ALQIeAECSKYSYKG--LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGF 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17958  155 EPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
12-204 1.54e-43

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: 150.80  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEK---KSKSLRCLVMVPTHELAQQIA 88
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKanlKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  89 DVFKSLAK--NTRLKIMALYGSTDQEPQIKAL-QKGVDVLVTTPGRMFDL--QAQGHLSLEDIKFLILDEADRMLDLGFY 163
Cdd:cd17960   81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 311908065 164 QDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
1-206 1.68e-43

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: 151.70  E-value: 1.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   1 MKFENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIP-VLHLLASE--KKSKSLRCLVM 77
Cdd:cd18049   24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaIVHINHQPflERGDGPICLVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  78 VPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRM 157
Cdd:cd18049  104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 311908065 158 LDLGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRIQI 206
Cdd:cd18049  184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
10-204 1.37e-42

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: 148.11  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  10 PEIKRAIADLGYKKPTDIQYKVLPKVLAG--EDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHELAQQI 87
Cdd:cd17963    3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  88 ADVFKSLAKNTRLKIMALYGSTDQEP--QIKAlqkgvDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDL-GFYQ 164
Cdd:cd17963   81 GEVVEKMGKFTGVKVALAVPGNDVPRgkKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 311908065 165 DIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd17963  156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
12-194 5.27e-41

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: 145.08  E-value: 5.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGE---------DIMGIAQTGTGKTAAFAIPVLHLLaSEKKSKSLRCLVMVPTHE 82
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRLRALIVVPTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKG--------VDVLVTTPGRMFD-LQAQGHLSLEDIKFLILDE 153
Cdd:cd17956   80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311908065 154 ADRMLDLGFYQ--------------------DIIDVKKRIPKRHQTLFFSATLDEKIKKLA 194
Cdd:cd17956  160 ADRLLNQSFQDwletvmkalgrptapdlgsfGDANLLERSVRPLQKLLFSATLTRDPEKLS 220
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
3-204 7.03e-41

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: 143.74  E-value: 7.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHE 82
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKATQALVLAPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd18046   79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd18046  159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
12-197 6.72e-40

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: 141.32  E-value: 6.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  12 IKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIP-VLHLLASEKKSKSLR-----CLVMVPTHELAQ 85
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKLPFIKgegpyGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  86 QIADV----FKSLAKN--TRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLD 159
Cdd:cd17951   81 QTHEVieyyCKALQEGgyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 311908065 160 LGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYST 197
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSA 198
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
3-191 8.39e-40

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: 140.94  E-value: 8.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPTHE 82
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL--EPVDGQVSVLVICHTRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKN-TRLKIMALYGSTDQEPQIKALQKGV-DVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRML-D 159
Cdd:cd17950   82 LAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQ 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 311908065 160 LGFYQDIIDVKKRIPKRHQTLFFSATLDEKIK 191
Cdd:cd17950  162 LDMRRDVQEIFRATPHDKQVMMFSATLSKEIR 193
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
3-204 1.48e-39

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: 140.30  E-value: 1.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHllASEKKSKSLRCLVMVPTHE 82
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLDIQVRETQALILSPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  83 LAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF 162
Cdd:cd18045   79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 163 YQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKNAIRI 204
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
26-194 3.71e-37

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: 133.82  E-value: 3.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  26 DIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASE----KKSKSLRCLVMVPTHELAQQIADVFKSLAKntRLK 101
Cdd:cd17944   15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDqqprKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 102 IMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGF---YQDIIDV--KKRIPKR 176
Cdd:cd17944   93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFaeqVEEILSVsyKKDSEDN 172
                        170
                 ....*....|....*...
gi 311908065 177 HQTLFFSATLDEKIKKLA 194
Cdd:cd17944  173 PQTLLFSATCPDWVYNVA 190
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
14-193 4.31e-33

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: 122.76  E-value: 4.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  14 RAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEkkSKSLRCLVMVPTHELAQQIADVFKS 93
Cdd:cd17943    3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE--RRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  94 LAKN-TRLKIMALYGSTDQEPQIKALqKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKR 172
Cdd:cd17943   81 IGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                        170       180
                 ....*....|....*....|....*
gi 311908065 173 IPKRHQTLFFSAT----LDEKIKKL 193
Cdd:cd17943  160 LPKNKQVIAFSATypknLDNLLARY 184
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
227-334 2.48e-30

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: 112.69  E-value: 2.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  227 DKRFFLERMITENPQQKIIVFVRTKVRAErVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVD 306
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100
                  ....*....|....*....|....*...
gi 311908065  307 IPLVEYVINYDLPDVAENYVHRIGRTGR 334
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
3-204 4.23e-30

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: 116.32  E-value: 4.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIAD---------LGYKKPTDIQYKVLPKVLAG----------------EDIMGIAQTGTGKTAAFAI 57
Cdd:cd17965    1 FDQLKLLPSVREAIIKeilkgsnktDEEIKPSPIQTLAIKKLLKTlmrkvtkqtsneepklEVFLLAAETGSGKTLAYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  58 PVLHLL---------------ASEKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQ--IKALQK 120
Cdd:cd17965   81 PLLDYLkrqeqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQrlQLAFKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 121 GVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKN 200
Cdd:cd17965  161 RIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPD 240

                 ....
gi 311908065 201 AIRI 204
Cdd:cd17965  241 VVRI 244
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
19-174 7.03e-26

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: 104.37  E-value: 7.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  19 LGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSL-----RCLVMVPTHELAQQIADVFKS 93
Cdd:cd17948    8 QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnapRGLVITPSRELAEQIGSVAQS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  94 LAKNTRLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRI 173
Cdd:cd17948   88 LTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRRF 167

                 .
gi 311908065 174 P 174
Cdd:cd17948  168 P 168
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
3-205 1.94e-25

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: 103.18  E-value: 1.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAG--EDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKslRCLVMVPT 80
Cdd:cd18048   20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYP--QCLCLSPT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  81 HELAQQIADVFKSLAKNTrLKIMALYGSTDQEPQiKALQKGVDVLVTTPGRMFDLQAQGHL-SLEDIKFLILDEADRMLD 159
Cdd:cd18048   98 FELALQTGKVVEEMGKFC-VGIQVIYAIRGNRPG-KGTDIEAQIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMIN 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 311908065 160 L-GFYQDIIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTV--KNAIRIQ 205
Cdd:cd18048  176 VqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVpdPNIIKLK 224
HELICc smart00490
helicase superfamily c-terminal domain;
255-334 4.74e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.59  E-value: 4.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   255 ERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPDVAENYVHRIGRTGR 334
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
3-200 4.00e-22

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: 93.25  E-value: 4.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   3 FENYRILPEIKRAIADLGYKKPTDIQYKVLPKVLAG--EDIMGIAQTGTGKTAAFAIPVLHLLasEKKSKSLRCLVMVPT 80
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQCLCLSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  81 HELAQQIADVFKSLAKntrlkimaLYGSTDQEPQIKA--LQKGV----DVLVTTPGRMFDLQAQGHL-SLEDIKFLILDE 153
Cdd:cd18047   81 YELALQTGKVIEQMGK--------FYPELKLAYAVRGnkLERGQkiseQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 311908065 154 ADRMLDLGFYQD-IIDVKKRIPKRHQTLFFSATLDEKIKKLAYSTVKN 200
Cdd:cd18047  153 ADVMIATQGHQDqSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
45-185 3.40e-20

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: 86.30  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  45 AQTGTGKTAAFAIPVLHLLASekksKSLRCLVMVPTHELAQQIADVFKSLAKNTrLKIMALYGSTDQEPQIKALQKGVDV 124
Cdd:cd00046    8 APTGSGKTLAALLAALLLLLK----KGKKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKLGDADI 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311908065 125 LVTTPGRMF-DLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIID--VKKRIPKRHQTLFFSAT 185
Cdd:cd00046   83 IIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
115-354 1.47e-18

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 87.12  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 115 IKALQKG-VDVLVTTP-----GRMFDLQAQGHLSLedikfLILDEA--------DrmldlgF---YQDIIDVKKRIPKRh 177
Cdd:COG0514  100 LRALRAGeLKLLYVAPerllnPRFLELLRRLKISL-----FAIDEAhcisqwghD------FrpdYRRLGELRERLPNV- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 178 QTLFFSATLDEK-----IKKLAystVKNAIRIQISPDDPvskNIDHSVVMVSMEDKRFFLERMITENPQQKIIVFVRTKV 252
Cdd:COG0514  168 PVLALTATATPRvradiAEQLG---LEDPRVFVGSFDRP---NLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 253 RAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATdvSA--RGVDIPLVEYVINYDLPDVAENYVHRIG 330
Cdd:COG0514  242 KVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAfgMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
                        250       260
                 ....*....|....*....|....
gi 311908065 331 RTGRGTQKGKAVSFCSDEELPLLE 354
Cdd:COG0514  320 RAGRDGLPAEALLLYGPEDVAIQR 343
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
47-400 1.46e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.69  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  47 TGTGKT--AAFAIpvlhllasEKKSKSLRCLVMVPTHELAQQIADVFKslakntrlKIMALYGSTDQEPQIKAlqkgvDV 124
Cdd:COG1061  109 TGTGKTvlALALA--------AELLRGKRVLVLVPRRELLEQWAEELR--------RFLGDPLAGGGKKDSDA-----PI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 125 LVTTPGrmfdlQAQGHLSLEDIK----FLILDEADRmLDLGFYQDIID---VKKRI-----PKR----HQTLF------F 182
Cdd:COG1061  168 TVATYQ-----SLARRAHLDELGdrfgLVIIDEAHH-AGAPSYRRILEafpAAYRLgltatPFRsdgrEILLFlfdgivY 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 183 SATLDEKI-----KKLAYSTVKNAIRIQISPDDPVSKNIDHSVVMVSmEDKRFFLERMITENPQQ-KIIVFVRTKVRAER 256
Cdd:COG1061  242 EYSLKEAIedgylAPPEYYGIRVDLTDERAEYDALSERLREALAADA-ERKDKILRELLREHPDDrKTLVFCSSVDHAEA 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 257 VAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVInydLPDVAEN---YVHRIGRTG 333
Cdd:COG1061  321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSpreFIQRLGRGL 397
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311908065 334 RGTQKGKAVSFCS--DEELPLLE----SIEDYLGYTIASQTLSELEYQETLIFSNESSRTFKDVMKEIADFES 400
Cdd:COG1061  398 RPAPGKEDALVYDfvGNDVPVLEelakDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELE 470
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
215-334 1.22e-14

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: 70.32  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 215 NIDHSVVMV-SMEDKRFFLERMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETW 293
Cdd:cd18794    3 NLFYSVRPKdKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQ 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 311908065 294 VLIATDVSARGVDIPLVEYVINYDLPDVAENYVHRIGRTGR 334
Cdd:cd18794   83 VIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
232-342 3.86e-14

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.38  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 232 LERMITENPQQKIIVFVRTKVRAERVAAAMARVNIKTVTL------HSDK--SHIERKAALESFKKGETWVLIATDVSAR 303
Cdd:COG1111  344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERFRAGEFNVLVATSVAEE 423
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 311908065 304 GVDIPLVEYVINYDLPDVAENYVHRIGRTGRGTQkGKAV 342
Cdd:COG1111  424 GLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-GRVV 461
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
10-342 5.41e-14

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 73.72  E-value: 5.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  10 PEIKRAIADLGYKKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSkslRCLVMVPTHELAQ-QIA 88
Cdd:COG1205   43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA---TALYLYPTKALARdQLR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  89 DvFKSLAKNT--RLKIMALYGSTDQEPQIKALQKGvDVLVTTPgrmfD-LqaqgHLSL-----------EDIKFLILDEA 154
Cdd:COG1205  120 R-LRELAEALglGVRVATYDGDTPPEERRWIREHP-DIVLTNP----DmL----HYGLlphhtrwarffRNLRYVVIDEA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 155 ---------------DRMldlgfyqdiidvkKRIPKRH----QTLFFSATLD------EKIKKLAYSTVKN-------AI 202
Cdd:COG1205  190 htyrgvfgshvanvlRRL-------------RRICRHYgsdpQFILASATIGnpaehaERLTGRPVTVVDEdgsprgeRT 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 203 RIQISPdDPVSKNIDHSVVMVSMEdkrfFLERMITENpqQKIIVFVRTKVRAERVAAAMARVNIKtvtlHSDKSHI---- 278
Cdd:COG1205  257 FVLWNP-PLVDDGIRRSALAEAAR----LLADLVREG--LRTLVFTRSRRGAELLARYARRALRE----PDLADRVaayr 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311908065 279 ------ERKAALESFKKGETWVLIATdvSA--RGVDIPLVEYVINYDLPDVAENYVHRIGRTGRGTQKGKAV 342
Cdd:COG1205  326 agylpeERREIERGLRSGELLGVVST--NAleLGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
47-154 9.74e-12

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 63.82  E-value: 9.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  47 TGTGKT--AAFAIPVLHLLASEKKSKSLRCLVMVPTHELAQQIAdvfKSLAKNTRLKIMALYGSTDQEPQIKALQKGV-- 122
Cdd:cd18034   25 TGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQA---EAIRSHTDLKVGEYSGEMGVDKWTKERWKEEle 101
                         90       100       110
                 ....*....|....*....|....*....|....
gi 311908065 123 --DVLVTTPGRMFDLQAQGHLSLEDIKFLILDEA 154
Cdd:cd18034  102 kyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
25-187 1.02e-11

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 63.05  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  25 TDIQYKVLPKVLAGEDIMGI-AQTGTGKTAAFAIPVLHLLASEKKskslRCLVMVPTHELAQQIADVFKSLAKNTRLKIM 103
Cdd:cd17921    3 NPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATSGG----KAVYIAPTRALVNQKEADLRERFGPLGKNVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 104 ALYGstDQEPQIKALQKGvDVLVTTPgRMFD--LQAQGHLSLEDIKFLILDEA------DRMLDLgfyQDIIDVKKRIPK 175
Cdd:cd17921   79 LLTG--DPSVNKLLLAEA-DILVATP-EKLDllLRNGGERLIQDVRLVVVDEAhligdgERGVVL---ELLLSRLLRINK 151
                        170
                 ....*....|..
gi 311908065 176 RHQTLFFSATLD 187
Cdd:cd17921  152 NARFVGLSATLP 163
PRK13766 PRK13766
Hef nuclease; Provisional
238-342 5.88e-11

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 64.51  E-value: 5.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 238 ENPQQKIIVFvrTKVR--AERVAAAMARVNIKTVTL------HSDK--SHIERKAALESFKKGETWVLIATDVSARGVDI 307
Cdd:PRK13766 362 KNPDSRIIVF--TQYRdtAEKIVDLLEKEGIKAVRFvgqaskDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 311908065 308 PLVEYVINYDLPDVAENYVHRIGRTGRGTqKGKAV 342
Cdd:PRK13766 440 PSVDLVIFYEPVPSEIRSIQRKGRTGRQE-EGRVV 473
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
232-342 1.21e-10

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 59.29  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 232 LERMITENPQ-------QKIIVFVRTKVRAERVAAAMARV--NIKTVTL--HSDK------SHIERKAALESFKKGETWV 294
Cdd:cd18801   14 LEEIVKEHFKkkqegsdTRVIIFSEFRDSAEEIVNFLSKIrpGIRATRFigQASGksskgmSQKEQKEVIEQFRKGGYNV 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 311908065 295 LIATDVSARGVDIPLVEYVINYDLPDVAENYVHRIGRTGRGtQKGKAV 342
Cdd:cd18801   94 LVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRK-RQGRVV 140
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
28-154 1.41e-10

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: 59.91  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  28 QYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSlrcLVMVPTHELAQQIADVFKSLAKNTRLKI-MALY 106
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA---LYLYPTKALAQDQLRSLRELLEQLGLGIrVATY 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 311908065 107 -GSTDQEPQIKALQKGVDVLVTTPgRMFDLQ-----AQGHLSLEDIKFLILDEA 154
Cdd:cd17923   82 dGDTPREERRAIIRNPPRILLTNP-DMLHYAllphhDRWARFLRNLRYVVLDEA 134
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
22-156 1.54e-08

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 54.36  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  22 KKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLLASEKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLK 101
Cdd:cd17927    1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 311908065 102 IMALYGstDQEPQIKALQ--KGVDVLVTTPGRMF-DLQAQGHLSLEDIKFLILDEADR 156
Cdd:cd17927   81 VTGLSG--DTSENVSVEQivESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
237-331 1.26e-07

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: 50.28  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 237 TENPQQKIIVFVRTKVRAERVAAAMA-----RVNIKTVTL----HSDKS------HIERKAALESFKKGETWVLIATDVS 301
Cdd:cd18802   21 PKTPDFRGIIFVERRATAVVLSRLLKehpstLAFIRCGFLigrgNSSQRkrslmtQRKQKETLDKFRDGELNLLIATSVL 100
                         90       100       110
                 ....*....|....*....|....*....|
gi 311908065 302 ARGVDIPLVEYVINYDLPDVAENYVHRIGR 331
Cdd:cd18802  101 EEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
27-194 4.32e-07

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: 49.82  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  27 IQYKVLPKVLAGEDIMGIAQTGTGKTAaFAIPVLHLLASEKKSKslrCLVMVPTHELAQQIADVFKSLAkNTRLKIMALY 106
Cdd:cd18035    5 LYQVLIAAVALNGNTLIVLPTGLGKTI-IAILVAADRLTKKGGK---VLILAPSRPLVEQHAENLKRVL-NIPDKITSLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 107 GSTDQEPQIKALQKGvDVLVTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFYQDIIDVKKRIPKRHQTLFFSATL 186
Cdd:cd18035   80 GEVKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPLILGLTASP 158

                 ....*...
gi 311908065 187 DEKIKKLA 194
Cdd:cd18035  159 GSDKEKIM 166
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
241-342 5.10e-07

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: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 241 QQKIIVFVRTKVRAERVAAAMArvniktvtlhsdkshierkaalesfkkgetwVLIATDVSARGVDIPLVEYVINYDLPD 320
Cdd:cd18785    3 VVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPS 51
                         90       100
                 ....*....|....*....|..
gi 311908065 321 VAENYVHRIGRTGRGTQKGKAV 342
Cdd:cd18785   52 SAASYIQRVGRAGRGGKDEGEV 73
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
244-350 7.96e-07

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 48.84  E-value: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 244 IIVFVRT---KVRAERVAAAMARVNIKTVTLHSDkshieRKAALESFKKGETWVLIAT----DVSARGVDIPL-VEYVIN 315
Cdd:cd18798   27 GLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIF 101
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 311908065 316 YDLPdvAENYVHRIGRTGR----GTQKGKAVSFCSDEEL 350
Cdd:cd18798  102 YGVP--VTTYIQASGRTSRlyagGLTKGLSVVLVDDPEL 138
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
38-153 8.25e-07

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 48.73  E-value: 8.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  38 GEDIMGIAQTGTGKTAAFAIPVLHLLASEkKSKSLRCLVMVPTHELaqqIADVFKSLAK-----NTRLKIMALYGSTDQE 112
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADE-PEKGVQVLYISPLKAL---INDQERRLEEpldeiDLEIPVAVRHGDTSQS 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 311908065 113 PQIKALQKGVDVLVTTPGRMFDLQAQGHLS--LEDIKFLILDE 153
Cdd:cd17922   77 EKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
22-158 1.25e-06

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 48.48  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  22 KKPTDIQYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLHLlasekKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLK 101
Cdd:cd17924   16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTTFGLATSLYL-----ASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVE 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065 102 IMAL-YGS----TDQEPQIKALQKG-VDVLVTTPG---RMFDLqaqghLSLEDIKFLILDEADRML 158
Cdd:cd17924   91 VKILvYHSrlkkKEKEELLEKIEKGdFDILVTTNQflsKNFDL-----LSNKKFDFVFVDDVDAVL 151
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
45-307 1.29e-06

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 50.12  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  45 AQTGTGKTAAFAIPVLHLLaseKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRL-------KIMALYGSTDQEPQIKA 117
Cdd:cd09639    6 APTGYGKTEAALLWALHSL---KSQKADRVIIALPTRATINAMYRRAKEAFGETGLyhssilsSRIKEMGDSEEFEHLFP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 118 L-QKGVDVL------VTTPGRM---------FDLQAQGHLSLEDIkflILDEADRMLD--LGFYQDIIDVKKRipKRHQT 179
Cdd:cd09639   83 LyIHSNDTLfldpitVCTIDQVlksvfgefgHYEFTLASIANSLL---IFDEVHFYDEytLALILAVLEVLKD--NDVPI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 180 LFFSATLDEKIKKLAYStvknaIRIQISPDDPVSKNIDHSVVMVSMEDKRF---FLERMITENPQ-QKIIVFVRTKVRAE 255
Cdd:cd09639  158 LLMSATLPKFLKEYAEK-----IGYVEENEPLDLKPNERAPFIKIESDKVGeisSLERLLEFIKKgGSVAIIVNTVDRAQ 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 311908065 256 RV-AAAMARVNIKTVTL-HS--DKSHIERKAA--LESFKKGETWVLIATDVSARGVDI 307
Cdd:cd09639  233 EFyQQLKEKGPEEEIMLiHSrfTEKDRAKKEAelLLEFKKSEKFVIVATQVIEASLDI 290
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
232-330 1.30e-06

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: 47.47  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 232 LERMITE--NPQQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETW--VLIATDVSARGVDI 307
Cdd:cd18793   16 LLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNL 95
                         90       100
                 ....*....|....*....|....*....
gi 311908065 308 PLVEYVINYDLP------DVAENYVHRIG 330
Cdd:cd18793   96 TAANRVILYDPWwnpaveEQAIDRAHRIG 124
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
168-332 3.33e-06

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 49.07  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 168 DVKKRIPKRH-QTLFFSATLDEKikkLAYSTVKNAIRIQISPDDPVSKNIdhsVVMVSM--------------EDKRFF- 231
Cdd:COG0553  456 DVLKDLPEKTeETLYVELTPEQR---ALYEAVLEYLRRELEGAEGIRRRG---LILAALtrlrqicshpalllEEGAELs 529
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 232 --------LERMITEN--PQQKIIVF---VRTkvrAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKG-ETWV-LI 296
Cdd:COG0553  530 grsakleaLLELLEELlaEGEKVLVFsqfTDT---LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPVfLI 606
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311908065 297 ATDVSARGVDIPLVEYVINYDL---PDV---AENYVHRIGRT 332
Cdd:COG0553  607 SLKAGGEGLNLTAADHVIHYDLwwnPAVeeqAIDRAHRIGQT 648
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
47-186 8.94e-06

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: 45.37  E-value: 8.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  47 TGTGKTA-AFAIPVlhllasekKSKSLRCLVMVPTHELAQQIADVFKslAKNTRLKIMALYGStdqepqIKALQKGVDVL 125
Cdd:cd17926   27 TGSGKTLtALALIA--------YLKELRTLIVVPTDALLDQWKERFE--DFLGDSSIGLIGGG------KKKDFDDANVV 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311908065 126 VTTPGRMFDLQAQGHLSLEDIKFLILDEADRMLDLGFyqdiidvkKRIPKRHQ---TLFFSATL 186
Cdd:cd17926   91 VATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF--------SEILKELNakyRLGLTATP 146
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
242-314 1.03e-05

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


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 44.47  E-value: 1.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065 242 QKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIER-KAALESFKKGETW--VLIATDVSARGVDIPLVEYVI 314
Cdd:cd18799    7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV 82
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
242-334 1.43e-05

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 44.56  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 242 QKIIVFVRTKVRAERVAAAMAR------VNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVIN 315
Cdd:cd18796   39 KSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
                         90
                 ....*....|....*....
gi 311908065 316 YDLPDVAENYVHRIGRTGR 334
Cdd:cd18796  119 IGSPKSVARLLQRLGRSGH 137
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
35-154 4.98e-05

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members 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: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 44.09  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  35 VLAgeDIMGIaqtgtGKTaafaIPVLHLLASEKKSKSLR-CLVMVPThelaqqiadvfkSLAKNTR---------LKIMA 104
Cdd:cd18012   27 ILA--DDMGL-----GKT----LQTLALLLSRKEEGRKGpSLVVAPT------------SLIYNWEeeaakfapeLKVLV 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311908065 105 LYGSTDQEPQIKALqKGVDVLVTTPG---RMFDLQAQGHLSLedikfLILDEA 154
Cdd:cd18012   84 IHGTKRKREKLRAL-EDYDLVITSYGllrRDIELLKEVKFHY-----LVLDEA 130
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
245-344 9.91e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.32  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 245 IVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDLPDVAEN 324
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                         90       100
                 ....*....|....*....|
gi 311908065 325 YVHRIGRTGRGTQKGKAVSF 344
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLF 339
ResIII pfam04851
Type III restriction enzyme, res subunit;
47-185 1.46e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   47 TGTGKT--AAFAIPVLHllaseKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLKIMALYGSTDQEPQIKAlqkgvDV 124
Cdd:pfam04851  32 TGSGKTltAAKLIARLF-----KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESVDDN-----KI 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311908065  125 LVTTPGRMF--DLQAQGHLSLEDIKFLILDEADRMLDlGFYQDIIDVKKripkrHQTLF-FSAT 185
Cdd:pfam04851 102 VVTTIQSLYkaLELASLELLPDFFDVIIIDEAHRSGA-SSYRNILEYFK-----PAFLLgLTAT 159
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
23-153 1.53e-04

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 42.46  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  23 KPTDIQYKVLPKVLAGEDIMGIAQTGTGKT-AAFAIPVLHLLASEKKSKSLRCLVMVPTHELAQQIADVFkSLAKNTRLK 101
Cdd:cd18036    2 ELRNYQLELVLPALRGKNTIICAPTGSGKTrVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEKF-FKYFRKGYK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065 102 IMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQG----HLSLEDIKFLILDE 153
Cdd:cd18036   81 VTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDE 136
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
28-346 1.78e-04

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 43.73  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065   28 QYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPvlhllasekkskSLRC----LVMVPTHELAQ-QIADVFKSlakntrlKI 102
Cdd:PLN03137  465 QREIINATMSGYDVFVLMPTGGGKSLTYQLP------------ALICpgitLVISPLVSLIQdQIMNLLQA-------NI 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  103 MALYGSTDQE--PQIKALQK------GVDVLVTTPGR----------MFDLQAQGHLSlediKFLIlDEADRMLDLGF-- 162
Cdd:PLN03137  526 PAASLSAGMEwaEQLEILQElsseysKYKLLYVTPEKvaksdsllrhLENLNSRGLLA----RFVI-DEAHCVSQWGHdf 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  163 ---YQDIIDVKKRIPKRhQTLFFSATLDEKIKK---LAYSTVkNAIRIQISPDDPvskNIDHSVVMVS---MEDkrffLE 233
Cdd:PLN03137  601 rpdYQGLGILKQKFPNI-PVLALTATATASVKEdvvQALGLV-NCVVFRQSFNRP---NLWYSVVPKTkkcLED----ID 671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  234 RMITENPQQKI-IVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEY 312
Cdd:PLN03137  672 KFIKENHFDECgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRF 751
                         330       340       350
                  ....*....|....*....|....*....|....
gi 311908065  313 VINYDLPDVAENYVHRIGRTGRGTQKGKAVSFCS 346
Cdd:PLN03137  752 VIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYS 785
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
27-154 3.23e-04

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 41.48  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  27 IQYKVLPKVLAGEDIMGI-AQTGTGKT--AAFAIpvLHLLASEKKSkslRCLVMVPTHELA-QQIADVFKSLAKNTRLKI 102
Cdd:cd18021    7 IQTQVFNSLYNTDDNVFVgAPTGSGKTvcAELAL--LRHWRQNPKG---RAVYIAPMQELVdARYKDWRAKFGPLLGKKV 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 103 MALYGSTDQEpqIKALQKGvDVLVTTPGRmFDLqaqghLS--------LEDIKFLILDEA 154
Cdd:cd18021   82 VKLTGETSTD--LKLLAKS-DVILATPEQ-WDV-----LSrrwkqrknVQSVELFIADEL 132
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
27-153 4.37e-04

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 41.19  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  27 IQYKVLPKVLAGEDIMGI-AQTGTGKTAAFAIPVLHLL--ASEKKSKSLRCLVMVPTHELAQQIADVFKSLAKNTRLKIM 103
Cdd:cd18023    5 IQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELAILRLLkeRNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311908065 104 ALYGSTDQEPQIKAlqKGVDVLVTTPGR---MFDLQAQGHLSLEDIKFLILDE 153
Cdd:cd18023   85 ELTGDTEMDDTFEI--QDADIILTTPEKwdsMTRRWRDNGNLVQLVALVLIDE 135
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
243-308 5.63e-04

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: 40.31  E-value: 5.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065 243 KIIVFVRTKVRAERVAAamaRVNIKTVTlhSDKSHIERKAALESFKKGETWVLIATDVSARGVDIP 308
Cdd:cd18789   51 KIIVFTDNVEALYRYAK---RLLKPFIT--GETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLP 111
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
271-345 6.06e-04

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


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 40.02  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 271 LHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYDlpdvAENY----VHRI-GRTGRGTQKgkavSFC 345
Cdd:cd18811   67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED----AERFglsqLHQLrGRVGRGDHQ----SYC 138
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
243-338 8.79e-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: 39.55  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 243 KIIVFVRTKVRAERVAAaMARVNIKTVTLHSDK--SH------IERKAALESFKKGETWVLIATDVSARGVDIPLVEYVI 314
Cdd:cd18797   37 KTIVFCRSRKLAELLLR-YLKARLVEEGPLASKvaSYragylaEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
                         90       100
                 ....*....|....*....|....
gi 311908065 315 NYDLPDVAENYVHRIGRTGRGTQK 338
Cdd:cd18797  116 LAGYPGSLASLWQQAGRAGRRGKD 139
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
48-157 1.18e-03

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 39.71  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  48 GTGKTAAFAIPVLHLLASEKkskslRCLVMVPTHELAQQIADVFKSLAKNtrLKIMALYGSTDQepQIKAlqkGVDVLVT 127
Cdd:cd17918   46 GSGKTLVALGAALLAYKNGK-----QVAILVPTEILAHQHYEEARKFLPF--INVELVTGGTKA--QILS---GISLLVG 113
                         90       100       110
                 ....*....|....*....|....*....|
gi 311908065 128 TPGRMFdLQAQGHlsleDIKFLILDEADRM 157
Cdd:cd17918  114 THALLH-LDVKFK----NLDLVIVDEQHRF 138
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
242-317 1.45e-03

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 39.15  E-value: 1.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065 242 QKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYVINYD 317
Cdd:cd18790   28 ERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
28-185 1.59e-03

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 39.55  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  28 QYKVLPKVLAGEDIMGIAQTGTGKTAAFAIPVLhLLASEKKSKSlrcLVMVPTHELaqqIADVFKSLAKntRLKIMALYG 107
Cdd:cd18018   17 QEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL-LLRRRGPGLT---LVVSPLIAL---MKDQVDALPR--AIKAAALNS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 108 S---TDQEPQIKALQKG-VDVLVTTPGRmfdLQAQGHLSL----EDIKFLILDEADRMLDLGF-----YQDIIDVKKRIP 174
Cdd:cd18018   88 SltrEERRRILEKLRAGeVKILYVSPER---LVNESFRELlrqtPPISLLVVDEAHCISEWSHnfrpdYLRLCRVLRELL 164
                        170
                 ....*....|.
gi 311908065 175 KRHQTLFFSAT 185
Cdd:cd18018  165 GAPPVLALTAT 175
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
241-313 1.88e-03

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 40.36  E-value: 1.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311908065  241 QQKIIVFVRTKVRAERVAAAMARVNIKTVTLHSDKSHIERKAALESFKKGETWVLIATDVSARGVDIPLVEYV 313
Cdd:TIGR00631 442 NERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 514
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
22-153 1.98e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 39.03  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  22 KKPTDIQYKVLPKVLAGEDIMGIAQTGTGKT-AAFAIPVLHL--LASEKKSKSLRCLVMVPTHElaqQIADVFKSLAKNT 98
Cdd:cd18073    1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTfVSLLICEHHLkkFPQGQKGKVVFFATKVPVYE---QQKSVFSKYFERH 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311908065  99 RLKIMALYGSTDQEPQIKALQKGVDVLVTTPGRMFDLQAQGHL-SLEDIKFLILDE 153
Cdd:cd18073   78 GYRVTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
44-307 3.04e-03

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 39.68  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  44 IAQTGTGKT-AAFAIpVLHLLASEKKSkslRCLVMVPTHELAQQIADVFK-----SLAK---NTRLKIMALYGSTDQEPQ 114
Cdd:COG1203  153 TAPTGGGKTeAALLF-ALRLAAKHGGR---RIIYALPFTSIINQTYDRLRdlfgeDVLLhhsLADLDLLEEEEEYESEAR 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 115 IKALQKGV---DVLVTTPGRMFD--LQAQGHLSLediKF-------LILDEADrMLDLGFYQDIIDVKKRIpKRHQT--L 180
Cdd:COG1203  229 WLKLLKELwdaPVVVTTIDQLFEslFSNRKGQER---RLhnlansvIILDEVQ-AYPPYMLALLLRLLEWL-KNLGGsvI 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065 181 FFSATL----------------DEKIKKLAYSTVKNAIRIQISPDDpvsknidhsvvmVSMEDkrfFLERMITE-NPQQK 243
Cdd:COG1203  304 LMTATLppllreelleayelipDEPEELPEYFRAFVRKRVELKEGP------------LSDEE---LAELILEAlHKGKS 368
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311908065 244 IIVFVRTKVRAERVAAAMA--RVNIKTVTLHS-----DKSHIERKaALESFKKGETWVLIATDVSARGVDI 307
Cdd:COG1203  369 VLVIVNTVKDAQELYEALKekLPDEEVYLLHSrfcpaDRSEIEKE-IKERLERGKPCILVSTQVVEAGVDI 438
DEXHc_TRCF cd17991
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ...
76-156 7.71e-03

DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a 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: 350749 [Multi-domain]  Cd Length: 193  Bit Score: 37.17  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311908065  76 VMVPTHELAQQIADVFKSLAKNTRLKIMALYGST---DQEPQIKALQKG-VDVLVTTpgrmfdlqaqgH-LSLEDIKF-- 148
Cdd:cd17991   69 VLVPTTLLAQQHYETFKERFANFPVNVELLSRFTtaaEQREILEGLKEGkVDIVIGT-----------HrLLSKDVEFkn 137
                         90
                 ....*....|.
gi 311908065 149 ---LILDEADR 156
Cdd:cd17991  138 lglLIIDEEQR 148
 
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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