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Conserved domains on  [gi|550794329|gb|ERS91912|]
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hypothetical protein Q671_14400 [Halomonas sp. PBN3]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 11485501)

ATP-dependent RNA helicase DbpA is a DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
9-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


:

Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 770.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTREL 88
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:PRK11776  85 ADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDqaRLEALSRLLLHLRP 248
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE--RLPALQRLLLHHQP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 249 ASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARE 328
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 329 LEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALPPRAVLAGDPLVPLMATLQLGAGKKQKVRPGD 408
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRPGD 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 550794329 409 ILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:PRK11776 403 ILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKG 451
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
9-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 770.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTREL 88
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:PRK11776  85 ADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDqaRLEALSRLLLHLRP 248
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE--RLPALQRLLLHHQP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 249 ASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARE 328
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 329 LEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALPPRAVLAGDPLVPLMATLQLGAGKKQKVRPGD 408
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRPGD 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 550794329 409 ILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:PRK11776 403 ILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKG 451
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
10-407 1.45e-179

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 508.92  E-value: 1.45e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDL-ASFRVQGLVLCPTREL 88
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:COG0513   84 ALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESH-DAGSIHERVYRVADGDqaRLEALSRLLLHLR 247
Cdd:COG0513  163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENaTAETIEQRYYLVDKRD--KLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 248 PASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIAR 327
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 328 ELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALPPRAVLAGDPLVPLMATLQLGAGKKQKVRPG 407
Cdd:COG0513  321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
19-211 1.12e-90

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: 273.93  E-value: 1.12e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFR----VQGLVLCPTRELADQVAS 94
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  95 ELRRLARtLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEA 174
Cdd:cd00268   81 VARKLGK-GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 175 IVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVE 211
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
32-197 1.98e-55

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: 182.06  E-value: 1.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   32 TPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQVASELRRLARTLpNVKVLTL 111
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  112 CGGAPFGPQLASLAhGAHLVVGTPGRIEEHLRKGSLvLDGLATLVLDEADRMLDMGFQASLEAIVAETPAHRQTLLFSAT 191
Cdd:pfam00270  80 LGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*.
gi 550794329  192 FSDAVR 197
Cdd:pfam00270 158 LPRNLE 163
DEXDc smart00487
DEAD-like helicases superfamily;
23-212 2.57e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 164.59  E-value: 2.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329    23 LDSLGFTAMTPIQAESLPPILAG-RDVIARARTGSGKTAAFGLGLLSRLdLASFRVQGLVLCPTRELADQVASELRRLAR 101
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   102 TLpNVKVLTLCGGAPFGPQLASLAHG-AHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEAIVAETP 180
Cdd:smart00487  80 SL-GLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 550794329   181 AHRQTLLFSATFSDAVRPLAAALMRDPVGVEV 212
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
146-314 3.32e-04

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 42.83  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  146 SLVLDGLATLVLDEADRMLD---MGFQASLEAIVAETPAHrqtLLFSATFSDAVRPLAAALmrDPVGVEVAESHDAGSIH 222
Cdd:TIGR01587 119 TLASIANSLLIFDEVHFYDEytlALILAVLEVLKDNDVPI---LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRF 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  223 ERV---YRVAD--GDQARLEALSRLLLhlRPASSVVFCNTKRETDEVAQAL--DAAGFSALALHGDLEQADRDR-----L 290
Cdd:TIGR01587 194 ENHrfiLIESDkvGEISSLERLLEFIK--KGGSIAIIVNTVDRAQEFYQQLkeKAPEEEIILYHSRFTEKDRAKkeaelL 271
                         170       180
                  ....*....|....*....|....
gi 550794329  291 LVLFANRSASILVATDVAARGLDI 314
Cdd:TIGR01587 272 REMKKSNEKFVIVATQVIEASLDI 295
 
Name Accession Description Interval E-value
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
9-457 0e+00

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 770.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTREL 88
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:PRK11776  85 ADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDqaRLEALSRLLLHLRP 248
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE--RLPALQRLLLHHQP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 249 ASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARE 328
Cdd:PRK11776 243 ESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 329 LEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALPPRAVLAGDPLVPLMATLQLGAGKKQKVRPGD 408
Cdd:PRK11776 323 PEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRPGD 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 550794329 409 ILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:PRK11776 403 ILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKG 451
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
10-407 1.45e-179

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 508.92  E-value: 1.45e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDL-ASFRVQGLVLCPTREL 88
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsRPRAPQALILAPTREL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:COG0513   84 ALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESH-DAGSIHERVYRVADGDqaRLEALSRLLLHLR 247
Cdd:COG0513  163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENaTAETIEQRYYLVDKRD--KLELLRRLLRDED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 248 PASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIAR 327
Cdd:COG0513  241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 328 ELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALPPRAVLAGDPLVPLMATLQLGAGKKQKVRPG 407
Cdd:COG0513  321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGG 400
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
10-373 8.93e-93

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 287.99  E-value: 8.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG----LVLCPT 85
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGppriLILTPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  86 RELADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLD 165
Cdd:PRK11192  83 RELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 166 MGFQASLEAIVAETPAHRQTLLFSATF-SDAVRPLAAALMRDPVGVEVAES-HDAGSIHERVYRvADGDQARLEALSRLL 243
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEPSrRERKKIHQWYYR-ADDLEHKTALLCHLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 244 LHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNY 323
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794329 324 HIARELEVHVHRVGRTGRAGSAGVACTLVgEGEAYR-LARLTEFLGEPLEE 373
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLV-EAHDHLlLGKIERYIEEPLKA 370
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
19-211 1.12e-90

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: 273.93  E-value: 1.12e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFR----VQGLVLCPTRELADQVAS 94
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  95 ELRRLARtLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEA 174
Cdd:cd00268   81 VARKLGK-GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 175 IVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVE 211
Cdd:cd00268  160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
4-365 5.15e-89

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 284.05  E-value: 5.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   4 TSPDAAFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLC 83
Cdd:PRK11634   2 AEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  84 PTRELADQVASELRRLARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRM 163
Cdd:PRK11634  82 PTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 164 LDMGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDQaRLEALSRLL 243
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 244 LHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNY 323
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 550794329 324 HIARELEVHVHRVGRTGRAGSAGVACTLVgEGEAYRLARLTE 365
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFV-ENRERRLLRNIE 361
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
10-382 2.23e-80

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 257.15  E-value: 2.23e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL---DLASFRVQG----LVL 82
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtPPPKERYMGepraLII 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  83 CPTRELADQVASELRRLARtLPNVKVLTLCGGAPFGPQLASL-AHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEAD 161
Cdd:PRK01297 169 APTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 162 RMLDMGFQASLEAIVAETP--AHRQTLLFSATFSDAVRPLAAALMRDPVGVEV-AESHDAGSIHERVYRVADGDQARLea 238
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIePENVASDTVEQHVYAVAGSDKYKL-- 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 239 LSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELD 318
Cdd:PRK01297 326 LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550794329 319 AVFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLeEAALPPRAVL 382
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI-SCEMPPAELL 468
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
9-377 8.17e-76

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 244.72  E-value: 8.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG------LVL 82
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrpvraLIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  83 CPTRELADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADR 162
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 163 MLDMGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDQARlEALSRL 242
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKR-ELLSQM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 243 LLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFN 322
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 550794329 323 YHIARELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEEAALP 377
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
PTZ00110 PTZ00110
helicase; Provisional
19-378 6.13e-75

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 245.07  E-value: 6.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG-----LVLCPTRELADQVA 93
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLVLAPTRELAEQIR 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  94 SELRRLARTLpnvKVLTLC--GGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQAS 171
Cdd:PTZ00110 221 EQCNKFGASS---KIRNTVayGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQ 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 172 LEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRD-PVGVEVAE-----SHdagSIHERVYRVADGDQ-ARLEALSRLLL 244
Cdd:PTZ00110 298 IRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSldltaCH---NIKQEVFVVEEHEKrGKLKMLLQRIM 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 245 hlRPASSV-VFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNY 323
Cdd:PTZ00110 375 --RDGDKIlIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINF 452
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794329 324 HIARELEVHVHRVGRTGRAGSAGVACTLVgEGEAYRLAR-LTEFLGEPLEEaaLPP 378
Cdd:PTZ00110 453 DFPNQIEDYVHRIGRTGRAGAKGASYTFL-TPDKYRLARdLVKVLREAKQP--VPP 505
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
10-371 1.74e-74

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 240.26  E-value: 1.74e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLG----LLSRLDLASFRVQG---LVL 82
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVNQpraLIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  83 CPTRELADQVASELRRLARTlPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADR 162
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQA-TGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 163 MLDMGFQASLEAIVAETPA--HRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGS-IHERVYRVADGDQARLeaL 239
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHrIKEELFYPSNEEKMRL--L 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 240 SRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDA 319
Cdd:PRK04837 247 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550794329 320 VFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPL 371
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
PTZ00424 PTZ00424
helicase 45; Provisional
9-373 2.16e-70

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 228.94  E-value: 2.16e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTREL 88
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGF 168
Cdd:PTZ00424 109 AQQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 169 QASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHDAGSIHERVYRVADGDQARLEALSRLLLHLRP 248
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTI 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 249 ASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARE 328
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 550794329 329 LEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLGEPLEE 373
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEE 392
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-457 3.99e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 219.82  E-value: 3.99e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   1 MSDTS-PDAAFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLG----LLSRLDLASF 75
Cdd:PRK04537   1 MSDKPlTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAvmnrLLSRPALADR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  76 RVQ---GLVLCPTRELADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLV-LDG 151
Cdd:PRK04537  81 KPEdprALILAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVsLHA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 152 LATLVLDEADRMLDMGFQASLEAIVAETPAH--RQTLLFSATFSDAVRPLAAALMRDPVGVEV-AESHDAGSIHERVYRV 228
Cdd:PRK04537 160 CEICVLDEADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVeTETITAARVRQRIYFP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 229 ADGDQARLeaLSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVA 308
Cdd:PRK04537 240 ADEEKQTL--LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 309 ARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTEFLgepleEAALPPRAVLAgDPLV 388
Cdd:PRK04537 318 ARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYI-----EQKIPVEPVTA-ELLT 391
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 389 PLmatlqlgagkkqkVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVA-VRREVADRALARLRDGRIKG 457
Cdd:PRK04537 392 PL-------------PRPPRVPVEGEEADDEAGDSVGTIFREAREQRAAeEQRRGGGRSGPGGGSRSGSV 448
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
10-211 2.04e-58

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: 191.28  E-value: 2.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELA 89
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSL---VLDGLATLVLDEADRMLDM 166
Cdd:cd17955   81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttkVLSRVKFLVLDEADRLLTG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 550794329 167 GFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVE 211
Cdd:cd17955  160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
19-210 2.38e-58

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: 190.54  E-value: 2.38e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL---DLASFRVQGLVLCPTRELADQVASE 95
Cdd:cd17947    1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  96 LRRLARtLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKG-SLVLDGLATLVLDEADRMLDMGFQASLEA 174
Cdd:cd17947   81 LQQLAQ-FTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKE 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 550794329 175 IVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17947  160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
10-206 5.78e-58

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: 190.39  E-value: 5.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL----DLASFRV------QG 79
Cdd:cd17967    2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgPPSVGRGrrkaypSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  80 LVLCPTRELADQVASELRRLARTLPnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDE 159
Cdd:cd17967   82 LILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794329 160 ADRMLDMGFQASLEAIVAET----PAHRQTLLFSATFSDAVRPLAAALMRD 206
Cdd:cd17967  161 ADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAADFLKN 211
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
15-205 7.41e-57

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: 187.41  E-value: 7.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  15 LATSLLDNLDSLGFTAMTPIQAESLPPILA-GRDVIARARTGSGKTAAFGLGLLSRL-----DLASFRVQGLVLCPTREL 88
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLPNVKVLTLCGGAPFGPQLASLAH-GAHLVVGTPGRIEEHLRKGSL--VLDGLATLVLDEADRMLD 165
Cdd:cd17964   81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLD 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 550794329 166 MGFQASLEAIVAETPA----HRQTLLFSATFSDAVRPLAAALMR 205
Cdd:cd17964  161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
10-211 3.01e-56

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: 185.60  E-value: 3.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELA 89
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLArTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLR--KGsLVLDGLATLVLDEADRMLDMG 167
Cdd:cd17954   82 QQISEQFEALG-SSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKG-FSLKSLKFLVMDEADRLLNMD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 550794329 168 FQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVE 211
Cdd:cd17954  160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
32-197 1.98e-55

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: 182.06  E-value: 1.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   32 TPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQVASELRRLARTLpNVKVLTL 111
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  112 CGGAPFGPQLASLAhGAHLVVGTPGRIEEHLRKGSLvLDGLATLVLDEADRMLDMGFQASLEAIVAETPAHRQTLLFSAT 191
Cdd:pfam00270  80 LGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                  ....*.
gi 550794329  192 FSDAVR 197
Cdd:pfam00270 158 LPRNLE 163
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
9-205 2.67e-54

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: 182.47  E-value: 2.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL-----DLASFR----VQG 79
Cdd:cd18052   44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkeglTASSFSevqePQA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  80 LVLCPTRELADQVASELRRLARTLPnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDE 159
Cdd:cd18052  124 LIVAPTRELANQIFLEARKFSYGTC-IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 550794329 160 ADRMLDMGFQASLEAIVAE--TPA--HRQTLLFSATFSDAVRPLAAALMR 205
Cdd:cd18052  203 ADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAAEFLK 252
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
2-354 4.89e-53

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 186.15  E-value: 4.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   2 SDTSPDAAFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRldLASFRVQG-- 79
Cdd:PLN00206 115 AVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISR--CCTIRSGHps 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  80 -------LVLCPTRELADQVASELRRLARTLPnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGL 152
Cdd:PLN00206 193 eqrnplaMVLTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 153 ATLVLDEADRMLDMGFQASLEAIVAETPaHRQTLLFSATFSDAVRPLAAALMRDPVGVEVAESHD-AGSIHERVYRV-AD 230
Cdd:PLN00206 272 SVLVLDEVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRpNKAVKQLAIWVeTK 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 231 GDQARLEALSRLLLHLRPaSSVVFCNTKRETDEVAQALD-AAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAA 309
Cdd:PLN00206 351 QKKQKLFDILKSKQHFKP-PAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLG 429
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 550794329 310 RGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGE 354
Cdd:PLN00206 430 RGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
10-208 2.51e-52

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: 175.18  E-value: 2.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELA 89
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQ 169
Cdd:cd17940   81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 550794329 170 ASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17940  160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
19-210 1.88e-51

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: 172.76  E-value: 1.88e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL-----DLASFRVQGLVLCPTRELADQVA 93
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  94 SELRR-LARTLPNVKVLTLCGGAPFGPQLASL-AHGAHLVVGTPGRIEEHLRKGSLVLDG--LATLVLDEADRMLDMGFQ 169
Cdd:cd17960   81 EVLQSfLEHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADKVKVksLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 550794329 170 ASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
10-208 1.96e-51

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: 172.87  E-value: 1.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRV--QGLVLCPTRE 87
Cdd:cd17959    3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  88 LADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMG 167
Cdd:cd17959   83 LALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 550794329 168 FQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17959  162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPV 202
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
19-210 1.15e-49

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: 167.93  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG-----LVLCPTRELADQVA 93
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgpivLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  94 SELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLE 173
Cdd:cd17966   81 QEANKFGGSS-RLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 174 AIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17966  160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
19-208 1.23e-49

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: 168.53  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDS-LGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQ------GLVLCPTRELADQ 91
Cdd:cd17949    1 LVSHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  92 VASELRRLARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRK-GSLVLDGLATLVLDEADRMLDMGFQA 170
Cdd:cd17949   81 IYEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794329 171 SLEAIV-------------AETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17949  161 DITKILellddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
19-210 3.63e-49

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: 166.82  E-value: 3.63e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL-DLASFRVQ----GLVLCPTRELADQVA 93
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRELEKGegpiAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  94 SELRRLARtLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLE 173
Cdd:cd17952   81 LEAKKFGK-AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 174 AIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17952  160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
15-208 6.61e-49

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: 166.78  E-value: 6.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  15 LATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLsRLDLASFRVQ------GLVLCPTREL 88
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF-RHIKDQRPVKpgegpiGLIMAPTREL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGS---LVLDGLATLVLDEADRMLD 165
Cdd:cd17953   98 ALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 550794329 166 MGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17953  177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
12-208 7.82e-49

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: 165.96  E-value: 7.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  12 TLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQ 91
Cdd:cd17939    1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  92 VASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQAS 171
Cdd:cd17939   81 IQKVVKALGDYM-GVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 172 LEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17939  160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPV 196
DEXDc smart00487
DEAD-like helicases superfamily;
23-212 2.57e-48

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 164.59  E-value: 2.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329    23 LDSLGFTAMTPIQAESLPPILAG-RDVIARARTGSGKTAAFGLGLLSRLdLASFRVQGLVLCPTRELADQVASELRRLAR 101
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   102 TLpNVKVLTLCGGAPFGPQLASLAHG-AHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEAIVAETP 180
Cdd:smart00487  80 SL-GLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 550794329   181 AHRQTLLFSATFSDAVRPLAAALMRDPVGVEV 212
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
19-210 1.48e-47

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: 163.26  E-value: 1.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLD-----LASFRVQG---LVLCPTRELAD 90
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlpplDEETKDDGpyaLILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  91 QVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQA 170
Cdd:cd17945   81 QIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 171 SLEAIVAETP--------------------AHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17945  160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
221-352 3.23e-47

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: 159.21  E-value: 3.23e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 221 IHERVYRVaDGDQARLEALSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSAS 300
Cdd:cd18787    1 IKQLYVVV-EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550794329 301 ILVATDVAARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLV 352
Cdd:cd18787   80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
19-212 4.08e-47

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: 161.22  E-value: 4.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL--DLASFRVQGLVLCPTRELADQVASEL 96
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  97 RRLARTLPN-VKVLT--LCGGAPFGPQLASlahGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLE 173
Cdd:cd17957   81 LKLSKGTGLrIVLLSksLEAKAKDGPKSIT---KYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 550794329 174 AIVAE-TPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEV 212
Cdd:cd17957  158 EILAAcTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
27-212 1.04e-46

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: 160.59  E-value: 1.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  27 GFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQVASELRRLARTLPNV 106
Cdd:cd17950   21 GFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 107 KVLTLCGGAPFGPQLASLAHGA-HLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRML-DMGFQASLEAIVAETPAHRQ 184
Cdd:cd17950  101 KTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRATPHDKQ 180
                        170       180
                 ....*....|....*....|....*...
gi 550794329 185 TLLFSATFSDAVRPLAAALMRDPVGVEV 212
Cdd:cd17950  181 VMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
15-208 2.09e-46

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: 159.28  E-value: 2.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  15 LATSLLDNLDSLGFTAMTPIQAESLPPILAG--RDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQV 92
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  93 ASELRRLARtLPNVKV-LTLCGGAPFGPQLASlahgAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDM-GFQA 170
Cdd:cd17963   81 GEVVEKMGK-FTGVKVaLAVPGNDVPRGKKIT----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGD 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 550794329 171 SLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17963  156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNAN 193
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
10-211 3.02e-46

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: 159.41  E-value: 3.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRldlasfrVQGLVLCPTRELA 89
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTL--PNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMG 167
Cdd:cd17938   74 EQTYNCIENFKKYLdnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550794329 168 FQASLEAIVAETPAHR------QTLLFSATF-SDAVRPLAAALMRDPVGVE 211
Cdd:cd17938  154 NLETINRIYNRIPKITsdgkrlQVIVCSATLhSFEVKKLADKIMHFPTWVD 204
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
10-200 3.96e-46

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: 160.59  E-value: 3.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL-------------DLASFR 76
Cdd:cd18051   23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpsesGYYGRR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  77 VQ---GLVLCPTRELADQVASELRRLA-RTLpnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGL 152
Cdd:cd18051  103 KQyplALVLAPTRELASQIYDEARKFAyRSR--VRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550794329 153 ATLVLDEADRMLDMGFQASLEAIVAE----TPAHRQTLLFSATFSDAVRPLA 200
Cdd:cd18051  181 KYLVLDEADRMLDMGFEPQIRRIVEQdtmpPTGERQTLMFSATFPKEIQMLA 232
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
19-210 4.13e-46

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: 158.48  E-value: 4.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQVASELRR 98
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  99 LARTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEAIVAE 178
Cdd:cd17962   81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 550794329 179 TPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17962  161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
19-211 1.07e-45

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: 157.43  E-value: 1.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELADQVASELRR 98
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  99 LARTLPNVKVLTLCGGAPFGPQLASLAhGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEAIVAE 178
Cdd:cd17943   81 IGKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 550794329 179 TPAHRQTLLFSATFSDAVRPLAAALMRDPVGVE 211
Cdd:cd17943  160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
23-212 1.39e-45

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: 157.45  E-value: 1.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  23 LDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASF-RVQG---LVLCPTRELADQVASELRR 98
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWtPEDGlgaLIISPTRELAMQIFEVLRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  99 LARtLPNVKVLTLCGGAPFGPQLASLaHGAHLVVGTPGRIEEHLRKG-SLVLDGLATLVLDEADRMLDMGFQASLEAIVA 177
Cdd:cd17941   85 VGK-YHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550794329 178 ETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEV 212
Cdd:cd17941  163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
20-205 2.04e-43

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: 151.92  E-value: 2.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  20 LDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL-----DLASFRV-QGLVLCPTRELADQVA 93
Cdd:cd17944    2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLqedqqPRKRGRApKVLVLAPTRELANQVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  94 SELRRLARTLpnvKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLE 173
Cdd:cd17944   82 KDFKDITRKL---SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 550794329 174 AIV-----AETPAHRQTLLFSATFSDAVRPLAAALMR 205
Cdd:cd17944  159 EILsvsykKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
19-193 8.97e-43

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: 151.24  E-value: 8.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILA-GRDVIARARTGSGKTAAFGLGLLSR-LDLASFR--------VQGLVLCPTREL 88
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERlLSQKSSNgvggkqkpLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTlPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLAT---LVLDEADRMLD 165
Cdd:cd17946   81 AVQVKDHLKAIAKY-TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSlrfLVLDEADRMLE 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550794329 166 MGFQASLEAIVAETPAH-------RQTLLFSATFS 193
Cdd:cd17946  160 KGHFAELEKILELLNKDragkkrkRQTFVFSATLT 194
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
19-208 1.16e-42

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: 149.66  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL------DLASFRVQGLVLCPTRELADQV 92
Cdd:cd17961    5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  93 ASELRRLARTL-PNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVL-DGLATLVLDEADRMLDMGFQA 170
Cdd:cd17961   85 SKVLEQLTAYCrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEE 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 550794329 171 SLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd17961  165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
19-210 3.38e-42

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: 148.64  E-value: 3.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLL-----SRLDLASFRVQG---LVLCPTRELAD 90
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEGpygLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  91 QVASELRRLARTL-----PNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLD 165
Cdd:cd17951   81 QTHEVIEYYCKALqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 550794329 166 MGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17951  161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
23-210 3.65e-42

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: 148.28  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  23 LDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAF---GLGLLSRLDLASFRVQG-LVLCPTRELADQVASELRR 98
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFlipAIELLYKLKFKPRNGTGvIIISPTRELALQIYGVAKE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  99 LArTLPNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLR-KGSLVLDGLATLVLDEADRMLDMGFQASLEAIVA 177
Cdd:cd17942   85 LL-KYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 550794329 178 ETPAHRQTLLFSATFSDAVRPLA-AALMRDPVGV 210
Cdd:cd17942  164 LLPKRRQTMLFSATQTRKVEDLArISLKKKPLYV 197
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
6-213 7.89e-42

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: 148.62  E-value: 7.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   6 PDAAFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG-----L 80
Cdd:cd18049   22 PVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  81 VLCPTRELADQV---ASELRRLARtlpnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVL 157
Cdd:cd18049  102 VLAPTRELAQQVqqvAAEYGRACR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794329 158 DEADRMLDMGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVA 213
Cdd:cd18049  178 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
10-208 9.29e-41

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: 144.53  E-value: 9.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELA 89
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQ 169
Cdd:cd18045   81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 550794329 170 ASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd18045  160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPI 198
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
6-213 2.55e-40

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: 145.92  E-value: 2.55e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   6 PDAAFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQG-----L 80
Cdd:cd18050   60 PVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  81 VLCPTRELADQV---ASELRRLARtlpnVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVL 157
Cdd:cd18050  140 VLAPTRELAQQVqqvADDYGKSSR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794329 158 DEADRMLDMGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGVEVA 213
Cdd:cd18050  216 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
19-210 2.62e-39

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: 140.68  E-value: 2.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASF-RVQG-----LVLCPTRELADQV 92
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIpREQRngpgvLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  93 ASELRRLARTlpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASL 172
Cdd:cd17958   81 EAECSKYSYK--GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 550794329 173 EAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPVGV 210
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
10-208 5.39e-39

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: 139.89  E-value: 5.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRELA 89
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQ 169
Cdd:cd18046   81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 550794329 170 ASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDPV 208
Cdd:cd18046  160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
RRM_EcDbpA_like cd12501
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ...
393-457 5.52e-32

RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.


Pssm-ID: 409924 [Multi-domain]  Cd Length: 73  Bit Score: 116.57  E-value: 5.52e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550794329 393 TLQLGAGKKQKVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:cd12501    1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKG 65
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
234-343 1.53e-27

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: 105.76  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  234 ARLEALSRLLLHLRPASSVVFCNTKRETDEvAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLD 313
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 550794329  314 IAELDAVFNYHIARELEVHVHRVGRTGRAG 343
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
9-207 2.06e-27

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: 109.34  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   9 AFATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAG--RDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTR 86
Cdd:cd18048   19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  87 ELADQVASELRRLARTLPNVKVLTLCGG--APFGPQLAslahgAHLVVGTPGRIEEHLRKGSLV-LDGLATLVLDEADRM 163
Cdd:cd18048   99 ELALQTGKVVEEMGKFCVGIQVIYAIRGnrPGKGTDIE-----AQIVIGTPGTVLDWCFKLRLIdVTNISVFVLDEADVM 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 550794329 164 LDM-GFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDP 207
Cdd:cd18048  174 INVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
19-193 8.12e-26

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: 105.02  E-value: 8.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAG---------RDVIARARTGSGKTAAFGLGLLSRL-DLASFRVQGLVLCPTREL 88
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  89 ADQVASELRRLARTLpNVKVLTLCGGAPFGPQLASLAHGAHL--------VVGTPGRIEEHLRKG-SLVLDGLATLVLDE 159
Cdd:cd17956   81 VQQVYKVFESLCKGT-GLKVVSLSGQKSFKKEQKLLLVDTSGrylsrvdiLVATPGRLVDHLNSTpGFTLKHLRFLVIDE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550794329 160 ADRMLDMGFQASLEAIVAET--------------------PAHRQTLLFSATFS 193
Cdd:cd17956  160 ADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATLT 213
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
19-199 1.77e-25

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: 103.99  E-value: 1.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  19 LLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRL------DLASFRV-QGLVLCPTRELADQ 91
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllAEGPFNApRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  92 VASELRRLARTLP-NVKVLTlcGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQA 170
Cdd:cd17948   81 IGSVAQSLTEGLGlKVKVIT--GGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 550794329 171 SLEAIVAETPAHR-------------QTLLFSATFSDAVRPL 199
Cdd:cd17948  159 KLSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEV 200
DbpA pfam03880
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ...
393-457 2.50e-24

DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].


Pssm-ID: 461082 [Multi-domain]  Cd Length: 72  Bit Score: 95.90  E-value: 2.50e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550794329  393 TLQLGAGKKQKVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:pfam03880   1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKG 65
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
10-207 2.48e-21

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: 91.71  E-value: 2.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  10 FATLPLATSLLDNLDSLGFTAMTPIQAESLPPILAG--RDVIARARTGSGKTAAFGLGLLSRLDLASFRVQGLVLCPTRE 87
Cdd:cd18047    3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  88 LADQVASELRRLARTLPNVKVLTLCGGAPF--GPQLASlahgaHLVVGTPGRIEEHLRKGSLV-LDGLATLVLDEADRML 164
Cdd:cd18047   83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLerGQKISE-----QIVIGTPGTVLDWCSKLKFIdPKKIKVFVLDEADVMI 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 550794329 165 -DMGFQASLEAIVAETPAHRQTLLFSATFSDAVRPLAAALMRDP 207
Cdd:cd18047  158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
HELICc smart00490
helicase superfamily c-terminal domain;
262-343 6.41e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 86.50  E-value: 6.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   262 DEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARELEVHVHRVGRTGR 341
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 550794329   342 AG 343
Cdd:smart00490  81 AG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
45-191 8.26e-18

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: 80.14  E-value: 8.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  45 GRDVIARARTGSGKTAAFGLGLLSRLDLASFRVqgLVLCPTRELADQVASELRRLARtlPNVKVLTLCGGAPFGPQLASL 124
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKV--LVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550794329 125 AHGAHLVVGTPGRIEEHL-RKGSLVLDGLATLVLDEADRMLDMGFQASLEAIvAETPAHR---QTLLFSAT 191
Cdd:cd00046   77 LGDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDL-AVRKAGLknaQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
44-352 8.51e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 79.68  E-value: 8.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  44 AGRDVIARARTGSGKTAaFGLGLLSRLdLASFRVqgLVLCPTRELADQVASELRRLARTLPNVkvltlcggapfgpqLAS 123
Cdd:COG1061   99 GGGRGLVVAPTGTGKTV-LALALAAEL-LRGKRV--LVLVPRRELLEQWAEELRRFLGDPLAG--------------GGK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 124 LAHGAHLVVGTPGRIEEHLRKGSLVlDGLATLVLDEADRMLDMGFQASLEAIvaeTPAHRqtLLFSAT--FSDAVRPLA- 200
Cdd:COG1061  161 KDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAF---PAAYR--LGLTATpfRSDGREILLf 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 201 -----------AALMRD---------PVGVEV-AESHDAGSIHERV-YRVADGDQARLEALSRLLL-HLRPASSVVFCNT 257
Cdd:COG1061  235 lfdgivyeyslKEAIEDgylappeyyGIRVDLtDERAEYDALSERLrEALAADAERKDKILRELLReHPDDRKTLVFCSS 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 258 KRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIAELDAVFnyhIARELE---VHVH 334
Cdd:COG1061  315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGsprEFIQ 391
                        330
                 ....*....|....*...
gi 550794329 335 RVGRTGRAGSAGVACTLV 352
Cdd:COG1061  392 RLGRGLRPAPGKEDALVY 409
RRM_DbpA cd12252
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ...
393-457 1.14e-14

RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.


Pssm-ID: 409698 [Multi-domain]  Cd Length: 71  Bit Score: 68.73  E-value: 1.14e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550794329 393 TLQLGAGKKQKVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:cd12252    1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKG 65
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
48-191 2.86e-13

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: 69.33  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  48 VIArARTGSGKTAAFGLGLLSRL---DLASF--------------RVQGLVLCPTRELADQVASELRRLARTLP-NVKVL 109
Cdd:cd17965   65 LLA-AETGSGKTLAYLAPLLDYLkrqEQEPFeeaeeeyesakdtgRPRSVILVPTHELVEQVYSVLKKLSHTVKlGIKTF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 110 TLCGGAPFGPQLASLAHGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEADRMLDMGFQASLEAIVAETPAHRQTLLFS 189
Cdd:cd17965  144 SSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCS 223

                 ..
gi 550794329 190 AT 191
Cdd:cd17965  224 AT 225
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
226-365 5.64e-13

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 70.55  E-value: 5.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 226 YRVADG-DQARLEALSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVA 304
Cdd:COG0514  207 LEVVPKpPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550794329 305 TdVA-ARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGEGEAYRLARLTE 365
Cdd:COG0514  287 T-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
31-195 4.22e-12

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: 64.59  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  31 MTPIQAESLPPI-LAGRDVIARARTGSGKTAAFGLGLLSRLDLASFRVqgLVLCPTRELADQVASELRRLARTLP-NVKV 108
Cdd:cd17921    2 LNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA--VYIAPTRALVNQKEADLRERFGPLGkNVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 109 LTlcGGAPFGPQLASlahGAHLVVGTPGRIEEHLRKG-SLVLDGLATLVLDEAdRMLDMGFQA-SLEAIVAETPA---HR 183
Cdd:cd17921   80 LT--GDPSVNKLLLA---EADILVATPEKLDLLLRNGgERLIQDVRLVVVDEA-HLIGDGERGvVLELLLSRLLRinkNA 153
                        170
                 ....*....|..
gi 550794329 184 QTLLFSATFSDA 195
Cdd:cd17921  154 RFVGLSATLPNA 165
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
221-351 4.61e-11

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: 60.30  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 221 IHERVYRVADGDQARLEaLSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSAS 300
Cdd:cd18794    4 LFYSVRPKDKKDEKLDL-LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQ 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550794329 301 ILVATdVA-ARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTL 351
Cdd:cd18794   83 VIVAT-VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
7-378 1.23e-10

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: 63.70  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329   7 DAAFATLP--LATSLLDNLDSLGFTAMTPIQAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLdLASFRVQGLVLCP 84
Cdd:COG1205   31 EARYAPWPdwLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  85 TRELA-DQVAsELRRLARTL-PNVKVLTLCGGAPFGPQLASLAHgAHLVVGTPGRIEEHL----RKGSLVLDGLATLVLD 158
Cdd:COG1205  110 TKALArDQLR-RLRELAEALgLGVRVATYDGDTPPEERRWIREH-PDIVLTNPDMLHYGLlphhTRWARFFRNLRYVVID 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 159 EA---------------DRMLDmgfqasleaIVAETPAHRQTLLFSATFSDAVRpLAAALmrdpVGVEVAESHDAGSIHE 223
Cdd:COG1205  188 EAhtyrgvfgshvanvlRRLRR---------ICRHYGSDPQFILASATIGNPAE-HAERL----TGRPVTVVDEDGSPRG 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 224 RVYRV-----ADGDQARLEALS---RLLLHL--RPASSVVFCNTKRETDEVA-QALDAAGFSALAL-----HGDLEQADR 287
Cdd:COG1205  254 ERTFVlwnppLVDDGIRRSALAeaaRLLADLvrEGLRTLVFTRSRRGAELLArYARRALREPDLADrvaayRAGYLPEER 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 288 DRLLVLFANRSASILVATDVAARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLVGEG--EAYRLARLTE 365
Cdd:COG1205  334 REIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDplDQYYVRHPEE 413
                        410
                 ....*....|...
gi 550794329 366 FLGEPLEEAALPP 378
Cdd:COG1205  414 LFERPPEAAVIDP 426
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
11-305 2.33e-09

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 59.52  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  11 ATLPLATsLLDNLDSLGFTAMTPIQAESLPP-ILAGRDVIARARTGSGKTAAFGLGLLSRLdLASFRVqgLVLCPTRELA 89
Cdd:COG1204    4 AELPLEK-VIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKAL-LNGGKA--LYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  90 DQVASELRRLARTLpNVKVLTLCGGAPFGPQLASlahGAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEA------DRm 163
Cdd:COG1204   80 SEKYREFKRDFEEL-GIKVGVSTGDYDSDDEWLG---RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 164 ldmGFQasLEAIVA---ETPAHRQTLLFSATFSDAvRPLAAALMRDPVGVE------VAESHDAGSIHervyrVADGDQA 234
Cdd:COG1204  155 ---GPT--LEVLLArlrRLNPEAQIVALSATIGNA-EEIAEWLDAELVKSDwrpvplNEGVLYDGVLR-----FDDGSRR 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 235 RLEALSRLLLH-LRPASSV-VFCNTKRETDEVAQAL-----------DAAGFSALAL----------------------- 278
Cdd:COG1204  224 SKDPTLALALDlLEEGGQVlVFVSSRRDAESLAKKLadelkrrltpeEREELEELAEellevseethtnekladclekgv 303
                        330       340       350
                 ....*....|....*....|....*....|
gi 550794329 279 ---HGDLEQADRDRLLVLFANRSASILVAT 305
Cdd:COG1204  304 afhHAGLPSELRRLVEDAFREGLIKVLVAT 333
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
234-335 3.70e-09

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 54.79  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 234 ARLEALSRLLLHLRPAS--SVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSAS--ILVATDVAA 309
Cdd:cd18793   11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGG 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 550794329 310 RGLDIAELDAVFNYHI----AREL-------------EVHVHR 335
Cdd:cd18793   91 VGLNLTAANRVILYDPwwnpAVEEqaidrahrigqkkPVVVYR 133
RRM_BsYxiN_like cd12500
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ...
394-457 1.55e-07

RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409923 [Multi-domain]  Cd Length: 73  Bit Score: 48.61  E-value: 1.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550794329 394 LQLGAGKKQKVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:cd12500    2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKG 65
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
35-160 2.98e-07

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: 50.28  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  35 QAESLPPILAGRDVIARARTGSGKTAAFGLGLLSRLdLASFRVQGLVLCPTRELA-DQVASELRRLARTLPNVKVLTLCG 113
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAqDQLRSLRELLEQLGLGIRVATYDG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550794329 114 GAPFGPQLASLAHGAHLVVGTPGRIE-----EHLRKGSLvLDGLATLVLDEA 160
Cdd:cd17923   84 DTPREERRAIIRNPPRILLTNPDMLHyallpHHDRWARF-LRNLRYVVLDEA 134
RRM_EcCsdA_like cd12499
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ...
393-457 9.34e-07

RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.


Pssm-ID: 409922 [Multi-domain]  Cd Length: 73  Bit Score: 46.41  E-value: 9.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550794329 393 TLQLGAGKKQKVRPGDILGALTGEAGLAGDQVGKIKVLANSAYVAVRREVADRALARLRDGRIKG 457
Cdd:cd12499    1 RYRIEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCG 65
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
229-359 1.19e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 50.88  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 229 ADGDQARLEALSRLL---LHLRPASSV-VFCNTkRET-DEVAQALDAAGFSALALHGdleQADRD---------RLLVL- 293
Cdd:COG1111  330 ADIEHPKLSKLREILkeqLGTNPDSRIiVFTQY-RDTaEMIVEFLSEPGIKAGRFVG---QASKEgdkgltqkeQIEILe 405
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550794329 294 -FANRSASILVATDVAARGLDIAELDAVFNYhiarEL---EVH-VHRVGRTGRAGsAGVACTLVGEG---EAYR 359
Cdd:COG1111  406 rFRAGEFNVLVATSVAEEGLDIPEVDLVIFY----EPvpsEIRsIQRKGRTGRKR-EGRVVVLIAKGtrdEAYY 474
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
34-177 6.03e-06

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: 46.97  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  34 IQAESLPPIL-AGRDVIARARTGSGKTAAFGLGLL----SRLDLASFRVQGLVLCPTRELADQVASELR-RLARtlPNVK 107
Cdd:cd18023    5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKALCSEKYDDWKeKFGP--LGLS 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550794329 108 VLTLCGGAPFGPqLASLAHgAHLVVGTPGRIEEHLRK----GSLVLDgLATLVLDEAdRMLDMGFQASLEAIVA 177
Cdd:cd18023   83 CAELTGDTEMDD-TFEIQD-ADIILTTPEKWDSMTRRwrdnGNLVQL-VALVLIDEV-HIIKENRGATLEVVVS 152
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
297-352 6.55e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 43.85  E-value: 6.55e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550794329 297 RSASILVATDVAARGLDIAELDAVFNYHIARELEVHVHRVGRTGRAGSAGVACTLV 352
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
PRK13766 PRK13766
Hef nuclease; Provisional
230-359 1.03e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 47.95  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 230 DGDQARLEALSRLL---LHLRPASSV-VFCNTkRETDE-VAQALDAAGFSALALHGdleQADRDR-----------LLVL 293
Cdd:PRK13766 343 DIEHPKLEKLREIVkeqLGKNPDSRIiVFTQY-RDTAEkIVDLLEKEGIKAVRFVG---QASKDGdkgmsqkeqieILDK 418
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 294 FANRSASILVATDVAARGLDIAELDAVFNYH-IARELEVhVHRVGRTGRaGSAGVACTLVGEG---EAYR 359
Cdd:PRK13766 419 FRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAKGtrdEAYY 486
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
236-343 1.19e-05

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 47.79  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 236 LEALSRLLLHLRPASSVVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSASILVATDVAARGLDIA 315
Cdd:PRK11057 224 LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP 303
                         90       100
                 ....*....|....*....|....*...
gi 550794329 316 ELDAVFNYHIARELEVHVHRVGRTGRAG 343
Cdd:PRK11057 304 NVRFVVHFDIPRNIESYYQETGRAGRDG 331
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
54-192 2.33e-05

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: 44.22  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  54 TGSGKTAafgLGLLSRLDLASFRVqgLVLCPTRELADQVAselRRLARTLPNVKVLTLCGGAPFGPQlaslahGAHLVVG 133
Cdd:cd17926   27 TGSGKTL---TALALIAYLKELRT--LIVVPTDALLDQWK---ERFEDFLGDSSIGLIGGGKKKDFD------DANVVVA 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 134 TPGRIEEHLRKGSLVLDGLATLVLDEADRmldmgFQA-SLEAIVAETPAHRQtLLFSATF 192
Cdd:cd17926   93 TYQSLSNLAEEEKDLFDQFGLLIVDEAHH-----LPAkTFSEILKELNAKYR-LGLTATP 146
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
249-320 2.74e-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: 43.32  E-value: 2.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550794329 249 ASSVVFCNTKRETDEVAQALDAAGFSALALHGDL-------EQADRDRllvlFANRSASILVATDVAARGLDIAELDAV 320
Cdd:cd18799    7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYsdrergdEALILLF----FGELKPPILVTVDLLTTGVDIPEVDNV 81
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
54-162 3.20e-05

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: 44.43  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  54 TGSGKTAAFGLGLLSRLDLASFRVqgLVLCPTRELADQVASELRRLARTLPNVKVLTlcgGAPFGPQLASLAHGAHLVVG 133
Cdd:cd18035   25 TGLGKTIIAILVAADRLTKKGGKV--LILAPSRPLVEQHAENLKRVLNIPDKITSLT---GEVKPEERAERWDASKIIVA 99
                         90       100
                 ....*....|....*....|....*....
gi 550794329 134 TPGRIEEHLRKGSLVLDGLATLVLDEADR 162
Cdd:cd18035  100 TPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
23-163 3.75e-05

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 44.33  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  23 LDSLGFTaMTPIQAESLPPILAG------RDVIARARTGSGKTAAFGLGLLSRLDlASFRVqgLVLCPTRELADQVASEL 96
Cdd:cd17918    9 CKSLPFS-LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYK-NGKQV--AILVPTEILAHQHYEEA 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550794329  97 RRLartLPNVKVLTLCGGAPfgpqlASLAHGAHLVVGTPGRIEEHLRKGSLVLdglatLVLDEADRM 163
Cdd:cd17918   85 RKF---LPFINVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
234-323 8.37e-05

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 45.22  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 234 ARLEALSRLLLHLRPASS--VVFCNTKRETDEVAQALDAAGFSALALHGDLEQADRDRLLVLFANRSAS--ILVATDVAA 309
Cdd:COG0553  533 AKLEALLELLEELLAEGEkvLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGG 612
                         90
                 ....*....|....
gi 550794329 310 RGLDIAELDAVFNY 323
Cdd:COG0553  613 EGLNLTAADHVIHY 626
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
28-70 2.18e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 43.94  E-value: 2.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 550794329  28 FTAMTPIQAESLPPILAGRDVIARARTGSGKT-AAFgLGLLSRL 70
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDEL 64
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
146-314 2.51e-04

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 43.19  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 146 SLVLDGLATLVLDEADRMLD---MGFQASLEAIVAETPAHrqtLLFSATFSDAVRPLAAALmrDPVGVEVAESHDAGSIH 222
Cdd:cd09639  118 TLASIANSLLIFDEVHFYDEytlALILAVLEVLKDNDVPI---LLMSATLPKFLKEYAEKI--GYVEENEPLDLKPNERA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 223 ERVYRVAD--GDQARLEALSRLLLhlRPASSVVFCNTKRETDEVAQAL--DAAGFSALALHGDLEQADR----DRLLVLF 294
Cdd:cd09639  193 PFIKIESDkvGEISSLERLLEFIK--KGGSVAIIVNTVDRAQEFYQQLkeKGPEEEIMLIHSRFTEKDRakkeAELLLEF 270
                        170       180
                 ....*....|....*....|
gi 550794329 295 ANRSASILVATDVAARGLDI 314
Cdd:cd09639  271 KKSEKFVIVATQVIEASLDI 290
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
146-314 3.32e-04

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 42.83  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  146 SLVLDGLATLVLDEADRMLD---MGFQASLEAIVAETPAHrqtLLFSATFSDAVRPLAAALmrDPVGVEVAESHDAGSIH 222
Cdd:TIGR01587 119 TLASIANSLLIFDEVHFYDEytlALILAVLEVLKDNDVPI---LLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRF 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  223 ERV---YRVAD--GDQARLEALSRLLLhlRPASSVVFCNTKRETDEVAQAL--DAAGFSALALHGDLEQADRDR-----L 290
Cdd:TIGR01587 194 ENHrfiLIESDkvGEISSLERLLEFIK--KGGSIAIIVNTVDRAQEFYQQLkeKAPEEEIILYHSRFTEKDRAKkeaelL 271
                         170       180
                  ....*....|....*....|....
gi 550794329  291 LVLFANRSASILVATDVAARGLDI 314
Cdd:TIGR01587 272 REMKKSNEKFVIVATQVIEASLDI 295
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
35-160 4.35e-04

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: 41.48  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  35 QAESLPPILAgRDVIARARTGSGKT--AAFG---LGLLSRLDLASFRVQgLVLCPTRELADQVASELRRLArtlpNVKVL 109
Cdd:cd18034    7 QLELFEAALK-RNTIVVLPTGSGKTliAVMLikeMGELNRKEKNPKKRA-VFLVPTVPLVAQQAEAIRSHT----DLKVG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 550794329 110 TLCGGApfGPQLASLAH------GAHLVVGTPGRIEEHLRKGSLVLDGLATLVLDEA 160
Cdd:cd18034   81 EYSGEM--GVDKWTKERwkeeleKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
PRK13766 PRK13766
Hef nuclease; Provisional
54-162 7.59e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 42.17  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  54 TGSGKTAAFGLGLLSRLDLASFRVqgLVLCPTRELADQVASELRRlARTLPNVKVLTLCGGAPfgP-QLASLAHGAHLVV 132
Cdd:PRK13766  38 TGLGKTAIALLVIAERLHKKGGKV--LILAPTKPLVEQHAEFFRK-FLNIPEEKIVVFTGEVS--PeKRAELWEKAKVIV 112
                         90       100       110
                 ....*....|....*....|....*....|
gi 550794329 133 GTPGRIEEHLRKGSLVLDGLATLVLDEADR 162
Cdd:PRK13766 113 ATPQVIENDLIAGRISLEDVSLLIFDEAHR 142
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
242-305 1.33e-03

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 39.07  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550794329 242 LLLHLRPASSV-VFCNTKRETDEVAQALDAAGFsalaLHGDLEQADRDRLLVLFANRSASILVAT 305
Cdd:cd18795   36 KIETVSEGKPVlVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVAT 96
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
45-159 1.59e-03

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: 39.10  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329  45 GRDVIARARTGSGKTAAFGLGLLSRL-DLASFRVQGLVLCPTRELADQVASELRRLARTL-PNVKVLTLCGGAPFGPQLA 122
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIdLEIPVAVRHGDTSQSEKAK 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 550794329 123 SLAHGAHLVVGTPGRIEEHL--RKGSLVLDGLATLVLDE 159
Cdd:cd17922   81 QLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
240-345 3.19e-03

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: 38.01  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550794329 240 SRLLLHLRPASSVVFCNTKRETDEVAQAL-DAAGFSALAL-----HGDLEQADRDRLLVLFANRSASILVATDVAARGLD 313
Cdd:cd18796   30 EVIFLLERHKSTLVFTNTRSQAERLAQRLrELCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
                         90       100       110
                 ....*....|....*....|....*....|..
gi 550794329 314 IAELDAVFNYHIARELEVHVHRVGRTGRAGSA 345
Cdd:cd18796  110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPGA 141
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
294-341 4.84e-03

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 37.34  E-value: 4.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 550794329 294 FANRSASILVATDVAARGLDIAELDAVFNYHIARELEVHVHRVGRTGR 341
Cdd:cd18801   86 FRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
42-116 5.77e-03

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: 38.08  E-value: 5.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550794329  42 ILAGRDVIARARTGSGKTAafgLGLLSRLDLASFRVQGLVLCPTRELADQVASELRRLAR-TLPNVKVLTLCGGAP 116
Cdd:cd17924   29 LLRGKSFAIIAPTGVGKTT---FGLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEkAGVEVKILVYHSRLK 101
PRK13767 PRK13767
ATP-dependent helicase; Provisional
28-70 6.11e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 39.10  E-value: 6.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 550794329  28 FTAMTPIQAESLPPILAGRDVIARARTGSGKT-AAFgLGLLSRL 70
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDEL 72
 
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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