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Conserved domains on  [gi|330443505|ref|NP_010253|]
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putative ATP-dependent RNA helicase DBP10 [Saccharomyces cerevisiae S288C]

Protein Classification

DEADc_DDX54 and SF2_C_DEAD domain-containing protein( domain architecture ID 13028811)

protein containing domains DEADc_DDX54, SF2_C_DEAD, and DBP10CT

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
137-341 2.79e-139

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: 415.16  E-value: 2.79e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 137 GSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGARAVILSPS 216
Cdd:cd17959    1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 217 RELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:cd17959   81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17959  161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
138-555 9.72e-128

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 393.36  E-value: 9.72e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKiGARAVILSPSR 217
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKvEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:COG0513   82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLdLIE-RGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEMLFLSSKNADREANLLYILqeii 376
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL---- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 377 kiplatseqlqklqnsnneadsdsDDENDRQkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYISQLLRDCG 456
Cdd:COG0513  237 ------------------------RDEDPER---------------------------AIVFCNTKRGADRLAEKLQKRG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 457 YLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIV 536
Cdd:COG0513  266 ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV 345
                        410
                 ....*....|....*....
gi 330443505 537 AENELPYLLDLELFLGKKI 555
Cdd:COG0513  346 TPDERRLLRAIEKLIGQKI 364
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
820-880 2.29e-20

DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of hypothetical RNA helicases.


:

Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 85.80  E-value: 2.29e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443505  820 DLNSDDKVQVHKQT---ATVKWDKKRKKYVNTQGI--DNKKYIIGESGQKIAASFRSGRFDDWSKA 880
Cdd:pfam08147   1 DLTGDDGQELNQQKqvqKKMRWDKKKKKFVKRSGNdeDGKKKIRTESGVKIPASYKSGRYDEWKKK 66
 
Name Accession Description Interval E-value
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
137-341 2.79e-139

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: 415.16  E-value: 2.79e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 137 GSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGARAVILSPS 216
Cdd:cd17959    1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 217 RELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:cd17959   81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17959  161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
138-555 9.72e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 393.36  E-value: 9.72e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKiGARAVILSPSR 217
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKvEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:COG0513   82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLdLIE-RGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEMLFLSSKNADREANLLYILqeii 376
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL---- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 377 kiplatseqlqklqnsnneadsdsDDENDRQkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYISQLLRDCG 456
Cdd:COG0513  237 ------------------------RDEDPER---------------------------AIVFCNTKRGADRLAEKLQKRG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 457 YLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIV 536
Cdd:COG0513  266 ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV 345
                        410
                 ....*....|....*....
gi 330443505 537 AENELPYLLDLELFLGKKI 555
Cdd:COG0513  346 TPDERRLLRAIEKLIGQKI 364
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-555 6.52e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 253.96  E-value: 6.52e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKShsGKIGARAVILSPSR 217
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV--KRFRVQALVLCPTR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVL-LTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEmNLDLKSVEYVVFDEADRLFE 295
Cdd:PRK11776  83 ELADQVAKEIRRLARFIPNIKVLtLCGGVPMGPQIDSLEHGAHIIVGTPGRILdHLRKG-TLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 296 MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSEnLEMLFLSSKNADREANLLYILQei 375
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLL-- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 376 ikiplatseqlqklqnsnneadsdsddendrqkkrrnfkkeKFRkqkmPAanelpsekATILFVPTRHHVEYISQLLRDC 455
Cdd:PRK11776 239 -----------------------------------------HHQ----PE--------SCVVFCNTKKECQEVADALNAQ 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 456 GYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSI 535
Cdd:PRK11776 266 GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSL 345
                        410       420
                 ....*....|....*....|
gi 330443505 536 VAENELPYLLDLELFLGKKI 555
Cdd:PRK11776 346 VAPEEMQRANAIEDYLGRKL 365
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
138-565 1.24e-61

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 220.21  E-value: 1.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIG-----ARAVI 212
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 213 LSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEAD 291
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHACEICVLDEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 292 RLFEMGFQEQLNELLASLP--TTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETkvsenlemlflssKNADREANLL 369
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETET-------------ITAARVRQRI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 370 YILQEIIKIPLAtseqLQKLQNSnneadsdsddENDRqkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYIS 449
Cdd:PRK04537 237 YFPADEEKQTLL----LGLLSRS----------EGAR----------------------------TMVFVNTKAFVERVA 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 450 QLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNK 529
Cdd:PRK04537 275 RTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEE 354
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 330443505 530 GWAYSIVAENELPYLLDLELFLGKKILLTPMYDSLV 565
Cdd:PRK04537 355 GDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELL 390
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
161-329 6.47e-61

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: 204.78  E-value: 6.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  161 TPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRELAMQTFNVFKDFARGTELRSVL 240
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGP--QALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  241 LTGGDSLEEQFGMMmTNPDVIIATPGRFLHLKVEMNLdLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTLLFSA 320
Cdd:pfam00270  79 LLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 330443505  321 TLPNSLVDF 329
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
152-353 2.40e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 181.92  E-value: 2.40e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   152 IKRKGFRQPTPIQRKTIPLILQS-RDIVGMARTGSGKTAAFILPMVEKLKSHSGKigaRAVILSPSRELAMQTFNVFKDF 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG---RVLVLVPTRELAEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   231 ARGTELRSVLLTGGDSLEEQF-GMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASL 309
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLrKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 330443505   310 PTTRQTLLFSATLPNSLVDFVKAGLVNPvlVRLDAETKVSENLE 353
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIE 199
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
406-536 1.16e-42

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: 151.51  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 406 RQKKRRNFKKEKFRKQKMPAANELPSEKaTILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSI 485
Cdd:cd18787    2 KQLYVVVEEEEKKLLLLLLLLEKLKPGK-AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330443505 486 LVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIV 536
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
435-527 1.89e-23

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: 96.13  E-value: 1.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  435 TILFVPTRHHVEyISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSK 514
Cdd:pfam00271  18 VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPA 96
                          90
                  ....*....|...
gi 330443505  515 IFVHRVGRTARAG 527
Cdd:pfam00271  97 SYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
446-527 2.23e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 2.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   446 EYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTAR 525
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 330443505   526 AG 527
Cdd:smart00490  81 AG 82
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
820-880 2.29e-20

DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of hypothetical RNA helicases.


Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 85.80  E-value: 2.29e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443505  820 DLNSDDKVQVHKQT---ATVKWDKKRKKYVNTQGI--DNKKYIIGESGQKIAASFRSGRFDDWSKA 880
Cdd:pfam08147   1 DLTGDDGQELNQQKqvqKKMRWDKKKKKFVKRSGNdeDGKKKIRTESGVKIPASYKSGRYDEWKKK 66
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
152-324 3.45e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 63.76  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPLILQSRDIVGM-ARTGSGKTAAFILPMVEKLKShsgkiGARAVILSPSRELAMQTFNVFKDF 230
Cdd:COG1204   15 LKERGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILKALLN-----GGKALYIVPLRALASEKYREFKRD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 231 ARGTELRSVLLTGG-DSLEEQFGmmmtNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEA------DR--LFEMgfqeQ 301
Cdd:COG1204   90 FEELGIKVGVSTGDyDSDDEWLG----RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSRgpTLEV----L 161
                        170       180
                 ....*....|....*....|...
gi 330443505 302 LNELLASLPTTrQTLLFSATLPN 324
Cdd:COG1204  162 LARLRRLNPEA-QIVALSATIGN 183
 
Name Accession Description Interval E-value
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
137-341 2.79e-139

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: 415.16  E-value: 2.79e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 137 GSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGARAVILSPS 216
Cdd:cd17959    1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 217 RELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:cd17959   81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17959  161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
138-555 9.72e-128

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 393.36  E-value: 9.72e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKiGARAVILSPSR 217
Cdd:COG0513    3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKvEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:COG0513   82 ELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLdLIE-RGALDLSGVETLVLDEADRMLDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEMLFLSSKNADREANLLYILqeii 376
Cdd:COG0513  161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL---- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 377 kiplatseqlqklqnsnneadsdsDDENDRQkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYISQLLRDCG 456
Cdd:COG0513  237 ------------------------RDEDPER---------------------------AIVFCNTKRGADRLAEKLQKRG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 457 YLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIV 536
Cdd:COG0513  266 ISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV 345
                        410
                 ....*....|....*....
gi 330443505 537 AENELPYLLDLELFLGKKI 555
Cdd:COG0513  346 TPDERRLLRAIEKLIGQKI 364
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
148-341 2.28e-83

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 267.39  E-value: 2.28e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGA--RAVILSPSRELAMQTFN 225
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgpQALVLAPTRELAMQIAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 226 VFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNEL 305
Cdd:cd00268   81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 330443505 306 LASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd00268  161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-555 6.52e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 253.96  E-value: 6.52e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKShsGKIGARAVILSPSR 217
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV--KRFRVQALVLCPTR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVL-LTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEmNLDLKSVEYVVFDEADRLFE 295
Cdd:PRK11776  83 ELADQVAKEIRRLARFIPNIKVLtLCGGVPMGPQIDSLEHGAHIIVGTPGRILdHLRKG-TLDLDALNTLVLDEADRMLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 296 MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSEnLEMLFLSSKNADREANLLYILQei 375
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYEVSPDERLPALQRLLL-- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 376 ikiplatseqlqklqnsnneadsdsddendrqkkrrnfkkeKFRkqkmPAanelpsekATILFVPTRHHVEYISQLLRDC 455
Cdd:PRK11776 239 -----------------------------------------HHQ----PE--------SCVVFCNTKKECQEVADALNAQ 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 456 GYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSI 535
Cdd:PRK11776 266 GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSL 345
                        410       420
                 ....*....|....*....|
gi 330443505 536 VAENELPYLLDLELFLGKKI 555
Cdd:PRK11776 346 VAPEEMQRANAIEDYLGRKL 365
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
139-591 1.91e-74

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 252.17  E-value: 1.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL----KSHSGKigARAVILS 214
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGP--PRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 215 PSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLF 294
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 295 EMGFQEQLNELLASLPTTRQTLLFSATLPNSLV-DFVKAGLVNPVLVrlDAETKVSEN---LEMLFLSSKNADREANLLY 370
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDAVqDFAERLLNDPVEV--EAEPSRRERkkiHQWYYRADDLEHKTALLCH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 371 ILQEiikiplatsEQLQKlqnsnneadsdsddendrqkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYISQ 450
Cdd:PRK11192 239 LLKQ---------PEVTR----------------------------------------------SIVFVRTRERVHELAG 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 451 LLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKG 530
Cdd:PRK11192 264 WLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKG 343
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443505 531 WAYSIVAENELPYLLDLELFLGKKIlltpmydslvdvmKKRWIDEGKPEYQFQPPKLSYTK 591
Cdd:PRK11192 344 TAISLVEAHDHLLLGKIERYIEEPL-------------KARVIDELRPKTKAPSEKKTGKP 391
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
138-555 5.20e-72

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 246.26  E-value: 5.20e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHS----GKIGARAVIL 213
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakGRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 214 SPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRL 293
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 294 FEMGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEM-LFLSSKNADREanllyIL 372
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQhVHFVDKKRKRE-----LL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 373 QEIIkiplatseqlqklqnsnneadsdsddendrqkKRRNFKKekfrkqkmpaanelpsekaTILFVPTRHHVEYISQLL 452
Cdd:PRK10590 237 SQMI--------------------------------GKGNWQQ-------------------VLVFTRTKHGANHLAEQL 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 453 RDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWA 532
Cdd:PRK10590 266 NKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEA 345
                        410       420
                 ....*....|....*....|...
gi 330443505 533 YSIVAENELPYLLDLELFLGKKI 555
Cdd:PRK10590 346 LSLVCVDEHKLLRDIEKLLKKEI 368
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
156-341 9.38e-69

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: 227.52  E-value: 9.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 156 GFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGA-RAVILSPSRELAMQTFNVFKDFARGT 234
Cdd:cd17947    9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAAtRVLVLVPTRELAMQCFSVLQQLAQFT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 235 ELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTR 313
Cdd:cd17947   89 DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRLCPRTR 168
                        170       180
                 ....*....|....*....|....*...
gi 330443505 314 QTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17947  169 QTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
148-340 1.05e-64

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: 216.69  E-value: 1.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGARAVILSPSRELAMQTFNVF 227
Cdd:cd17957    1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 228 KDFARGTELRSVLLTGGDSLEEQFGMMM-TNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELL 306
Cdd:cd17957   81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 330443505 307 ASLPTTR-QTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17957  161 AACTNPNlQRSLFSATIPSEVEELARSVMKDPIRI 195
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
148-341 3.44e-63

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: 212.44  E-value: 3.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL---KSHSGKIGARAVILSPSRELAMQTF 224
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQVGALIISPTRELATQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 225 NVFKDFAR--GTELRSVLLTGGDSLEEQFGM-MMTNPDVIIATPGRFLHL--KVEMNLDLKSVEYVVFDEADRLFEMGFQ 299
Cdd:cd17960   81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKfKRNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 330443505 300 EQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17960  161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
138-565 1.24e-61

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 220.21  E-value: 1.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIG-----ARAVI 212
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedPRALI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 213 LSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEAD 291
Cdd:PRK04537  90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHACEICVLDEAD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 292 RLFEMGFQEQLNELLASLP--TTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETkvsenlemlflssKNADREANLL 369
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETET-------------ITAARVRQRI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 370 YILQEIIKIPLAtseqLQKLQNSnneadsdsddENDRqkkrrnfkkekfrkqkmpaanelpsekaTILFVPTRHHVEYIS 449
Cdd:PRK04537 237 YFPADEEKQTLL----LGLLSRS----------EGAR----------------------------TMVFVNTKAFVERVA 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 450 QLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNK 529
Cdd:PRK04537 275 RTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEE 354
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 330443505 530 GWAYSIVAENELPYLLDLELFLGKKILLTPMYDSLV 565
Cdd:PRK04537 355 GDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELL 390
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
161-329 6.47e-61

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: 204.78  E-value: 6.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  161 TPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRELAMQTFNVFKDFARGTELRSVL 240
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGP--QALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  241 LTGGDSLEEQFGMMmTNPDVIIATPGRFLHLKVEMNLdLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTLLFSA 320
Cdd:pfam00270  79 LLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 330443505  321 TLPNSLVDF 329
Cdd:pfam00270 157 TLPRNLEDL 165
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
152-340 1.46e-60

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: 205.22  E-value: 1.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSH--SGKIGARAVILSPSRELAMQTFNVFKD 229
Cdd:cd17941    5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwTPEDGLGALIISPTRELAMQIFEVLRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 230 FARGTELRSVLLTGGDSLEEQfGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLAS 308
Cdd:cd17941   85 VGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVEN 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 330443505 309 LPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17941  164 LPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
136-571 1.83e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 211.69  E-value: 1.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 136 KGSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL-------KSHSGKigA 208
Cdd:PRK01297  86 KTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGE--P 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 209 RAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTN-PDVIIATPGRFLHLKVEMNLDLKSVEYVVF 287
Cdd:PRK01297 164 RALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 288 DEADRLFEMGFQEQLNELLASLP--TTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEmlflssknadre 365
Cdd:PRK01297 244 DEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVE------------ 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 366 anllyilQEIIKIplATSEQLQKLQNsnneadsdsddendrqkkrrnfkkekfrkqkmpAANELPSEKATIlFVPTRHHV 445
Cdd:PRK01297 312 -------QHVYAV--AGSDKYKLLYN---------------------------------LVTQNPWERVMV-FANRKDEV 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 446 EYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTAR 525
Cdd:PRK01297 349 RRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGR 428
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 330443505 526 AGNKGWAYSIVAENELPYLLDLELFLGKKILL-TPMYDSLVDVMKKR 571
Cdd:PRK01297 429 AGASGVSISFAGEDDAFQLPEIEELLGRKISCeMPPAELLKPVPRKH 475
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
139-563 7.65e-59

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 208.29  E-value: 7.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIG-----ARAVIL 213
Cdd:PRK04837  10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqPRALIM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 214 SPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRL 293
Cdd:PRK04837  90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 294 FEMGFQEQLNELLASLP--TTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENL-EMLFLSSkNADREANLLY 370
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIkEELFYPS-NEEKMRLLQT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 371 ILQEiikiplatseqlqklqnsnneadsdsddendrqkkrrnfkkekfrkqkmpaanELPsEKAtILFVPTRHHVEYISQ 450
Cdd:PRK04837 249 LIEE-----------------------------------------------------EWP-DRA-IIFANTKHRCEEIWG 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 451 LLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKG 530
Cdd:PRK04837 274 HLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASG 353
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 330443505 531 WAYSIVAENelpYLLDL---ELFLGKKILLTPmYDS 563
Cdd:PRK04837 354 HSISLACEE---YALNLpaiETYIGHSIPVSK-YDS 385
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
138-340 3.87e-58

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: 198.31  E-value: 3.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHsgKIGARAVILSPSR 217
Cdd:cd17954    1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN--PQRFFALVLAPTR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEADRLFEM 296
Cdd:cd17954   79 ELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLLNM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 330443505 297 GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17954  159 DFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
138-323 5.69e-57

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: 195.78  E-value: 5.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL--------KSHSGKIGAR 209
Cdd:cd17967    1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAYPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 210 AVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLkVEMN-LDLKSVEYVVFD 288
Cdd:cd17967   81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDF-IERGrISLSSIKFLVLD 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 330443505 289 EADRLFEMGFQEQLNELLA--SLPTT--RQTLLFSATLP 323
Cdd:cd17967  160 EADRMLDMGFEPQIRKIVEhpDMPPKgeRQTLMFSATFP 198
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
148-340 1.93e-55

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: 191.38  E-value: 1.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVE------KLKSHSGKIGARAVILSPSRELAM 221
Cdd:cd17945    1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisrlpPLDEETKDDGPYALILAPTRELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 222 QTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-----HLKVemnldLKSVEYVVFDEADRLFEM 296
Cdd:cd17945   81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLdclerRLLV-----LNQCTYVVLDEADRMIDM 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443505 297 GFQEQLNELLASLPTT--------------------RQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17945  156 GFEPQVTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
139-339 2.43e-55

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: 190.51  E-value: 2.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSgkIGARAVILSPSRE 218
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP--YGIFALVLTPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLK--VEMNLDLKSVEYVVFDEADRLFE 295
Cdd:cd17955   79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLRssDDTTKVLSRVKFLVLDEADRLLT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 330443505 296 MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVL 339
Cdd:cd17955  159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFF 202
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
143-338 3.66e-55

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: 190.67  E-value: 3.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 143 GLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSH---SGKIGARAVILSPSREL 219
Cdd:cd17953   18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvKPGEGPIGLIMAPTREL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 220 AMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLkVEMN----LDLKSVEYVVFDEADRLFE 295
Cdd:cd17953   98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDI-LTANngrvTNLRRVTYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 330443505 296 MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd17953  177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPI 219
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
138-548 1.05e-53

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 198.92  E-value: 1.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGkiGARAVILSPSR 217
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELK--APQILVLAPTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTE-LRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKvEMNLDLKSVEYVVFDEADRLFE 295
Cdd:PRK11634  85 ELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLdHLK-RGTLDLSKLSGLVLDEADEMLR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 296 MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSENLEMLFLSSKNADREANLLYILqei 375
Cdd:PRK11634 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL--- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 376 ikiplatseqlqklqnsnnEADsDSDdendrqkkrrnfkkekfrkqkmpaanelpsekATILFVPTRHHVEYISQLLRDC 455
Cdd:PRK11634 241 -------------------EAE-DFD--------------------------------AAIIFVRTKNATLEVAEALERN 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 456 GYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSI 535
Cdd:PRK11634 269 GYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
                        410
                 ....*....|...
gi 330443505 536 VAENELPYLLDLE 548
Cdd:PRK11634 349 VENRERRLLRNIE 361
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
148-340 1.84e-52

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: 182.54  E-value: 1.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMV------EKLKSHSGKIGARAVILSPSRELAM 221
Cdd:cd17951    1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 222 QTFNVFKDFARGTE------LRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHL--KVEMNLDLksVEYVVFDEADRL 293
Cdd:cd17951   81 QTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMlnKKKINLDI--CRYLCLDEADRM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 330443505 294 FEMGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17951  159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEXDc smart00487
DEAD-like helicases superfamily;
152-353 2.40e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 181.92  E-value: 2.40e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   152 IKRKGFRQPTPIQRKTIPLILQS-RDIVGMARTGSGKTAAFILPMVEKLKSHSGKigaRAVILSPSRELAMQTFNVFKDF 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG---RVLVLVPTRELAEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   231 ARGTELRSVLLTGGDSLEEQF-GMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASL 309
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLrKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 330443505   310 PTTRQTLLFSATLPNSLVDFVKAGLVNPvlVRLDAETKVSENLE 353
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIE 199
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
152-342 4.13e-52

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: 181.63  E-value: 4.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL---KSHSGKIGA-RAVILSPSRELAMQTFNVF 227
Cdd:cd17961    9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkaKAESGEEQGtRALILVPTRELAQQVSKVL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 228 KDFAR--GTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKS-VEYVVFDEADRLFEMGFQEQLNE 304
Cdd:cd17961   89 EQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEEDLKS 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 330443505 305 LLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRL 342
Cdd:cd17961  169 LLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
PTZ00110 PTZ00110
helicase; Provisional
132-534 4.18e-52

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 192.30  E-value: 4.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 132 TKHKKGSFPSFglskiVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILP-MVEKLKSHSGKIGARA 210
Cdd:PTZ00110 130 VSFEYTSFPDY-----ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRYGDGP 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 211 V--ILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFD 288
Cdd:PTZ00110 205 IvlVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 289 EADRLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAglvnpvlvrLDAETKVSENLEMLFL-SSKNADREan 367
Cdd:PTZ00110 285 EADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARD---------LCKEEPVHVNVGSLDLtACHNIKQE-- 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 368 lLYILQEiikiplatseqlqklqnsnneadsdsddendrQKKRRNFKkeKFRKQKMPAANELpsekatILFVPTRHHVEY 447
Cdd:PTZ00110 354 -VFVVEE--------------------------------HEKRGKLK--MLLQRIMRDGDKI------LIFVETKKGADF 392
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 448 ISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAG 527
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472

                 ....*..
gi 330443505 528 NKGWAYS 534
Cdd:PTZ00110 473 AKGASYT 479
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
148-340 4.08e-51

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: 178.38  E-value: 4.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL---KSHSGKIGARAVILSPSRELAMQTF 224
Cdd:cd17952    1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVIVAPTRELAQQIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 225 NVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNE 304
Cdd:cd17952   81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 330443505 305 LLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17952  161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
139-338 9.98e-50

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 174.41  E-value: 9.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRE 218
Cdd:cd17940    1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVI--QALILVPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFgMMMTNP-DVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMG 297
Cdd:cd17940   79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDI-MRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQD 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 330443505 298 FQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd17940  158 FQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
144-323 1.46e-46

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 165.83  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 144 LSKIVLNNIKRKGFRQPTPIQRKTIPLILQSR-DIVGMARTGSGKTAAFILPMVEKL-----KSHSGKIGAraVILSPSR 217
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSA--LIISPTR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARG-TELRSVLLTGGDSLEEQFGMMMT-NPDVIIATPGRFL-HL-KVEMNLDLKSVEYVVFDEADRL 293
Cdd:cd17964   79 ELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIdHLeNPGVAKAFTDLDYLVLDEADRL 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 330443505 294 FEMGFQEQLNELLASLP----TTRQTLLFSATLP 323
Cdd:cd17964  159 LDMGFRPDLEQILRHLPeknaDPRQTLLFSATVP 192
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
138-324 1.21e-45

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: 165.14  E-value: 1.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIGA-------RA 210
Cdd:cd18052   44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfsevqepQA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 211 VILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEA 290
Cdd:cd18052  124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 330443505 291 DRLFEMGFQEQLNELLASLPTT----RQTLLFSATLPN 324
Cdd:cd18052  204 DRMLDMGFGPEIRKLVSEPGMPskedRQTLMFSATFPE 241
PTZ00424 PTZ00424
helicase 45; Provisional
113-561 1.71e-45

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 169.24  E-value: 1.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 113 TGDDEDDVNEYFSTNNLE-KTKHKKGSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAF 191
Cdd:PTZ00424   3 TSEQKNQSEQVASTGTIEsNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 192 ILPMVEKLKSHSgkIGARAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHL 271
Cdd:PTZ00424  83 VIAALQLIDYDL--NACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 272 KVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAETKVSEN 351
Cdd:PTZ00424 161 IDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 352 LEMLFLSSKNADREANLLYILQEIIKIPLAtseqlqklqnsnneadsdsddendrqkkrrnfkkekfrkqkmpaanelps 431
Cdd:PTZ00424 241 IRQFYVAVEKEEWKFDTLCDLYETLTITQA-------------------------------------------------- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 432 ekatILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPG 511
Cdd:PTZ00424 271 ----IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 330443505 512 SSKIFVHRVGRTARAGNKGWAYSIVAENELPYLLDLELFLGKKILLTPMY 561
Cdd:PTZ00424 347 SPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPME 396
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
148-334 5.15e-45

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: 162.41  E-value: 5.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSR-DIVGMARTGSGKTAAFILPMVEKLKSH-------SGKIGARAVILSPSREL 219
Cdd:cd17946    1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQkssngvgGKQKPLRALILTPTREL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 220 AMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNL---DLKSVEYVVFDEADRLFEM 296
Cdd:cd17946   81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEK 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 297 G-FQE--QLNELLASLPTT----RQTLLFSATLpnSLVDFVKAGL 334
Cdd:cd17946  161 GhFAEleKILELLNKDRAGkkrkRQTFVFSATL--TLDHQLPLKL 203
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
148-323 1.13e-44

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: 159.84  E-value: 1.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMV------EKLKSHSGKIgarAVILSPSRELAM 221
Cdd:cd17966    1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERGDGPI---VLVLAPTRELAQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 222 QTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQ 301
Cdd:cd17966   78 QIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQ 157
                        170       180
                 ....*....|....*....|..
gi 330443505 302 LNELLASLPTTRQTLLFSATLP 323
Cdd:cd17966  158 IRKIVDQIRPDRQTLMWSATWP 179
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
152-340 3.03e-44

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: 158.68  E-value: 3.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVE---KLKsHSGKIGARAVILSPSRELAMQTFNVFK 228
Cdd:cd17942    5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLK-FKPRNGTGVIIISPTRELALQIYGVAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 229 DFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLA 307
Cdd:cd17942   84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 330443505 308 SLPTTRQTLLFSATLPNSLVDFVKAGLVN-PVLV 340
Cdd:cd17942  164 LLPKRRQTMLFSATQTRKVEDLARISLKKkPLYV 197
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
148-340 3.18e-44

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 158.48  E-value: 3.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVekLKSHSGKIGARAVILSPSRELAMQTFNVF 227
Cdd:cd17962    1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI--IRCLTEHRNPSALILTPTRELAVQIEDQA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 228 KDFARGT-ELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELL 306
Cdd:cd17962   79 KELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 330443505 307 ASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17962  159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
406-536 1.16e-42

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: 151.51  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 406 RQKKRRNFKKEKFRKQKMPAANELPSEKaTILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSI 485
Cdd:cd18787    2 KQLYVVVEEEEKKLLLLLLLLEKLKPGK-AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330443505 486 LVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKGWAYSIV 536
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
148-340 1.99e-42

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: 153.39  E-value: 1.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILP----MVEKLKSHSGKIGARAVILSPSRELAMQT 223
Cdd:cd17958    1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihLDLQPIPREQRNGPGVLVLTPTRELALQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 224 FNVFKDFA-RGteLRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQL 302
Cdd:cd17958   81 EAECSKYSyKG--LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 330443505 303 NELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLV 340
Cdd:cd17958  159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
147-341 3.36e-42

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: 153.51  E-value: 3.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 147 IVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKI----GARAVILSPSRELAMQ 222
Cdd:cd17949    1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdGTLALVLVPTRELALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 223 TFNVFKDFARG-TELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDEADRLFEMGFQE 300
Cdd:cd17949   81 IYEVLEKLLKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDMGFEK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330443505 301 QLNELL-------------ASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17949  161 DITKILellddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
148-341 4.65e-42

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: 152.42  E-value: 4.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRELAMQTFNVF 227
Cdd:cd17943    1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHP--QVLILAPTREIAVQIHDVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 228 KDFA-RGTELRSVLLTGGDSLEEQFgMMMTNPDVIIATPGRFLHLkVEMN-LDLKSVEYVVFDEADRLFEMGFQEQLNEL 305
Cdd:cd17943   79 KKIGkKLEGLKCEVFIGGTPVKEDK-KKLKGCHIAVGTPGRIKQL-IELGaLNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 330443505 306 LASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17943  157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
138-540 1.20e-41

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 160.72  E-value: 1.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKS-HSGKIGAR----AVI 212
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPSEQrnplAMV 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 213 LSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADR 292
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 293 LFEMGFQEQLNELLASLPTTrQTLLFSATLPNSLvdfvkaglvnpvlvrldaeTKVSENL--EMLFLSSKNADReanlly 370
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEV-------------------EKFASSLakDIILISIGNPNR------ 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 371 ilqeiikiPLATSEQLQKLQNSnneadsdsddendRQKKRRNFKKEKFRKQKMPAAnelpsekatILFVPTRHHVEYISQ 450
Cdd:PLN00206 336 --------PNKAVKQLAIWVET-------------KQKKQKLFDILKSKQHFKPPA---------VVFVSSRLGADLLAN 385
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 451 LLR-DCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNK 529
Cdd:PLN00206 386 AITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEK 465
                        410
                 ....*....|.
gi 330443505 530 GWAysIVAENE 540
Cdd:PLN00206 466 GTA--IVFVNE 474
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
139-322 1.73e-40

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: 148.24  E-value: 1.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLkshsgkigaRAVILSPSRE 218
Cdd:cd17938    1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV---------VALILEPSRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQT---FNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFE 295
Cdd:cd17938   72 LAEQTyncIENFKKYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 330443505 296 MGFQEQLNELLASLP--TTR----QTLLFSATL 322
Cdd:cd17938  152 QGNLETINRIYNRIPkiTSDgkrlQVIVCSATL 184
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
143-338 2.70e-39

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: 144.77  E-value: 2.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 143 GLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRELAMQ 222
Cdd:cd17939    3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET--QALVLAPTRELAQQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 223 TFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQL 302
Cdd:cd17939   81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 330443505 303 NELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd17939  161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPV 196
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
138-324 3.62e-39

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: 145.95  E-value: 3.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPM---------VEKLKSHSGKIGA 208
Cdd:cd18051   22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIlsqiyeqgpGESLPSESGYYGR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 209 R-----AVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVE 283
Cdd:cd18051  102 RkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 284 YVVFDEADRLFEMGFQEQLNELLA--SLPTT--RQTLLFSATLPN 324
Cdd:cd18051  182 YLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPK 226
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
148-322 2.65e-37

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: 140.07  E-value: 2.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQS---------RDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgARAVILSPSRE 218
Cdd:cd17956    1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPR-LRALIVVPTKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQTFNVFKDFARGTELRSVLLTGGDSL-EEQFGMMMTN-------PDVIIATPGRFL-HLKVEMNLDLKSVEYVVFDE 289
Cdd:cd17956   80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFkKEQKLLLVDTsgrylsrVDILVATPGRLVdHLNSTPGFTLKHLRFLVIDE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443505 290 ADRLFEMGFQEQLNELLASLPTTR--------------------QTLLFSATL 322
Cdd:cd17956  160 ADRLLNQSFQDWLETVMKALGRPTapdlgsfgdanllersvrplQKLLFSATL 212
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
133-331 1.34e-34

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: 132.44  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 133 KHKKGSFPSFglskiVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLkSHSGKI----GA 208
Cdd:cd18049   25 NFYEANFPAN-----VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLergdGP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 209 RAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFD 288
Cdd:cd18049   99 ICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLD 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 330443505 289 EADRLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSL----VDFVK 331
Cdd:cd18049  179 EADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVrqlaEDFLK 225
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
136-326 7.99e-34

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: 131.29  E-value: 7.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 136 KGSFPSFglskiVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLkSHSGKI----GARAV 211
Cdd:cd18050   66 QANFPQY-----VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLergdGPICL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 212 ILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEAD 291
Cdd:cd18050  140 VLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 330443505 292 RLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSL 326
Cdd:cd18050  220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEV 254
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
149-331 4.49e-33

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: 126.89  E-value: 4.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 149 LNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKI----GARAVILSPSRELAMQTF 224
Cdd:cd17944    2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrAPKVLVLAPTRELANQVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 225 NVFKDFARgtELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNE 304
Cdd:cd17944   82 KDFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEE 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 330443505 305 LL-----ASLPTTRQTLLFSATLPNSLVDFVK 331
Cdd:cd17944  160 ILsvsykKDSEDNPQTLLFSATCPDWVYNVAK 191
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
144-341 5.34e-32

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: 123.45  E-value: 5.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 144 LSKIVLNNIKRKGFRQPTPIQRKTIPLILQS--RDIVGMARTGSGKTAAFILPMVEK----LKShsgkigARAVILSPSR 217
Cdd:cd17963    1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRvdptLKS------PQALCLAPTR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 218 ELAMQTFNVFKDFARGTEL------RSVLLTGGDSLEEQfgmmmtnpdVIIATPGRFLHLKVEMNLDLKSVEYVVFDEAD 291
Cdd:cd17963   75 ELARQIGEVVEKMGKFTGVkvalavPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEAD 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330443505 292 RLFEM-GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd17963  146 VMLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
139-338 4.02e-31

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: 121.42  E-value: 4.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPSRE 218
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRET--QALILSPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGF 298
Cdd:cd18045   79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 330443505 299 QEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd18045  159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPI 198
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
148-328 1.59e-30

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: 120.55  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 148 VLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKL----KSHSGKIGA-RAVILSPSRELAMQ 222
Cdd:cd17948    1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykLLAEGPFNApRGLVITPSRELAEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 223 TFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQL 302
Cdd:cd17948   81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 330443505 303 NELLASLP--------TTR-----QTLLFSATLPNSLVD 328
Cdd:cd17948  161 SHFLRRFPlasrrsenTDGldpgtQLVLVSATMPSGVGE 199
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
137-338 2.83e-29

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: 116.29  E-value: 2.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 137 GSFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKIgaRAVILSPS 216
Cdd:cd17950    2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV--SVLVICHT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 217 RELAMQTFNVFKDFARG-TELRSVLLTGGDSLEEQFGMMMTN-PDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLF 294
Cdd:cd17950   80 RELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443505 295 E-MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd17950  160 EqLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPL 204
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
139-338 3.27e-29

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: 115.62  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 139 FPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLkSHSGKiGARAVILSPSRE 218
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLK-ATQALVLAPTRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 219 LAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGF 298
Cdd:cd18046   79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 330443505 299 QEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPV 338
Cdd:cd18046  159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
435-527 1.89e-23

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: 96.13  E-value: 1.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  435 TILFVPTRHHVEyISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSK 514
Cdd:pfam00271  18 VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPA 96
                          90
                  ....*....|...
gi 330443505  515 IFVHRVGRTARAG 527
Cdd:pfam00271  97 SYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
138-345 5.91e-23

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: 98.55  E-value: 5.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQS--RDIVGMARTGSGKTAAFILPMVEKLKSHsgKIGARAVILSP 215
Cdd:cd18048   19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL--KLYPQCLCLSP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 216 SRELAMQTFNVFKD---FARGTE----LRSVLLTGGDSLEEQfgmmmtnpdVIIATPGRFLHLKVEMNL-DLKSVEYVVF 287
Cdd:cd18048   97 TFELALQTGKVVEEmgkFCVGIQviyaIRGNRPGKGTDIEAQ---------IVIGTPGTVLDWCFKLRLiDVTNISVFVL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443505 288 DEADRLFEM-GFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVRLDAE 345
Cdd:cd18048  168 DEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKE 226
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
153-326 2.51e-22

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: 97.45  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 153 KRKGFRQPTPIQRKTIPLILQSRDI----------------VGMARTGSGKTAAFILPMVEKLK---------------- 200
Cdd:cd17965   24 KTDEEIKPSPIQTLAIKKLLKTLMRkvtkqtsneepklevfLLAAETGSGKTLAYLAPLLDYLKrqeqepfeeaeeeyes 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 201 -SHSGKIgaRAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFgMMMTNP---DVIIATPGRFLHL-KVEM 275
Cdd:cd17965  104 aKDTGRP--RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQR-LQLAFKgriDILVTTPGKLASLaKSRP 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330443505 276 NLdLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTLLFSATLPNSL 326
Cdd:cd17965  181 KI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEF 230
HELICc smart00490
helicase superfamily c-terminal domain;
446-527 2.23e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 2.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505   446 EYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTAR 525
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 330443505   526 AG 527
Cdd:smart00490  81 AG 82
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
820-880 2.29e-20

DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of hypothetical RNA helicases.


Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 85.80  E-value: 2.29e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443505  820 DLNSDDKVQVHKQT---ATVKWDKKRKKYVNTQGI--DNKKYIIGESGQKIAASFRSGRFDDWSKA 880
Cdd:pfam08147   1 DLTGDDGQELNQQKqvqKKMRWDKKKKKFVKRSGNdeDGKKKIRTESGVKIPASYKSGRYDEWKKK 66
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
183-547 1.81e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 93.55  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKT--AAFIlpmVEKLKShsgkiGARAVILSPSRELAMQTFNVFKDFARGTElrsvllTGGDSLEEQFgmmmtnpDV 260
Cdd:COG1061  109 TGTGKTvlALAL---AAELLR-----GKRVLVLVPRRELLEQWAEELRRFLGDPL------AGGGKKDSDA-------PI 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 261 IIATPGRfLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEqlneLLASLPTTRqTLLFSATLpnslvdfvkaglvnpvlV 340
Cdd:COG1061  168 TVATYQS-LARRAHLDELGDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATP-----------------F 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 341 RLDAETKVSENLEmlflssknadreaNLLY-------ILQEIIKIP--LATSEQLQKLQNSNNEADSDSDDENDRQKKRr 411
Cdd:COG1061  225 RSDGREILLFLFD-------------GIVYeyslkeaIEDGYLAPPeyYGIRVDLTDERAEYDALSERLREALAADAER- 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 412 nfKKEKFRKqkmpAANELPSEKATILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDV 491
Cdd:COG1061  291 --KDKILRE----LLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDV 364
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443505 492 AARGVDIPMLANVINYTLPGSSKIFVHRVGRTAR-AGNKGWA--YSIVAeNELPYLLDL 547
Cdd:COG1061  365 LNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRpAPGKEDAlvYDFVG-NDVPVLEEL 422
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
138-341 1.61e-18

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: 85.16  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 138 SFPSFGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQS--RDIVGMARTGSGKTAAFILPMVEKLKSHSGkiGARAVILSP 215
Cdd:cd18047    2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANK--YPQCLCLSP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 216 SRELAMQTFNVFKDFAR-GTELRSVLLTGGDSLEEqfGMMMTNpDVIIATPGRFLHLKVEMNL-DLKSVEYVVFDEADRL 293
Cdd:cd18047   80 TYELALQTGKVIEQMGKfYPELKLAYAVRGNKLER--GQKISE-QIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVM 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 330443505 294 FE-MGFQEQLNELLASLPTTRQTLLFSATLPNSLVDFVKAGLVNPVLVR 341
Cdd:cd18047  157 IAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
161-324 2.99e-15

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: 74.99  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 161 TPIQRKTIPLILQSRDIVGM-ARTGSGKTAAFILPMVEKLKSHsgkiGARAVILSPSRELAMQTFNVFKDFARGTELRSV 239
Cdd:cd17921    3 NPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATS----GGKAVYIAPTRALVNQKEADLRERFGPLGKNVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 240 LLTGGDSLeeqFGMMMTNPDVIIATPGRF-LHLKVEMNLDLKSVEYVVFDEA---------DRLfemgfQEQLNELLASL 309
Cdd:cd17921   79 LLTGDPSV---NKLLLAEADILVATPEKLdLLLRNGGERLIQDVRLVVVDEAhligdgergVVL-----ELLLSRLLRIN 150
                        170
                 ....*....|....*
gi 330443505 310 PTTRQTLLfSATLPN 324
Cdd:cd17921  151 KNARFVGL-SATLPN 164
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
183-321 6.40e-15

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: 72.82  E-value: 6.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKTAAFILPMVEKLKSHsgkiGARAVILSPSRELAMQTFNVFKDFARGtELRSVLLTGGDSLEEQFGMMMTNPDVII 262
Cdd:cd00046   10 TGSGKTLAALLAALLLLLKK----GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKLGDADIII 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330443505 263 ATPGRFLHLKVEMN-LDLKSVEYVVFDEADRL----FEMGFQEQLNELLASLPTtrQTLLFSAT 321
Cdd:cd00046   85 ATPDMLLNLLLREDrLFLKDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNA--QVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
183-539 1.39e-12

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 71.68  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKTAAFILPMVEKLKSHSGKIgaraVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQfGMMMTNPDVII 262
Cdd:COG1111   26 TGLGKTAVALLVIAERLHKKGGKV----LFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKR-KELWEKARIIV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 263 ATPGRFLHLKVEMNLDLKSVEYVVFDE-------------ADRLFE-------MGF-------QEQLNELLASL------ 309
Cdd:COG1111  101 ATPQVIENDLIAGRIDLDDVSLLIFDEahravgnyayvyiAERYHEdakdpliLGMtaspgsdEEKIEEVCENLgienve 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 310 ----------PTTRQTLL--FSATLPNSLVDFVKagLVNPV-------LVRLDAETKVSENL---EML----FLSSKNAD 363
Cdd:COG1111  181 vrteedpdvaPYVHDTEVewIRVELPEELKEIRD--LLNEVlddrlkkLKELGVIVSTSPDLskkDLLalqkKLQRRIRE 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 364 REANL---LYILQEIIKIPLAT-------SEQLQK-LQNSNNEADSDS---------DDENDRQ--KKRRNFKKE--KFR 419
Cdd:COG1111  259 DDSEGyraISILAEALKLRHALelletqgVEALLRyLERLEEEARSSGgskaskrlvSDPRFRKamRLAEEADIEhpKLS 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 420 KQKMPAANEL---PSEKAtILFVPTRHHVEYISQLLRDCGYLISYIYG--------TLDQHARKRQLYNFRAGLTSILVV 488
Cdd:COG1111  339 KLREILKEQLgtnPDSRI-IVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVA 417
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 330443505 489 TDVAARGVDIPMLANVINYTlPGSSKI-FVHRVGRTARaGNKGWAYSIVAEN 539
Cdd:COG1111  418 TSVAEEGLDIPEVDLVIFYE-PVPSEIrSIQRKGRTGR-KREGRVVVLIAKG 467
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
152-324 3.45e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 63.76  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPLILQSRDIVGM-ARTGSGKTAAFILPMVEKLKShsgkiGARAVILSPSRELAMQTFNVFKDF 230
Cdd:COG1204   15 LKERGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILKALLN-----GGKALYIVPLRALASEKYREFKRD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 231 ARGTELRSVLLTGG-DSLEEQFGmmmtNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEA------DR--LFEMgfqeQ 301
Cdd:COG1204   90 FEELGIKVGVSTGDyDSDDEWLG----RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSRgpTLEV----L 161
                        170       180
                 ....*....|....*....|...
gi 330443505 302 LNELLASLPTTrQTLLFSATLPN 324
Cdd:COG1204  162 LARLRRLNPEA-QIVALSATIGN 183
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
137-290 6.02e-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: 63.32  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 137 GSFPSfGLSKIVLNNIKRKGFRQPTPIQRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSgkiGARAVILSPS 216
Cdd:COG1205   35 APWPD-WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP---GATALYLYPT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 217 RELA---MQTFNVFKDFArGTELRSVLLTgGDSLEEQFGMMMTNPDVIIATPGrFLHLKVemnLD--------LKSVEYV 285
Cdd:COG1205  111 KALArdqLRRLRELAEAL-GLGVRVATYD-GDTPPEERRWIREHPDIVLTNPD-MLHYGL---LPhhtrwarfFRNLRYV 184

                 ....*
gi 330443505 286 VFDEA 290
Cdd:COG1205  185 VIDEA 189
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
164-290 1.50e-09

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 58.37  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 164 QRKTIPLILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSgkiGARAVILSPSRELAMQTFNVFKDFAR--GTELRSVLL 241
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP---GSRALYLYPTKALAQDQLRSLRELLEqlGLGIRVATY 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330443505 242 TGGDSLEEQFGMMMTNPDVIIATPgRFLHLKVEMNLD-----LKSVEYVVFDEA 290
Cdd:cd17923   82 DGDTPREERRAIIRNPPRILLTNP-DMLHYALLPHHDrwarfLRNLRYVVLDEA 134
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
435-528 2.48e-09

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 56.83  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 435 TILFVPTRHHVEYISQLLRD---------CGYLI---SYIYGTLDQHARKRQ---LYNFRAGLTSILVVTDVAARGVDIP 499
Cdd:cd18802   28 GIIFVERRATAVVLSRLLKEhpstlafirCGFLIgrgNSSQRKRSLMTQRKQketLDKFRDGELNLLIATSVLEEGIDVP 107
                         90       100
                 ....*....|....*....|....*....
gi 330443505 500 MLANVINYTLPGSSKIFVHRVGRtARAGN 528
Cdd:cd18802  108 ACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
PRK13766 PRK13766
Hef nuclease; Provisional
183-292 3.13e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 57.58  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKTAAFILPMVEKLKSHSGKIgaraVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMtNPDVII 262
Cdd:PRK13766  38 TGLGKTAIALLVIAERLHKKGGKV----LILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKRAELWE-KAKVIV 112
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330443505 263 ATP---------GRflhlkvemnLDLKSVEYVVFDEADR 292
Cdd:PRK13766 113 ATPqviendliaGR---------ISLEDVSLLIFDEAHR 142
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
417-536 6.18e-08

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 53.02  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 417 KFRKQKMPAANELPSEKaTILFVPTRHHVEYISQLLrdcgyLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGV 496
Cdd:cd18789   35 KLRALEELLKRHEQGDK-IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 330443505 497 DIPMlANV---INYTLpGSSKIFVHRVGRTARAGNKGWA----YSIV 536
Cdd:cd18789  109 DLPE-ANVaiqISGHG-GSRRQEAQRLGRILRPKKGGGKnaffYSLV 153
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
175-290 7.80e-08

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: 53.81  E-value: 7.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 175 RDIVGMARTGSGKTaaFILPMVEKLKSHSGKI----GARAVILSPSRELAMQTFNVFKDFargTELRSVLLTGGDSLEEQ 250
Cdd:cd18034   17 RNTIVVLPTGSGKT--LIAVMLIKEMGELNRKeknpKKRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKW 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 330443505 251 FGMM----MTNPDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEA 290
Cdd:cd18034   92 TKERwkeeLEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
183-292 8.12e-08

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 53.59  E-value: 8.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKTAAFILPMVEKLKSHSGKIGARAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQFGMMMTNPDVII 262
Cdd:cd17927   26 TGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVEQIVESSDVII 105
                         90       100       110
                 ....*....|....*....|....*....|.
gi 330443505 263 ATPGRFLH-LKVEMNLDLKSVEYVVFDEADR 292
Cdd:cd17927  106 VTPQILVNdLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
152-326 4.19e-07

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: 51.26  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRqPTPIQRKTIPLILQS------RDIVGMARTGSGKTAAFILPMVEKLKShsgkiGARAVILSPSRELAMQTFN 225
Cdd:cd17918    9 CKSLPFS-LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKN-----GKQVAILVPTEILAHQHYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 226 VFKDFArgTELRSVLLTGGdsLEEQFGmmmTNPDVIIATPGrFLHLKV-EMNLDLksveyVVFDEADRlFEMGFQEQLNE 304
Cdd:cd17918   83 EARKFL--PFINVELVTGG--TKAQIL---SGISLLVGTHA-LLHLDVkFKNLDL-----VIVDEQHR-FGVAQREALYN 148
                        170       180
                 ....*....|....*....|...
gi 330443505 305 LLASlpttrQTLLFSAT-LPNSL 326
Cdd:cd17918  149 LGAT-----HFLEATATpIPRTL 166
PRK00254 PRK00254
ski2-like helicase; Provisional
152-341 4.79e-07

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 53.67  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 152 IKRKGFRQPTPIQRKTIPL-ILQSRDIVGMARTGSGKTAAFILPMVEKLKSHSGKigarAVILSPSRELAMQTFNVFKDF 230
Cdd:PRK00254  16 LKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGK----AVYLVPLKALAEEKYREFKDW 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 231 ARgTELRSVLLTGG-DSLEEQFGMMmtnpDVIIATPGRFLHLKVEMNLDLKSVEYVVFDEADRLFEMGFQEQLNELLASL 309
Cdd:PRK00254  92 EK-LGLRVAMTTGDyDSTDEWLGKY----DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHM 166
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 330443505 310 PTTRQTLLFSATL--PNSLVDFVKAGLV----NPVLVR 341
Cdd:PRK00254 167 LGRAQILGLSATVgnAEELAEWLNAELVvsdwRPVKLR 204
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
163-268 1.35e-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: 50.05  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 163 IQRKTIPLILQS-RDIVGMARTGSGKTAAFILPMVEKLKSHSGK--IGARAVILSPSRELAMQTFNVFKDFARGTELRSV 239
Cdd:cd18023    5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLpwGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
                         90       100
                 ....*....|....*....|....*....
gi 330443505 240 LLTGGDSLEEQFGmmMTNPDVIIATPGRF 268
Cdd:cd18023   85 ELTGDTEMDDTFE--IQDADIILTTPEKW 111
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
432-532 1.74e-06

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: 48.36  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 432 EKATILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTdVA-ARGVDIPMLANVINYTLP 510
Cdd:cd18794   30 GGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRFVIHYSLP 108
                         90       100
                 ....*....|....*....|..
gi 330443505 511 GSSKIFVHRVGRTARAGNKGWA 532
Cdd:cd18794  109 KSMESYYQESGRAGRDGLPSEC 130
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
183-292 5.80e-06

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: 47.89  E-value: 5.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 183 TGSGKTAAFILPMVEKLKSHSGKIgaraVILSPSRELAMQTFNVFKDFARgTELRSVLLTGGDSLEEQfGMMMTNPDVII 262
Cdd:cd18035   25 TGLGKTIIAILVAADRLTKKGGKV----LILAPSRPLVEQHAENLKRVLN-IPDKITSLTGEVKPEER-AERWDASKIIV 98
                         90       100       110
                 ....*....|....*....|....*....|
gi 330443505 263 ATPGRFLHLKVEMNLDLKSVEYVVFDEADR 292
Cdd:cd18035   99 ATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
173-322 2.54e-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: 45.37  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 173 QSRDIVGMArTGSGKTaAFILPMVEKLKSHsgkigaRAVILSPSRELAMQTFNVFKDFargTELRSVLLTGGDSLEEQFG 252
Cdd:cd17926   18 NRRGILVLP-TGSGKT-LTALALIAYLKEL------RTLIVVPTDALLDQWKERFEDF---LGDSSIGLIGGGKKKDFDD 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330443505 253 MmmtnpDVIIATP-GRFLHLKVEMNLdLKSVEYVVFDEADRLFEMGFQEQLNELLASLpttrqTLLFSATL 322
Cdd:cd17926   87 A-----NVVVATYqSLSNLAEEEKDL-FDQFGLLIVDEAHHLPAKTFSEILKELNAKY-----RLGLTATP 146
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
162-324 2.69e-05

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 45.79  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 162 PIQRKTI-PLILQSRDIVGMARTGSGKTAAFILPMVEKLKShsgkiGARAVILSPSRELAMQTFNVFKDFaRGTELRsVL 240
Cdd:cd18028    4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE-----GGKALYLVPLRALASEKYEEFKKL-EEIGLK-VG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 241 LTGGDSLEEQFGmmMTNPDVIIATPGRFLHL-KVEMNLdLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTT---RQTL 316
Cdd:cd18028   77 ISTGDYDEDDEW--LGDYDIIVATYEKFDSLlRHSPSW-LRDVGVVVVDEIHLISDEERGPTLESIVARLRRLnpnTQII 153

                 ....*...
gi 330443505 317 LFSATLPN 324
Cdd:cd18028  154 GLSATIGN 161
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
484-530 4.08e-05

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: 42.69  E-value: 4.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 330443505 484 SILVVTDVAARGVDIPMLANVINYTLPGSSKIFVHRVGRTARAGNKG 530
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
181-289 2.50e-04

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: 42.57  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 181 ARTGSGKTAAFILPMVEKLKSHSGKiGARAVILSPSRELAMQTFNVFKDFARGTEL-RSVLLTGGDSLEEQFGMMMTN-P 258
Cdd:cd17922    8 APTGSGKTEAAFLPALSSLADEPEK-GVQVLYISPLKALINDQERRLEEPLDEIDLeIPVAVRHGDTSQSEKAKQLKNpP 86
                         90       100       110
                 ....*....|....*....|....*....|...
gi 330443505 259 DVIIATPGRFLHLKVEMNLD--LKSVEYVVFDE 289
Cdd:cd17922   87 GILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
435-529 3.99e-04

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: 41.01  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 435 TILFVPTRHHVEYISQLLRDCGYLISYIYGTLDQHAR---KRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINYTLPG 511
Cdd:cd18799    9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRPTE 88
                         90
                 ....*....|....*....
gi 330443505 512 SSKIFVHRVGRTAR-AGNK 529
Cdd:cd18799   89 SRTLFLQMLGRGLRlHEGK 107
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
159-326 4.64e-04

DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain]  Cd Length: 179  Bit Score: 42.25  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 159 QPTPIQRKTIPLILQSRDIVGMARTGSGKT--AAFILPMVEKLKShsgkigaRAVILSPSRELAMQTFNVFKDfargTEL 236
Cdd:cd18027    8 ELDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQKHMT-------RTIYTSPIKALSNQKFRDFKN----TFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 237 RSVLLTGGDSLEEQFGMMMTNPDVIIAtpgrFLHLKVEMnldLKSVEYVVFDEADRLFEMGFQEQLNELLASLPTTRQTL 316
Cdd:cd18027   77 DVGLITGDVQLNPEASCLIMTTEILRS----MLYNGSDV---IRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSII 149
                        170
                 ....*....|
gi 330443505 317 LFSATLPNSL 326
Cdd:cd18027  150 LLSATVPNTV 159
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
157-191 6.11e-04

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 43.94  E-value: 6.11e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 330443505 157 FRQPTPIQRKTIPLILQSRD--IVgmARTGSGKT-AAF 191
Cdd:COG1201   22 FGAPTPPQREAWPAIAAGEStlLI--APTGSGKTlAAF 57
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
415-525 8.13e-04

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 40.80  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 415 KEKFRKQKMPaanelpSEKATILFVPTRHHVEYISQLLRDCGYLI-----------SYIYGtLDQHARKRQLYNFRAGLT 483
Cdd:cd18801   19 KEHFKKKQEG------SDTRVIIFSEFRDSAEEIVNFLSKIRPGIratrfigqasgKSSKG-MSQKEQKEVIEQFRKGGY 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 330443505 484 SILVVTDVAARGVDIPMLANVINYTlPGSSKI-FVHRVGRTAR 525
Cdd:cd18801   92 NVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR 133
ResIII pfam04851
Type III restriction enzyme, res subunit;
180-321 1.46e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.35  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505  180 MArTGSGKT--AAFIlpmVEKLKSHSGKigARAVILSPSRELAMQTFNVFKDFARGTELRSVLLTGGDSLEEQfgmmmTN 257
Cdd:pfam04851  30 MA-TGSGKTltAAKL---IARLFKKGPI--KKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKDESV-----DD 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443505  258 PDVIIATP---GRFLHLKVEMNLDLKSVeYVVFDEADRLFEMGFQeqlnELLASLPTTRQtLLFSAT 321
Cdd:pfam04851  99 NKIVVTTIqslYKALELASLELLPDFFD-VIIIDEAHRSGASSYR----NILEYFKPAFL-LGLTAT 159
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
157-268 1.91e-03

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 40.32  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 157 FRQPTPIQRKTIPLILQSRD--IVGmARTGSGKT--AAFILpmvekLKSHSGKIGARAVILSPSRELAMQtfnVFKD--- 229
Cdd:cd18021    1 FKFFNPIQTQVFNSLYNTDDnvFVG-APTGSGKTvcAELAL-----LRHWRQNPKGRAVYIAPMQELVDA---RYKDwra 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 330443505 230 -FARGTELRSVLLTGGDSLEEQfgmMMTNPDVIIATPGRF 268
Cdd:cd18021   72 kFGPLLGKKVVKLTGETSTDLK---LLAKSDVILATPEQW 108
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
433-528 2.97e-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: 39.17  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 433 KATILFVPTRHHVEYISQLLRD-CGY----LISYIY-GTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVIN 506
Cdd:cd18796   39 KSTLVFTNTRSQAERLAQRLRElCPDrvppDFIALHhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
                         90       100
                 ....*....|....*....|..
gi 330443505 507 YTLPGSSKIFVHRVGRTARAGN 528
Cdd:cd18796  119 IGSPKSVARLLQRLGRSGHRPG 140
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
435-536 5.41e-03

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 38.39  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 435 TILFVPTRHHVEYISQLLRD-------CGYLISYIYGTLDQHARKRQLYNFRAGLTSILVVTDVAARGVDIPMLANVINY 507
Cdd:cd18797   38 TIVFCRSRKLAELLLRYLKArlveegpLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
                         90       100
                 ....*....|....*....|....*....
gi 330443505 508 TLPGSSKIFVHRVGRTARAGNKgwAYSIV 536
Cdd:cd18797  118 GYPGSLASLWQQAGRAGRRGKD--SLVIL 144
Cas3_I-D cd09710
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ...
172-345 7.58e-03

CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D


Pssm-ID: 187841 [Multi-domain]  Cd Length: 353  Bit Score: 39.85  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 172 LQSRD---IVGMARTGSGKTAAFILPMVEKlkshsgkiGARAVILSPSRELAM-QTFNV---FKDFARGTELRSVLLTGG 244
Cdd:cd09710    9 LQSKDadiIFNTAPTGAGKTLAWLTPLLHG--------ENKAIALYPTNALIEdQTEAIkefVDDANPRHQVKSLSASDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443505 245 DSLEE-----------------------QFGMMMTNPDV-IIATPGRFLHLKVEMNLDLKSVEYVVFDEadrlFEMGFQE 300
Cdd:cd09710   81 TLWPNdknvgsskgeklynllrndigtsTPIILLTNPDIfVYLTRFAYIDRGDIAAGFYTKFSTVIFDE----FHLYDAK 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 330443505 301 QLNELLASLPTT---------RQTLLFSATLPNSLVDFVK-AGLVNPVLVRLDAE 345
Cdd:cd09710  157 QLVGLLFYLAYMqlirffecrRKFVFLSATPDPALILRLQnAKQAGVKIAPIDGE 211
PRK13767 PRK13767
ATP-dependent helicase; Provisional
153-192 8.30e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 40.25  E-value: 8.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 330443505 153 KRKgFRQPTPIQRKTIPLILQSRDIVGMARTGSGKT-AAFI 192
Cdd:PRK13767  27 KEK-FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
 
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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