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Conserved domains on  [gi|1046854579|ref|XP_006249460|]
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ATP-dependent RNA helicase DDX54 isoform X2 [Rattus norvegicus]

Protein Classification

DDX54/DBP10 family DEAD/DEAH box RNA helicase( domain architecture ID 13028829)

DDX54/DBP10 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, such as fungal ATP-dependent RNA helicase DBP10 that is involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs

CATH:  3.40.50.300
EC:  3.6.4.13
Gene Ontology:  GO:0016887|GO:0003723|GO:0003724|GO:0005524
PubMed:  20206133|21779027|20225155

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 ...
 95-299 1.24e-146

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: 430.57  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  95 GGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGARALILSPT 174
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEM 254
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 310-441 6.59e-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: 149.19  E-value: 6.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 310 LKTSFFLVREDTKTAVLLYLLQNVvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCS 389
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEK-LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046854579 390 TLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLV 441
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
 705-765 5.56e-23

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: 92.74  E-value: 5.56e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 705 DLMGDEAQNMSRGRQ---QLKWDRKKKRFVGQSGQED--KKKIKTESGRFISSSYKRDLYQKWKQK 765
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 ...
 95-299 1.24e-146

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: 430.57  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  95 GGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGARALILSPT 174
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEM 254
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
97-469 3.02e-131

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 399.52  E-value: 3.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKArSAQTGARALILSPTRE 176
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP-SRPRAPQALILAPTRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGF 256
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 257 AEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYLLQnvVRP 336
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 337 QDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPA 416
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046854579 417 KGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLGRSVTLAR-PHEEP 469
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElPGFEP 374
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 108-469 1.28e-82

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 272.20  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL----KARSAQtgARALILSPTRELALQTMK 183
Cdd:PRK11192   14 EALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGP--PRILILTPTRELAMQVAD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 184 FTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEI 263
Cdd:PRK11192   92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 264 IGRLPGGHQTVLFSATLP-KLLVEFARAGLTEPVLIrlDVDSKLNEQLKTSFFLVREDT---KTAVLLYLLQN--VVRpq 337
Cdd:PRK11192  172 AAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKIHQWYYRADDlehKTALLCHLLKQpeVTR-- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 338 dqNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPAK 417
Cdd:PRK11192  248 --SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRS 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046854579 418 GKLFLHRVGRVARAGRSGTAYSLV-APDevpylldlHLFLGRsvtLARPHEEP 469
Cdd:PRK11192  326 ADTYLHRIGRTGRAGRKGTAISLVeAHD--------HLLLGK---IERYIEEP 367
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 119-287 3.66e-64

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: 212.49  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 119 TPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARsaQTGARALILSPTRELALQTMKFTKELGKFTGLKTAL 198
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 199 ILGGDKMEDQFAALHeNPDIIIATPGRLVHVAVEMNlKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPGGHQTVLFSA 278
Cdd:pfam00270  79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156


                  ....*....
gi 1046854579 279 TLPKLLVEF 287
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
112-299 4.08e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.77  E-value: 4.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  112 KKGYKVPTPIQRKTIPVILDG-KDVVAMARTGSGKTACFLLPMFERLKARSaqtGARALILSPTRELALQTMKFTKELGK 190
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  191 FTGLKTALILGGDKMEDQFAAL-HENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPG 269
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 1046854579  270 GHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFID 189
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 310-441 6.59e-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: 149.19  E-value: 6.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 310 LKTSFFLVREDTKTAVLLYLLQNVvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCS 389
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEK-LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046854579 390 TLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLV 441
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
 705-765 5.56e-23

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: 92.74  E-value: 5.56e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 705 DLMGDEAQNMSRGRQ---QLKWDRKKKRFVGQSGQED--KKKIKTESGRFISSSYKRDLYQKWKQK 765
Cdd:pfam08147   1 DLTGDDGQELNQQKQvqkKMRWDKKKKKFVKRSGNDEdgKKKIRTESGVKIPASYKSGRYDEWKKK 66
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 322-432 1.63e-21

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: 90.35  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 322 KTAVLLYLLQNvvRPQDQNVVFVATKHHAEyLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGL 401
Cdd:pfam00271   2 KLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1046854579 402 DIPLLDNVINYSFPAKGKLFLHRVGRVARAG 432
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
351-432 8.44e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.79  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  351 EYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVAR 430
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1046854579  431 AG 432
Cdd:smart00490  81 AG 82
 
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 ...
 95-299 1.24e-146

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: 430.57  E-value: 1.24e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  95 GGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGARALILSPT 174
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEM 254
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
97-469 3.02e-131

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 399.52  E-value: 3.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKArSAQTGARALILSPTRE 176
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP-SRPRAPQALILAPTRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGF 256
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 257 AEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYLLQnvVRP 336
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 337 QDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPA 416
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046854579 417 KGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLGRSVTLAR-PHEEP 469
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEElPGFEP 374
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 108-299 2.79e-85

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 270.47  E-value: 2.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGA--RALILSPTRELALQTMKFT 185
Cdd:cd00268     3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRgpQALVLAPTRELAMQIAEVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 186 KELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIG 265
Cdd:cd00268    83 RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1046854579 266 RLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd00268   163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
 108-469 1.28e-82

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 272.20  E-value: 1.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL----KARSAQtgARALILSPTRELALQTMK 183
Cdd:PRK11192   14 EALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGP--PRILILTPTRELAMQVAD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 184 FTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEI 263
Cdd:PRK11192   92 QARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 264 IGRLPGGHQTVLFSATLP-KLLVEFARAGLTEPVLIrlDVDSKLNEQLKTSFFLVREDT---KTAVLLYLLQN--VVRpq 337
Cdd:PRK11192  172 AAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKIHQWYYRADDlehKTALLCHLLKQpeVTR-- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 338 dqNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPAK 417
Cdd:PRK11192  248 --SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRS 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046854579 418 GKLFLHRVGRVARAGRSGTAYSLV-APDevpylldlHLFLGRsvtLARPHEEP 469
Cdd:PRK11192  326 ADTYLHRIGRTGRAGRKGTAISLVeAHD--------HLLLGK---IERYIEEP 367
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
 97-445 3.90e-75

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 252.80  E-value: 3.90e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSPTRE 176
Cdd:PRK11776    6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRV--QALVLCPTRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFT-GLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEmNLKLQSVEYVVFDEADRLFEM 254
Cdd:PRK11776   84 LADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILdHLRKG-TLDLDALNTLVLDEADRMLDM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLN--EQLktsFFLVREDTKTAVLLYLLQN 332
Cdd:PRK11776  163 GFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPaiEQR---FYEVSPDERLPALQRLLLH 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 333 vVRPQdQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINY 412
Cdd:PRK11776  240 -HQPE-SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1046854579 413 SFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDE 445
Cdd:PRK11776  318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE 350
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 97-469 5.77e-73

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 247.03  E-value: 5.77e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGAR----ALILS 172
Cdd:PRK10590    3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRrpvrALILT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 173 PTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLF 252
Cdd:PRK10590   83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 253 EMGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYLLQN 332
Cdd:PRK10590  163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGK 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 333 vvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINY 412
Cdd:PRK10590  243 --GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046854579 413 SFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLGRSVT-LARPHEEP 469
Cdd:PRK10590  321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPrIAIPGYEP 378
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 106-299 1.26e-67

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: 223.29  E-value: 1.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGA-RALILSPTRELALQTMKF 184
Cdd:cd17947     1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAAtRVLVLVPTRELAMQCFSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 185 TKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEI 263
Cdd:cd17947    81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1046854579 264 IGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17947   161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 119-287 3.66e-64

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: 212.49  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 119 TPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARsaQTGARALILSPTRELALQTMKFTKELGKFTGLKTAL 198
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 199 ILGGDKMEDQFAALHeNPDIIIATPGRLVHVAVEMNlKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPGGHQTVLFSA 278
Cdd:pfam00270  79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156


                  ....*....
gi 1046854579 279 TLPKLLVEF 287
Cdd:pfam00270 157 TLPRNLEDL 165
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
 97-440 1.09e-63

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 220.61  E-value: 1.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTG-----ARALIL 171
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqPRALIM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 172 SPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRL 251
Cdd:PRK04837   90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 252 FEMGFAEQLQEIIGRLPGGHQ--TVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYL 329
Cdd:PRK04837  170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 330 LQNvvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNV 409
Cdd:PRK04837  250 IEE--EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1046854579 410 INYSFPAKGKLFLHRVGRVARAGRSGTAYSL 440
Cdd:PRK04837  328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
PTZ00110 PTZ00110
helicase; Provisional
 103-445 2.02e-63

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 223.50  E-value: 2.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 103 SYP--VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSA---QTGARALILSPTREL 177
Cdd:PTZ00110  136 SFPdyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlryGDGPIVLVLAPTREL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 178 ALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFA 257
Cdd:PTZ00110  216 AEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFE 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 258 EQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTE-PVLIRL-DVDSKLNEQLKTSFFLVREDTKTAVLLYLLQNVVR 335
Cdd:PTZ00110  296 PQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMR 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 336 PQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFP 415
Cdd:PTZ00110  376 DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455

                         330       340       350
                  ....*....|....*....|....*....|
gi 1046854579 416 AKGKLFLHRVGRVARAGRSGTAYSLVAPDE 445
Cdd:PTZ00110  456 NQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 96-468 2.16e-61

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 215.93  E-value: 2.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  96 GFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTG-----ARALI 170
Cdd:PRK01297   88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgePRALI 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 171 LSPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHEN-PDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEAD 249
Cdd:PRK01297  168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 250 RLFEMGFAEQLQEIIGRLP--GGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAvll 327
Cdd:PRK01297  248 RMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK--- 324

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 328 yLLQNVVR--PQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPL 405
Cdd:PRK01297  325 -LLYNLVTqnPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046854579 406 LDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLGRSVTLARPHEE 468
Cdd:PRK01297  404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAE 466
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 97-441 1.02e-59

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 215.10  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKA--RSAQTgaraLILSPT 174
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPelKAPQI----LVLAPT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGK-FTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:PRK11634   84 RELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 254 MGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYLLQnv 333
Cdd:PRK11634  164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLE-- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 334 VRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYS 413
Cdd:PRK11634  242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321

                         330       340
                  ....*....|....*....|....*...
gi 1046854579 414 FPAKGKLFLHRVGRVARAGRSGTAYSLV 441
Cdd:PRK11634  322 IPMDSESYVHRIGRTGRAGRAGRALLFV 349
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 97-298 3.37e-59

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: 200.62  E-value: 3.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKArsAQTGARALILSPTRE 176
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE--NPQRFFALVLAPTRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRLFEMG 255
Cdd:cd17954    80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLLNMD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 256 FAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17954   160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 110-298 9.68e-59

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: 198.97  E-value: 9.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 110 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGARALILSPTRELALQTMKFTKELG 189
Cdd:cd17957     5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 190 KFTGLKTALILGGD-KMEDQFAALHENPDIIIATPGRLVHvAVEMNLK-LQSVEYVVFDEADRLFEMGFAEQLQEIIGRL 267
Cdd:cd17957    85 KGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVF-LLKQGPIdLSSVEYLVLDEADKLFEPGFREQTDEILAAC 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1046854579 268 PGGH-QTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17957   164 TNPNlQRSLFSATIPSEVEELARSVMKDPIRI 195
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
 97-478 3.17e-56

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 203.64  E-value: 3.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTG-----ARALIL 171
Cdd:PRK04537   11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedPRALIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 172 SPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADR 250
Cdd:PRK04537   91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHACEICVLDEADR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 251 LFEMGFAEQLQEIIGRLP--GGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLY 328
Cdd:PRK04537  171 MFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 329 LLQnvvRPQD-QNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLD 407
Cdd:PRK04537  251 LLS---RSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 408 NVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLGRSV-----------TLARPHEEPSSGAVGR 476
Cdd:PRK04537  328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIpvepvtaelltPLPRPPRVPVEGEEAD 407


                  ..
gi 1046854579 477 DG 478
Cdd:PRK04537  408 DE 409
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 101-298 6.52e-56

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: 192.21  E-value: 6.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 101 GLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKAR---SAQTGARALILSPTREL 177
Cdd:cd17953    18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvKPGEGPIGLIMAPTREL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 178 ALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLK---LQSVEYVVFDEADRLFEM 254
Cdd:cd17953    98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnLRRVTYVVLDEADRMFDM 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17953   178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 97-298 3.94e-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: 189.36  E-value: 3.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLkaRSAQTGARALILSPTRE 176
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL--SEDPYGIFALVLTPTRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HV--AVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:cd17955    79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLrsSDDTTKVLSRVKFLVLDEADRLLT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 254 MGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17955   159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFW 203
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 114-299 4.96e-55

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: 188.94  E-value: 4.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 114 GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQ---TGARALILSPTRELALQTMKFTKELGK 190
Cdd:cd17960     9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkGQVGALIISPTRELATQIYEVLQSFLE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 191 FTG--LKTALILGGDKMEDQFAALHEN-PDIIIATPGRL----VHVAVEMNLKlqSVEYVVFDEADRLFEMGFAEQLQEI 263
Cdd:cd17960    89 HHLpkLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLeellSRKADKVKVK--SLEVLVLDEADRLLDLGFEADLNRI 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1046854579 264 IGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17960   167 LSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
PTZ00424 PTZ00424
helicase 45; Provisional
 97-452 1.79e-54

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 194.27  E-value: 1.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL--KARSAQtgarALILSPT 174
Cdd:PTZ00424   30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdyDLNACQ----ALILAPT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEM 254
Cdd:PTZ00424  106 RELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 255 GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLV-REDTKTAVLLYLLQNV 333
Cdd:PTZ00424  186 GFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 334 VrpQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYS 413
Cdd:PTZ00424  266 T--ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1046854579 414 FPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDL 452
Cdd:PTZ00424  344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 108-280 7.77e-54

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: 185.87  E-value: 7.77e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFE---RLKARSAQTGA-RALILSPTRELALQTMK 183
Cdd:cd17961     7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQkilKAKAESGEEQGtRALILVPTRELAQQVSK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 184 FTKELGKFTG--LKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQS-VEYVVFDEADRLFEMGFAEQL 260
Cdd:cd17961    87 VLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEEDL 166

                         170       180
                  ....*....|....*....|
gi 1046854579 261 QEIIGRLPGGHQTVLFSATL 280
Cdd:cd17961   167 KSLLSYLPKNYQTFLMSATL 186
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 110-298 8.29e-54

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: 185.31  E-value: 8.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 110 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL---KARSAQTGARALILSPTRELALQTMKFTK 186
Cdd:cd17952     5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVIVAPTRELAQQIYLEAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 187 ELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGR 266
Cdd:cd17952    85 KFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1046854579 267 LPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17952   165 VRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
 106-298 6.04e-53

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: 183.68  E-value: 6.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFER------LKARSAQTGARALILSPTRELAL 179
Cdd:cd17945     1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYisrlppLDEETKDDGPYALILAPTRELAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 180 QTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQ 259
Cdd:cd17945    81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046854579 260 LQEIIGRLP-----------------GGH---QTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17945   161 VTKILDAMPvsnkkpdteeaeklaasGKHryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 108-298 6.75e-53

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: 182.87  E-value: 6.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL--KARSAQTGARALILSPTRELALQTMKFT 185
Cdd:cd17941     3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrERWTPEDGLGALIISPTRELAMQIFEVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 186 KELGKFTGLKTALILGGDKMEDQFAALHENpDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEII 264
Cdd:cd17941    83 RKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1046854579 265 GRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17941   162 ENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEXDc smart00487
DEAD-like helicases superfamily;
112-299 4.08e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.77  E-value: 4.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  112 KKGYKVPTPIQRKTIPVILDG-KDVVAMARTGSGKTACFLLPMFERLKARSaqtGARALILSPTRELALQTMKFTKELGK 190
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  191 FTGLKTALILGGDKMEDQFAAL-HENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPG 269
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 1046854579  270 GHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFID 189
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 97-282 5.93e-52

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: 181.15  E-value: 5.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL--------KARSAQTGARA 168
Cdd:cd17967     2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAYPSA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 169 LILSPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVaVEMN-LKLQSVEYVVFDE 247
Cdd:cd17967    82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDF-IERGrISLSSIKFLVLDE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1046854579 248 ADRLFEMGFAEQLQEII--GRLP--GGHQTVLFSATLPK 282
Cdd:cd17967   161 ADRMLDMGFEPQIRKIVehPDMPpkGERQTLMFSATFPR 199
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 97-476 8.13e-52

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 190.00  E-value: 8.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFE-----RLKARSAQTGARALIL 171
Cdd:PLN00206  123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctiRSGHPSEQRNPLAMVL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 172 SPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRL 251
Cdd:PLN00206  203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 252 FEMGFAEQLQEIIGRLPGGhQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDSKLNEQLKTSFFLVREDTKTAVLLYLLQ 331
Cdd:PLN00206  283 LERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 332 NVVRPQDQNVVFVATKHHAEYLTELLT-GQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVI 410
Cdd:PLN00206  362 SKQHFKPPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 411 NYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEVPYLLDLHLFLgRSVTLARPHEEPSSGAVGR 476
Cdd:PLN00206  442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL-KSSGAAIPRELANSRYLGS 506
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 97-298 1.02e-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: 176.72  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKarSAQTGARALILSPTRE 176
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID--PKKDVIQALILVPTRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGF 256
Cdd:cd17940    79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1046854579 257 AEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17940   159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 102-292 7.52e-49

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: 172.00  E-value: 7.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 102 LSYPVFKGIMKKGYKVPTPIQRKTIPVIL-DGKDVVAMARTGSGKTACFLLPMFERL---KARSAQTGARALILSPTREL 177
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntKPAGRRSGVSALIISPTREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 178 ALQTMK-FTKELGKFTGLKTALILGGDKMEDQFAALH-ENPDIIIATPGRLV-HVAVEMNLK-LQSVEYVVFDEADRLFE 253
Cdd:cd17964    81 ALQIAAeAKKLLQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEADRLLD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 254 MGFAEQLQEIIGRLP----GGHQTVLFSATLPKLLVEFARAGL 292
Cdd:cd17964   161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTL 203
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
 100-298 1.31e-48

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: 170.97  E-value: 1.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 100 MGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSPTRELAL 179
Cdd:cd17939     2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET--QALVLAPTRELAQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 180 QTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQ 259
Cdd:cd17939    80 QIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1046854579 260 LQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17939   160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 110-298 3.08e-48

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: 169.65  E-value: 3.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 110 IMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERlkARSAQTGARALILSPTRELALQTMKFTKELG 189
Cdd:cd17962     5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR--CLTEHRNPSALILTPTRELAVQIEDQAKELM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 190 K-FTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLP 268
Cdd:cd17962    83 KgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1046854579 269 GGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17962   163 HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
 106-280 2.86e-47

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: 168.57  E-value: 2.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPV-ILDGKDVVAMARTGSGKTACFLLPMFERL-------KARSAQTGARALILSPTREL 177
Cdd:cd17946     1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKPLRALILTPTREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 178 ALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNL---KLQSVEYVVFDEADRLFEM 254
Cdd:cd17946    81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1046854579 255 GFAEQLQEIIGRLPGGH-------QTVLFSATL 280
Cdd:cd17946   161 GHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
 106-298 3.17e-46

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: 164.43  E-value: 3.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMF------ERLKARSAQTGARALILSPTRELAL 179
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 180 QTMK----FTKEL--GKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:cd17951    81 QTHEvieyYCKALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 254 MGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
 106-298 2.53e-45

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: 161.38  E-value: 2.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKA---RSAQTGARALILSPTRELALQTM 182
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAqppLERGDGPIVLVLAPTRELAQQIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 183 KFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQE 262
Cdd:cd17966    81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1046854579 263 IIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17966   161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 106-298 1.31e-43

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: 156.47  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGAR----ALILSPTRELALQT 181
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRngpgVLVLTPTRELALQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 182 -MKFTKElgKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQL 260
Cdd:cd17958    81 eAECSKY--SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1046854579 261 QEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd17958   159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 114-299 1.70e-43

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: 156.98  E-value: 1.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 114 GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKA------RSaqTGARALILSPTRELALQTMK-FTK 186
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSleprvdRS--DGTLALVLVPTRELALQIYEvLEK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 187 ELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEII- 264
Cdd:cd17949    88 LLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILe 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1046854579 265 ------------GRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17949   168 llddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 108-298 4.06e-42

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 152.51  E-value: 4.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERL-KARSAQ-TGARALILSPTRELALQTMKFT 185
Cdd:cd17942     3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLyKLKFKPrNGTGVIIISPTRELALQIYGVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 186 KELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEII 264
Cdd:cd17942    83 KELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQII 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1046854579 265 GRLPGGHQTVLFSATLPKLLVEFARAGL-TEPVLI 298
Cdd:cd17942   163 KLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 310-441 6.59e-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: 149.19  E-value: 6.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 310 LKTSFFLVREDTKTAVLLYLLQNVvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCS 389
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEK-LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046854579 390 TLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLV 441
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 97-280 3.95e-41

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: 149.78  E-value: 3.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLkarsaqtgaRALILSPTRE 176
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV---------VALILEPSRE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFT---GLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:cd17938    72 LAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1046854579 254 MGFAEQLQEIIGRLPGGH------QTVLFSATL 280
Cdd:cd17938   152 QGNLETINRIYNRIPKITsdgkrlQVIVCSATL 184
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
 102-299 4.53e-41

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: 149.26  E-value: 4.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 102 LSYPVFKGIMKKGYKVPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSPTRELAL 179
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSP--QALCLAPTRELAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 180 QTMKFTKELGKFTGLKTALIL------GGDKMEDQfaalhenpdIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:cd17963    79 QIGEVVEKMGKFTGVKVALAVpgndvpRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1046854579 254 M-GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17963   150 TqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 106-299 3.20e-40

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: 146.64  E-value: 3.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 106 VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSPTRELALQTMKFT 185
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHP--QVLILAPTREIAVQIHDVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 186 KELG-KFTGLKTALILGGDKMEDQFAALhENPDIIIATPGRLVHVaVEMN-LKLQSVEYVVFDEADRLFEMGFAEQLQEI 263
Cdd:cd17943    79 KKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQL-IELGaLNVSHVRLFVLDEADKLMEGSFQKDVNWI 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1046854579 264 IGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd17943   157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 97-287 6.65e-39

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 145.50  E-value: 6.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKAR----SAQTGAR---AL 169
Cdd:cd18052    45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltaSSFSEVQepqAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 170 ILSPTRELALQTMkftKELGKF---TGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFD 246
Cdd:cd18052   125 IVAPTRELANQIF---LEARKFsygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1046854579 247 EADRLFEMGFAEQLQEII--GRLP--GGHQTVLFSATLP----KLLVEF 287
Cdd:cd18052   202 EADRMLDMGFGPEIRKLVsePGMPskEDRQTLMFSATFPeeiqRLAAEF 250
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
 97-298 1.65e-38

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: 142.22  E-value: 1.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACF---LLPMFErLKARSAQtgarALILSP 173
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFsisVLQCLD-IQVRETQ----ALILSP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 174 TRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFE 253
Cdd:cd18045    76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1046854579 254 MGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd18045   156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
 115-289 2.24e-38

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: 143.64  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 115 YKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLP----MFERLKARSAQTGAR----------ALILSPTRELALQ 180
Cdd:cd18051    41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsqIYEQGPGESLPSESGyygrrkqyplALVLAPTRELASQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 181 TMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQL 260
Cdd:cd18051   121 IYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQI 200

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1046854579 261 QEIIGR--LP--GGHQTVLFSATLPKLLVEFAR 289
Cdd:cd18051   201 RRIVEQdtMPptGERQTLMFSATFPKEIQMLAR 233
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
 97-298 2.10e-36

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: 136.04  E-value: 2.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSPTRE 176
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT--QALVLAPTRE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 177 LALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGF 256
Cdd:cd18046    79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1046854579 257 AEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLI 298
Cdd:cd18046   159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
 103-300 2.29e-35

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: 134.37  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 103 SYP--VFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKAR---SAQTGARALILSPTREL 177
Cdd:cd18049    30 NFPanVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpflERGDGPICLVLAPTREL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 178 ALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFA 257
Cdd:cd18049   110 AQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 258 EQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 300
Cdd:cd18049   190 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 112-282 1.27e-34

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: 132.11  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 112 KKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGA-----RALILSPTRELALQTMKFTK 186
Cdd:cd17948     7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnapRGLVITPSRELAEQIGSVAQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 187 ELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGR 266
Cdd:cd17948    87 SLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166

                         170       180
                  ....*....|....*....|....*....
gi 1046854579 267 LP-------------GGHQTVLFSATLPK 282
Cdd:cd17948   167 FPlasrrsentdgldPGTQLVLVSATMPS 195
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
 96-300 2.97e-33

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: 129.36  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  96 GFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKAR---SAQTGARALILS 172
Cdd:cd18050    63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylERGDGPICLVLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 173 PTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLF 252
Cdd:cd18050   143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1046854579 253 EMGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 300
Cdd:cd18050   223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 120-289 3.03e-32

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 124.19  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 120 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKA----RSAQTGARALILSPTRELALQTMKFTKELGKftGLK 195
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEdqqpRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 196 TALILGGDKMEDQFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRL-----PGG 270
Cdd:cd17944    93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDN 172

                         170
                  ....*....|....*....
gi 1046854579 271 HQTVLFSATLPKLLVEFAR 289
Cdd:cd17944   173 PQTLLFSATCPDWVYNVAK 191
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
 94-282 5.06e-32

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: 123.99  E-value: 5.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  94 SGGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTgaRALILSP 173
Cdd:cd17950     1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV--SVLVICH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 174 TRELALQTMKFTKELGKF-TGLKTALILGGDKMEDQFAALHEN-PDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRL 251
Cdd:cd17950    79 TRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1046854579 252 FE-MGFAEQLQEIIGRLPGGHQTVLFSATLPK 282
Cdd:cd17950   159 LEqLDMRRDVQEIFRATPHDKQVMMFSATLSK 190
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 112-280 1.04e-28

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: 115.04  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 112 KKGYKVPTPIQRKTIPVILDG---------KDVVAMARTGSGKTACFLLPMFERLKARSAqTGARALILSPTRELALQTM 182
Cdd:cd17956     7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVV-PRLRALIVVPTKELVQQVY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 183 KFTKELGKFTGLKTALiLGGDK---------MEDQFAALHENPDIIIATPGRLV-HVAVEMNLKLQSVEYVVFDEADRL- 251
Cdd:cd17956    86 KVFESLCKGTGLKVVS-LSGQKsfkkeqkllLVDTSGRYLSRVDILVATPGRLVdHLNSTPGFTLKHLRFLVIDEADRLl 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1046854579 252 ---FEmGFAEQLQEIIGR----------------LPGGH-QTVLFSATL 280
Cdd:cd17956   165 nqsFQ-DWLETVMKALGRptapdlgsfgdanlleRSVRPlQKLLFSATL 212
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
 97-300 8.66e-25

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 103.56  E-value: 8.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDG--KDVVAMARTGSGKTACFLLPMFERLKARsaQTGARALILSPT 174
Cdd:cd18048    20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL--KLYPQCLCLSPT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKF-TGLKTALILGGDK------MEDQfaalhenpdIIIATPGRLVHVAVEMNL-KLQSVEYVVFD 246
Cdd:cd18048    98 FELALQTGKVVEEMGKFcVGIQVIYAIRGNRpgkgtdIEAQ---------IVIGTPGTVLDWCFKLRLiDVTNISVFVLD 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046854579 247 EADRLFEM-GFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRL 300
Cdd:cd18048   169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
 705-765 5.56e-23

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: 92.74  E-value: 5.56e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 705 DLMGDEAQNMSRGRQ---QLKWDRKKKRFVGQSGQED--KKKIKTESGRFISSSYKRDLYQKWKQK 765
Cdd:pfam08147   1 DLTGDDGQELNQQKQvqkKMRWDKKKKKFVKRSGNDEdgKKKIRTESGVKIPASYKSGRYDEWKKK 66
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
 114-282 3.27e-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: 96.68  E-value: 3.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 114 GYKVPTPIQRKTIPVIL------------DGKD-----VVAmARTGSGKTACFLLPMFERLKARSAQTG----------- 165
Cdd:cd17965    27 EEIKPSPIQTLAIKKLLktlmrkvtkqtsNEEPklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesak 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 166 ----ARALILSPTRELALQTMKFTKELGKFTGLKTALILG--GDKMEDQFAALHENPDIIIATPGRLVHVA-VEMNLkLQ 238
Cdd:cd17965   106 dtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAkSRPKI-LS 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1046854579 239 SVEYVVFDEADRLFEMGFAEQLQEIIGRLPGGHQTVLFSATLPK 282
Cdd:cd17965   185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK 228
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 322-432 1.63e-21

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: 90.35  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 322 KTAVLLYLLQNvvRPQDQNVVFVATKHHAEyLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGL 401
Cdd:pfam00271   2 KLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1046854579 402 DIPLLDNVINYSFPAKGKLFLHRVGRVARAG 432
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
 97-299 1.94e-21

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


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 93.25  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  97 FQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVIL--DGKDVVAMARTGSGKTACFLLPMFERLKArsAQTGARALILSPT 174
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVEP--ANKYPQCLCLSPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 175 RELALQTMKFTKELGKF-TGLKTALILGGDKMEdqfAALHENPDIIIATPGRLVHVAVEMNL-KLQSVEYVVFDEADRLF 252
Cdd:cd18047    81 YELALQTGKVIEQMGKFyPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1046854579 253 -EMGFAEQLQEIIGRLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIR 299
Cdd:cd18047   158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
135-452 6.69e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 94.71  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 135 VVAMArTGSGKT--ACFLlpmferlkARSAQTGARALILSPTRELALQTMKftkELGKFTGLKtalILGGDKMEDQFaal 212
Cdd:COG1061   104 LVVAP-TGTGKTvlALAL--------AAELLRGKRVLVLVPRRELLEQWAE---ELRRFLGDP---LAGGGKKDSDA--- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 213 henpDIIIATPGRLVHVAVEMNLKlQSVEYVVFDEADRLFemgfAEQLQEIIGRLPGGHqTVLFSAT------LPKLLVE 286
Cdd:COG1061   166 ----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAG----APSYRRILEAFPAAY-RLGLTATpfrsdgREILLFL 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 287 F------------ARAG-LTEPVLIRLDVD--------SKLNEQLKTSFFLVREDTKTAVLLYLLQNvvRPQDQNVVFVA 345
Cdd:COG1061   236 FdgivyeyslkeaIEDGyLAPPEYYGIRVDltderaeyDALSERLREALAADAERKDKILRELLREH--PDDRKTLVFCS 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 346 TKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSfPAKGK-LFLHR 424
Cdd:COG1061   314 SVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGSPrEFIQR 392

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1046854579 425 VGRVARAGRSGTA---YSLVAPDeVPYLLDL 452
Cdd:COG1061   393 LGRGLRPAPGKEDalvYDFVGND-VPVLEEL 422
HELICc smart00490
helicase superfamily c-terminal domain;
351-432 8.44e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.79  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579  351 EYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVAR 430
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80


                   ..
gi 1046854579  431 AG 432
Cdd:smart00490  81 AG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 132-279 4.77e-17

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: 78.60  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 132 GKDVVAMARTGSGKTACFLLPMFERLKARsaqtGARALILSPTRELALQTMKFTKELGKfTGLKTALILGGDKMEDQFAA 211
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKK----GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKN 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046854579 212 LHENPDIIIATPGRLVHVAVEMN-LKLQSVEYVVFDEADR-LFEMGFAEQLQEIIGRL-PGGHQTVLFSAT 279
Cdd:cd00046    76 KLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHAlLIDSRGALILDLAVRKAgLKNAQVILLSAT 146
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 122-289 5.99e-16

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: 76.85  E-value: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 122 QRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLkARsaQTGARALILSPTRELAL-QTMKFTKELGKF-TGLKTALI 199
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LR--DPGSRALYLYPTKALAQdQLRSLRELLEQLgLGIRVATY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 200 LGGDKMEDQFAALHENPDIIIATPGRLvHVAVemnLK--------LQSVEYVVFDEADRlFEMGFAEQLQEIIGRL---- 267
Cdd:cd17923    82 DGDTPREERRAIIRNPPRILLTNPDML-HYAL---LPhhdrwarfLRNLRYVVLDEAHT-YRGVFGSHVALLLRRLrrlc 156

                         170       180
                  ....*....|....*....|....*
gi 1046854579 268 --PGGH-QTVLFSATLpKLLVEFAR 289
Cdd:cd17923   157 rrYGADpQFILTSATI-GNPAEHAR 180
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 119-281 8.46e-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: 73.45  E-value: 8.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 119 TPIQRKTI-PVILDGKDVVAMARTGSGKTACFLLPMFERLkarsAQTGARALILSPTRELALQ-TMKFTKELGKFtGLKT 196
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL----ATSGGKAVYIAPTRALVNQkEADLRERFGPL-GKNV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 197 ALILGGDKMEDQFAAlheNPDIIIATPGRLvhvavEM------NLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLP-- 268
Cdd:cd17921    78 GLLTGDPSVNKLLLA---EADILVATPEKL-----DLllrnggERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLri 149

                         170
                  ....*....|....
gi 1046854579 269 -GGHQTVLFSATLP 281
Cdd:cd17921   150 nKNARFVGLSATLP 163
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 122-466 2.49e-14

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 77.18  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 122 QRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKARSaqtGARALILSPTRELA---LQTM-KFTKELGkfTGLKTA 197
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP---GATALYLYPTKALArdqLRRLrELAEALG--LGVRVA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 198 lILGGDKMEDQFAALHENPDIIIATPGrLVHVAVemnLK--------LQSVEYVVFDEA---------------DRlfem 254
Cdd:COG1205   136 -TYDGDTPPEERRWIREHPDIVLTNPD-MLHYGL---LPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRR---- 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 255 gfaeqLQEIIGRLpGGHQTVLF-SATL--PKllvEFARAgLT-EPVLIrldVDSKLNEQLKTSFFLV--------REDTK 322
Cdd:COG1205   207 -----LRRICRHY-GSDPQFILaSATIgnPA---EHAER-LTgRPVTV---VDEDGSPRGERTFVLWnpplvddgIRRSA 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 323 TAVLLYLLQNVVRPQDQNVVFVATKHHAE----YLTELLTGQGV-SCAHIYSA--LDQTARKINlAKFTHNKCSTLIVT- 394
Cdd:COG1205   274 LAEAARLLADLVREGLRTLVFTRSRRGAEllarYARRALREPDLaDRVAAYRAgyLPEERREIE-RGLRSGELLGVVSTn 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 395 --DLaarGLDIPLLDNVINYSFPakGKL--FLHRVGRVARAGRSGTAYsLVAPDEvP---YLLDlH--LFLGRSVTLARP 465
Cdd:COG1205   353 alEL---GIDIGGLDAVVLAGYP--GTRasFWQQAGRAGRRGQDSLVV-LVAGDD-PldqYYVR-HpeELFERPPEAAVI 424


                  .
gi 1046854579 466 H 466
Cdd:COG1205   425 D 425
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
112-400 1.16e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 64.92  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 112 KKGYKVPTPIQRKTIP-VILDGKDVVAMARTGSGKTACFLLPMFerlkaRSAQTGARALILSPTRELALQTM-KFTKELG 189
Cdd:COG1204    17 ERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAIL-----KALLNGGKALYIVPLRALASEKYrEFKRDFE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 190 KFtGLKTALILGGDKMEDQFAalhENPDIIIATPGR---LVHVAVEMnlkLQSVEYVVFDEA------DRlfemGFaeQL 260
Cdd:COG1204    92 EL-GIKVGVSTGDYDSDDEWL---GRYDILVATPEKldsLLRNGPSW---LRDVDLVVVDEAhliddeSR----GP--TL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 261 QEIIGRL---PGGHQTVLFSATLPKlLVEFAR---AGLTE----PVLIRLDV--DSKLNeqlktsfFLVREDTKTAVLLY 328
Cdd:COG1204   159 EVLLARLrrlNPEAQIVALSATIGN-AEEIAEwldAELVKsdwrPVPLNEGVlyDGVLR-------FDDGSRRSKDPTLA 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046854579 329 LLQNVVRPQDQNVVFVATKHHAE----YLTELLTGQGVSCAHiySALDQTARKI-NLAKFTHNkCSTLIvtDLAARG 400
Cdd:COG1204   231 LALDLLEEGGQVLVFVSSRRDAEslakKLADELKRRLTPEER--EELEELAEELlEVSEETHT-NEKLA--DCLEKG 302
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
141-250 2.67e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.90  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 141 TGSGKTACFLLPMFERLKARsaqtGARALILSPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQfAALHENPDIII 220
Cdd:COG1111    26 TGLGKTAVALLVIAERLHKK----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKR-KELWEKARIIV 100

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046854579 221 ATPGRLVHVAVEMNLKLQSVEYVVFDEADR 250
Cdd:COG1111   101 ATPQVIENDLIAGRIDLDDVSLLIFDEAHR 130
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 121-223 3.28e-09

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: 57.75  E-value: 3.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 121 IQRKTIPVILDG-KDVVAMARTGSGKTACFLLPMFERLKAR--SAQTGARALILSPTRELALQTMKFTKElgKF--TGLK 195
Cdd:cd18023     5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERnpLPWGNRKVVYIAPIKALCSEKYDDWKE--KFgpLGLS 82

                          90       100
                  ....*....|....*....|....*...
gi 1046854579 196 TALILGGDKMEDQFAAlhENPDIIIATP 223
Cdd:cd18023    83 CAELTGDTEMDDTFEI--QDADIILTTP 108
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 135-280 4.88e-09

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: 55.77  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 135 VVAMArTGSGKTACFLLPMFERLKarsaqtgARALILSPTRELALQTMkftKELGKFTGLKTALILGGDKMEDQFAAlhe 214
Cdd:cd17926    22 ILVLP-TGSGKTLTALALIAYLKE-------LRTLIVVPTDALLDQWK---ERFEDFLGDSSIGLIGGGKKKDFDDA--- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 215 npDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLfemgFAEQLQEIIGRLPGGHQtVLFSATL 280
Cdd:cd17926    88 --NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL----PAKTFSEILKELNAKYR-LGLTATP 146
PRK13766 PRK13766
Hef nuclease; Provisional
 141-250 1.56e-08

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 58.35  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 141 TGSGKTACFLLPMFERLKARsaqtGARALILSPTRELALQTMKFTKELGKFTGLKTALILGGDKMEDQfAALHENPDIII 220
Cdd:PRK13766   38 TGLGKTAIALLVIAERLHKK----GGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKR-AELWEKAKVIV 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1046854579 221 ATPgrlvHVaVEMNL-----KLQSVEYVVFDEADR 250
Cdd:PRK13766  113 ATP----QV-IENDLiagriSLEDVSLLIFDEAHR 142
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 133-248 2.27e-07

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 52.27  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 133 KDVVAMARTGSGKT--ACFLLPMFERLKARSAQTGARALILSPTRELALQTmkfTKELGKFTGLKTAlILGGDKMEDQFA 210
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQ---AEAIRSHTDLKVG-EYSGEMGVDKWT 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 211 ALH-----ENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEA 248
Cdd:cd18034    93 KERwkeelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 108-303 2.68e-07

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 51.77  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 108 KGIMKK--GYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLP--MFERLkarsaqtgarALILSPTreLAL---Q 180
Cdd:cd17920     1 EQILKEvfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV----------TLVVSPL--ISLmqdQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 181 TMKFTKelgkfTGLKTALILGG----DKMEDQFAALHENPDIIIATPGRLVHVAVEMNL-KLQS---VEYVVFDEA---- 248
Cdd:cd17920    69 VDRLQQ-----LGIRAAALNSTlspeEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLqRLPErkrLALIVVDEAhcvs 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046854579 249 ----DrlF--EMGfaeQLQEIIGRLPgGHQTVLFSATLPKLLVE--FARAGLTEPVLIRLDVD 303
Cdd:cd17920   144 qwghD--FrpDYL---RLGRLRRALP-GVPILALTATATPEVREdiLKRLGLRNPVIFRASFD 200
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 128-250 5.45e-07

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 50.59  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 128 VILDGKDVVAMArTGSGKTACFLLPMFERLKARsaqtGARALILSPTRELALQTMKFTKELGKFTGLKTALIlgGDKMED 207
Cdd:cd18035    13 VALNGNTLIVLP-TGLGKTIIAILVAADRLTKK----GGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 208 QFAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADR 250
Cdd:cd18035    86 ERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 112-303 9.99e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 52.58  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 112 KKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLL---PMFERLKARSAQTGARALILSPTRELA-------LQ 180
Cdd:PRK13767   27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAiidELFRLGREGELEDKVYCLYVSPLRALNndihrnlEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 181 TMKFTKELGKFTGLKTALI----LGGD-------KMedqfaaLHENPDIIIATPGRL--VHVAVEMNLKLQSVEYVVFDE 247
Cdd:PRK13767  107 PLTEIREIAKERGEELPEIrvaiRTGDtssyekqKM------LKKPPHILITTPESLaiLLNSPKFREKLRTVKWVIVDE 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046854579 248 ADRLFE-------MGFAEQLQEIIGRLPgghQTVLFSATL-P-----KLLVEFARAGLTEPVLIrldVD 303
Cdd:PRK13767  181 IHSLAEnkrgvhlSLSLERLEELAGGEF---VRIGLSATIePleevaKFLVGYEDDGEPRDCEI---VD 243
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 130-250 1.25e-06

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: 50.12  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 130 LDGKDVVAMARTGSGKTACFLLPMFERLKARSAQTGARALILSPTRELALQTM-KFTKELGKfTGLKTALILGGDKMEDQ 208
Cdd:cd17927    15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKeVFRKHFER-PGYKVTGLSGDTSENVS 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1046854579 209 FAALHENPDIIIATPGRLVHVAVEMNL-KLQSVEYVVFDEADR 250
Cdd:cd17927    94 VEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
ResIII pfam04851
Type III restriction enzyme, res subunit;
123-279 1.85e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.82  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 123 RKTIPVILDGKD--VVAMArTGSGKTACFLLPMFERLKARSAQtgaRALILSPTRELALQTMK-FTKELGKFTGLKTalI 199
Cdd:pfam04851  13 ENLLESIKNGQKrgLIVMA-TGSGKTLTAAKLIARLFKKGPIK---KVLFLVPRKDLLEQALEeFKKFLPNYVEIGE--I 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 200 LGGDKMEDQFaalhENPDIIIATPGRLvHVAVEMNLKLQSVE---YVVFDEADRLfemgFAEQLQEIIGRLPggHQTVL- 275
Cdd:pfam04851  87 ISGDKKDESV----DDNKIVVTTIQSL-YKALELASLELLPDffdVIIIDEAHRS----GASSYRNILEYFK--PAFLLg 155


                  ....
gi 1046854579 276 FSAT 279
Cdd:pfam04851 156 LTAT 159
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
122-387 2.62e-06

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 50.91  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 122 QRKTIPVILDGKDVVAMARTGSGKTACFLLP--MFERLkarsaqtgarALILSPTreLALqtMK----FTKELgkftGLK 195
Cdd:COG0514    22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL----------TLVVSPL--IAL--MKdqvdALRAA----GIR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 196 TALI---LGGDKMEDQFAALHEN-PDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEA------------DRLfemgfaeQ 259
Cdd:COG0514    84 AAFLnssLSAEERREVLRALRAGeLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcisqwghdfrpDYR-------R 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 260 LQEIIGRLPgGHQTVLFSATlpkllvefAraglTEPVliRLDVDSKLN----EQLKTSF------FLVRE---DTKTAVL 326
Cdd:COG0514   157 LGELRERLP-NVPVLALTAT--------A----TPRV--RADIAEQLGledpRVFVGSFdrpnlrLEVVPkppDDKLAQL 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046854579 327 LYLLQNvvRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHiYSA-LDQTARKINLAKFTHNK 387
Cdd:COG0514   222 LDFLKE--HPGGSGIVYCLSRKKVEELAEWLREAGIRAAA-YHAgLDAEEREANQDRFLRDE 280
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
 118-250 7.91e-06

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: 47.41  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 118 PTPIQRKTIPVIL-DGKDVVAMAR-----TGSGKTACFLLPMFERLKArsaqtGARALILSPTRELALQTMKFTKELgkF 191
Cdd:cd17918    16 LTKDQAQAIKDIEkDLHSPEPMDRllsgdVGSGKTLVALGAALLAYKN-----GKQVAILVPTEILAHQHYEEARKF--L 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046854579 192 TGLKTALILGGDKMEDQfaalhENPDIIIATPGrLVHVAVemnlKLQSVEYVVFDEADR 250
Cdd:cd17918    89 PFINVELVTGGTKAQIL-----SGISLLVGTHA-LLHLDV----KFKNLDLVIVDEQHR 137
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 314-435 1.16e-05

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: 45.66  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 314 FFLVREDTKTAVLLYLLQNVVR--PQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCSTL 391
Cdd:cd18794     5 FYSVRPKDKKDEKLDLLKRIKVehLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1046854579 392 IVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGrvaRAGRSG 435
Cdd:cd18794    85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDG 125
PRK00254 PRK00254
ski2-like helicase; Provisional
 129-351 1.95e-05

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 48.27  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 129 ILDGKDVVAMARTGSGKTACFLLPMFERLkarsAQTGARALILSPTRELALQTMKFTKELGKFtGLKTALILGGDKMEDQ 208
Cdd:PRK00254   36 VLEGKNLVLAIPTASGKTLVAEIVMVNKL----LREGGKAVYLVPLKALAEEKYREFKDWEKL-GLRVAMTTGDYDSTDE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 209 FAALHenpDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPGGHQTVLFSATL--PKLLVE 286
Cdd:PRK00254  111 WLGKY---DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAE 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046854579 287 FARAGLT----EPVLIRLDVdsklneqlktsF---FLVREDTKTAVLL----YLLQNVVRPQDQNVVFVATKHHAE 351
Cdd:PRK00254  188 WLNAELVvsdwRPVKLRKGV-----------FyqgFLFWEDGKIERFPnsweSLVYDAVKKGKGALVFVNTRRSAE 252
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
115-247 3.27e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 47.79  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 115 YKVPTPIQRKTIPVILDGKDVVAMARTGSGKT-ACFLLP---MFERLKARSAQTGARALILSPTRELA------LQTmkF 184
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPAldeLARRPRPGELPDGLRVLYISPLKALAndiernLRA--P 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046854579 185 TKELGKFTGLKTALI-LG---GDKMEDQFAALHEN-PDIIIATP-----------GRlvhvavEMnlkLQSVEYVVFDE 247
Cdd:COG1201   100 LEEIGEAAGLPLPEIrVGvrtGDTPASERQRQRRRpPHILITTPeslallltspdAR------EL---LRGVRTVIVDE 169
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
120-294 5.49e-05

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 46.86  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 120 PIQRKTIPVILDGKDVVAMARTGSGKT--ACFLLpmFERLkarsaQTGARALILSPTRELALQtmKFtKELGKFTGLKTA 197
Cdd:COG4581    28 PFQEEAILALEAGRSVLVAAPTGSGKTlvAEFAI--FLAL-----ARGRRSFYTAPIKALSNQ--KF-FDLVERFGAENV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 198 LILGGDkmedqfaaLHENPD--IIIATpgrlvhvaVEM--NL------KLQSVEYVVFDE----ADRlfEMGFAeqLQEI 263
Cdd:COG4581    98 GLLTGD--------ASVNPDapIVVMT--------TEIlrNMlyregaDLEDVGVVVMDEfhylADP--DRGWV--WEEP 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1046854579 264 IGRLPGGHQTVLFSATLPKllVEFARAGLTE 294
Cdd:COG4581   158 IIHLPARVQLVLLSATVGN--AEEFAEWLTR 186
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 320-412 8.76e-05

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 43.23  E-value: 8.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 320 DTKTAVLLYLLQNVVRPQDQNVVFVATKHHAEYLTELLTGQGVSCAHIYSALDQTARKINLAKFTHNKCST--LIVTDLA 397
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRvfLLSTKAG 89

                          90
                  ....*....|....*
gi 1046854579 398 ARGLDIPLLDNVINY 412
Cdd:cd18793    90 GVGLNLTAANRVILY 104
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 120-281 8.91e-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: 44.25  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 120 PIQRKTI-PVILDGKDVVAMARTGSGKTACFLLPMFerlkaRSAQTGARALILSPTRELALQTMKFTKELGKFtGLKTAL 198
Cdd:cd18028     4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMV-----NTLLEGGKALYLVPLRALASEKYEEFKKLEEI-GLKVGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 199 ILGGDKMEDQFaaLHENpDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGR---LPGGHQTVL 275
Cdd:cd18028    78 STGDYDEDDEW--LGDY-DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARlrrLNPNTQIIG 154


                  ....*.
gi 1046854579 276 FSATLP 281
Cdd:cd18028   155 LSATIG 160
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
 120-152 1.72e-04

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 43.89  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1046854579 120 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLP 152
Cdd:cd18015    21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 136-250 2.98e-04

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 42.16  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 136 VAMArTGSGKT--ACFLlpmFERLKarSAQTGARALILSPTRELALQTMkftKELGKFTGLKTALILGGDKMEDQFAalh 213
Cdd:cd18032    25 LVMA-TGTGKTytAAFL---IKRLL--EANRKKRILFLAHREELLEQAE---RSFKEVLPDGSFGNLKGGKKKPDDA--- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046854579 214 enpDIIIATPGRLVHvavEMNLKLQSVE---YVVFDEADR 250
Cdd:cd18032    93 ---RVVFATVQTLNK---RKRLEKFPPDyfdLIIIDEAHH 126
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
 118-288 4.16e-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: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 118 PTPIQRKTIPVILDGKDVVAMARTGSGKTAcfllpMFERLKARSAQTGARALILSPTRELALQTMKFTKELGKFTGLKTa 197
Cdd:cd18027     9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTV-----VAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLIT- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 198 lilgGDkmedqfAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEADRLFEMGFAEQLQEIIGRLPGGHQTVLFS 277
Cdd:cd18027    83 ----GD------VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLS 152

                         170
                  ....*....|.
gi 1046854579 278 ATLPKlLVEFA 288
Cdd:cd18027   153 ATVPN-TVEFA 162
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 132-247 5.01e-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: 41.80  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 132 GKDVVAMARTGSGKTACFLLPMFERLkARSAQTGARALILSPTRELALQTMKFTKELGKFTGLK-TALILGGDKMEDQFA 210
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSL-ADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEiPVAVRHGDTSQSEKA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046854579 211 ALHEN-PDIIIATPGRL--VHVAVEMNLKLQSVEYVVFDE 247
Cdd:cd17922    80 KQLKNpPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 342-410 1.01e-03

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: 39.85  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046854579 342 VFVATKHHAEYLTELLTGQGVSCAHIYSalDQTARKINLAK----FTHNKCSTLIVT-DLAARGLDIPLLDNVI 410
Cdd:cd18799    11 IFCVSIEHAEFMAEAFNEAGIDAVALNS--DYSDRERGDEAlillFFGELKPPILVTvDLLTTGVDIPEVDNVV 82
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 120-223 1.59e-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: 40.70  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 120 PIQRKTIPVILDGKD-VVAMARTGSGKTACFLLPMferLKARSAQTGARALILSPTRELALQTM-----KFTKELGkftg 193
Cdd:cd18021     6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELAL---LRHWRQNPKGRAVYIAPMQELVDARYkdwraKFGPLLG---- 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1046854579 194 lKTALILGGDKMEDqfAALHENPDIIIATP 223
Cdd:cd18021    79 -KKVVKLTGETSTD--LKLLAKSDVILATP 105
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 117-247 1.99e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 40.54  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 117 VPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKAR-SAQTGARALILSPTRELALQTM-KFTKELGKftGL 194
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRrSAGEKGRVVVLVNKVPLVEQQLeKFFKYFRK--GY 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046854579 195 KTALILGGDKMEDQFAALHENPDIIIATPGRLVH----VAVEMNLKLQSVEYVVFDE 247
Cdd:cd18036    80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINnllsGREEERVYLSDFSLLIFDE 136
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
 102-289 2.54e-03

DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain]  Cd Length: 205  Bit Score: 40.12  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 102 LSYPVFKGIMKKGYK-VPTPIQRKTIPVILDGKDVVAMARTGSGKTACfllpmFERLKARSAQTGARALILSPTRELALQ 180
Cdd:cd18024    16 ISAHKPPGNPARTYPfTLDPFQKTAIACIERNESVLVSAHTSAGKTVV-----AEYAIAQSLRDKQRVIYTSPIKALSNQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 181 TMK-FTKELGKfTGLKTalilgGDkmedqfAALHENPDIIIATPGRLVHVAVEMNLKLQSVEYVVFDEA----DRlfEMG 255
Cdd:cd18024    91 KYReLQEEFGD-VGLMT-----GD------VTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIhymrDK--ERG 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1046854579 256 FAeqLQEIIGRLPGGHQTVLFSATLPKLLvEFAR 289
Cdd:cd18024   157 VV--WEETIILLPDKVRYVFLSATIPNAR-QFAE 187
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 120-248 3.23e-03

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


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 39.93  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046854579 120 PIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFerlkARSAQTGARALILSPTreLALqtMK-FTKELGKFtgLKTAL 198
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL----LLRRRGPGLTLVVSPL--IAL--MKdQVDALPRA--IKAAA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046854579 199 ILGGDKMEDQFAALHE----NPDIIIATPGRLVHVA-VEMNLKLQSVEYVVFDEA 248
Cdd:cd18018    85 LNSSLTREERRRILEKlragEVKILYVSPERLVNESfRELLRQTPPISLLVVDEA 139
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 141-190 6.58e-03

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 39.97  E-value: 6.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046854579 141 TGSGKTACFLLPMferlkARSAQTGARALILSPTRELALQTMKFTKELGK 190
Cdd:COG3505     8 TGSGKTVGLVIPN-----LTQLARGESVVVTDPKGDLAELTAGFRRRAGY 52
 
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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