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Conserved domains on  [gi|1050399450|gb|OCU01640|]
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hypothetical protein XELAEV_18007432mg [Xenopus laevis]

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

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 ...
75-279 2.27e-151

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: 442.13  E-value: 2.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  75 GGFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRGLILSPT 154
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEM 234
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 235 GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
290-421 5.30e-44

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: 154.97  E-value: 5.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 290 LKLSFFNVRVEDKPAVLLHLLrCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVR 369
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1050399450 370 ALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYSFI 421
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
679-739 9.80e-20

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


:

Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 83.49  E-value: 9.80e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 679 DLLGDHTEDLKKNKQVLK---WDRKKKKFVGTGGQED--KKKIKTESGRLISSSYKKNLYEGWKKK 739
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 ...
75-279 2.27e-151

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: 442.13  E-value: 2.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  75 GGFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRGLILSPT 154
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEM 234
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 235 GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
77-441 8.12e-138

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 415.70  E-value: 8.12e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQtGVRGLILSPTRE 156
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGF 236
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 237 AEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRcvVKP 316
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 317 QEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPP 396
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 397 KAKLFLHRVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIE 365
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
92-441 5.48e-86

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 280.68  E-value: 5.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL----KAHSAQTgvRGLILSPTRELALQTLKFTKE 167
Cdd:PRK11192   18 DKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGPP--RILILTPTRELAMQVADQARE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 168 LGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISrl 247
Cdd:PRK11192   96 LAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAA-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 248 pETR---QTLLFSATLP-KMLLEFARAGLTEPVLIrlDVDTKLSDQLKLSFFNVRVED---KPAVLLHLLRcvvKPQ-EQ 319
Cdd:PRK11192  174 -ETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKIHQWYYRADDlehKTALLCHLLK---QPEvTR 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 320 TVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAK 399
Cdd:PRK11192  248 SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSAD 327
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 400 LFLHRVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:PRK11192  328 TYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
99-267 5.22e-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: 211.72  E-value: 5.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  99 TPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHsaQTGVRGLILSPTRELALQTLKFTKELGKFTGLKTAL 178
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 179 ILGGDRMEDQFAALHeNPDIIIATPGRLMHVAIEMNlKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFSA 258
Cdd:pfam00270  79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 1050399450 259 TLPKMLLEF 267
Cdd:pfam00270 157 TLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
92-279 7.50e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.00  E-value: 7.50e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450   92 KKGYKVPTPIQRKVVPVILDG-KDVVAMARTGSGKTACFLIPMFEKLKAHSaqtGVRGLILSPTRELALQTLKFTKELGK 170
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  171 FTGLKTALILGGDRMEDQFAAL-HENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPE 249
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190
                   ....*....|....*....|....*....|
gi 1050399450  250 TRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFID 189
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
290-421 5.30e-44

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: 154.97  E-value: 5.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 290 LKLSFFNVRVEDKPAVLLHLLrCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVR 369
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1050399450 370 ALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYSFI 421
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
301-412 1.19e-25

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: 101.90  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 301 DKPAVLLHLLRCvvKPQEQTVIFVATKHHAEyLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARG 380
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1050399450 381 IDIPMLDNVINYNFPPKAKLFLHRVGRVARAG 412
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
679-739 9.80e-20

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


Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 83.49  E-value: 9.80e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 679 DLLGDHTEDLKKNKQVLK---WDRKKKKFVGTGGQED--KKKIKTESGRLISSSYKKNLYEGWKKK 739
Cdd:pfam08147   1 DLTGDDGQELNQQKQVQKkmrWDKKKKKFVKRSGNDEdgKKKIRTESGVKIPASYKSGRYDEWKKK 66
HELICc smart00490
helicase superfamily c-terminal domain;
331-412 6.75e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.87  E-value: 6.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  331 EYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVAR 410
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1050399450  411 AG 412
Cdd:smart00490  81 AG 82
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
302-428 8.53e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 39.71  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 302 KPAVLLHLL--RCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPC------SHIYSS--LDQTARKINLGLFLHGKVRAL 371
Cdd:COG1111   336 KLSKLREILkeQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVL 415
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 372 LVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARaGRSGTAYSFIAP---DEIPY 428
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAKgtrDEAYY 474
 
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 ...
75-279 2.27e-151

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: 442.13  E-value: 2.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  75 GGFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRGLILSPT 154
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEM 234
Cdd:cd17959    81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 235 GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17959   161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
77-441 8.12e-138

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 415.70  E-value: 8.12e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQtGVRGLILSPTRE 156
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-APQALILAPTRE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGF 236
Cdd:COG0513    83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 237 AEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRcvVKP 316
Cdd:COG0513   163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLR--DED 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 317 QEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPP 396
Cdd:COG0513   241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 397 KAKLFLHRVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:COG0513   321 DPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIE 365
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
88-279 3.50e-86

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: 272.39  E-value: 3.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  88 KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQT--GVRGLILSPTRELALQTLKFT 165
Cdd:cd00268     3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgrGPQALVLAPTRELAMQIAEVA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 166 KELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIIS 245
Cdd:cd00268    83 RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILS 162
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050399450 246 RLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd00268   163 ALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
92-441 5.48e-86

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 280.68  E-value: 5.48e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL----KAHSAQTgvRGLILSPTRELALQTLKFTKE 167
Cdd:PRK11192   18 DKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfpRRKSGPP--RILILTPTRELAMQVADQARE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 168 LGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISrl 247
Cdd:PRK11192   96 LAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAA-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 248 pETR---QTLLFSATLP-KMLLEFARAGLTEPVLIrlDVDTKLSDQLKLSFFNVRVED---KPAVLLHLLRcvvKPQ-EQ 319
Cdd:PRK11192  174 -ETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEV--EAEPSRRERKKIHQWYYRADDlehKTALLCHLLK---QPEvTR 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 320 TVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAK 399
Cdd:PRK11192  248 SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSAD 327
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 400 LFLHRVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:PRK11192  328 TYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
94-441 1.42e-78

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 261.66  E-value: 1.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  94 GYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAhsAQTGVRGLILSPTRELALQTLKFTKELGKFT- 172
Cdd:PRK11776   23 GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV--KRFRVQALVLCPTRELADQVAKEIRRLARFIp 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 173 GLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQ 252
Cdd:PRK11776  101 NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQ 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 253 TLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLS--DQLklsFFNVRVEDKPAVLLHLLRCVvKPqEQTVIFVATKHHA 330
Cdd:PRK11776  181 TLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPaiEQR---FYEVSPDERLPALQRLLLHH-QP-ESCVVFCNTKKEC 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 331 EYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVAR 410
Cdd:PRK11776  256 QEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGR 335
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1050399450 411 AGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:PRK11776  336 AGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
77-440 6.00e-75

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 252.04  E-value: 6.00e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTG----VRGLILS 152
Cdd:PRK10590    3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpVRALILT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 153 PTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLF 232
Cdd:PRK10590   83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 233 EMGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRc 312
Cdd:PRK10590  163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 313 vVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINY 392
Cdd:PRK10590  242 -KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1050399450 393 NFPPKAKLFLHRVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPL 440
Cdd:PRK10590  321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
29-441 5.03e-67

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 230.95  E-value: 5.03e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  29 RVKAAPQKDDGVH--LPAFPTADAGSDSEAEPDTRELVRAQNKKKKKS---------------GGFQSMGLSYPVYKGVM 91
Cdd:PRK01297   24 PAAAPAPPPPAKTaaPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASlwkledfvvepqegkTRFHDFNLAPELMHAIH 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTG-----VRGLILSPTRELALQTLKFTK 166
Cdd:PRK01297  104 DLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgePRALIIAPTRELVVQIAKDAA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 167 ELGKFTGLKTALILGGDRMEDQFAALHEN-PDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIIS 245
Cdd:PRK01297  184 ALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIR 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 246 RLP--ETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRcvVKPQEQTVIF 323
Cdd:PRK01297  264 QTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVT--QNPWERVMVF 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 324 VATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLH 403
Cdd:PRK01297  342 ANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVH 421
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1050399450 404 RVGRVARAGRSGTAYSFIAPDEIPYVYDLHLFLGRPLK 441
Cdd:PRK01297  422 RIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
88-279 8.85e-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: 220.59  E-value: 8.85e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  88 KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGV-RGLILSPTRELALQTLKFTK 166
Cdd:cd17947     3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAAtRVLVLVPTRELAMQCFSVLQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 167 ELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIIS 245
Cdd:cd17947    83 QLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILR 162
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050399450 246 RLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17947   163 LCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
77-433 7.55e-66

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 226.01  E-value: 7.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGV-----RGLIL 151
Cdd:PRK04837   10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvnqpRALIM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 152 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRL 231
Cdd:PRK04837   90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 232 FEMGFAEQLQEIISRLPET--RQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHL 309
Cdd:PRK04837  170 FDLGFIKDIRWLFRRMPPAnqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 310 L------RCvvkpqeqtVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDI 383
Cdd:PRK04837  250 IeeewpdRA--------IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1050399450 384 PMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYSFiAPDEipYVYDLH 433
Cdd:PRK04837  322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL-ACEE--YALNLP 368
PTZ00110 PTZ00110
helicase; Provisional
83-425 3.95e-65

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 227.73  E-value: 3.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  83 SYPVY--KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLkahSAQTGVRG------LILSPT 154
Cdd:PTZ00110  136 SFPDYilKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI---NAQPLLRYgdgpivLVLAPT 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEM 234
Cdd:PTZ00110  213 RELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDM 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 235 GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTE-PVLIRL-DVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRC 312
Cdd:PTZ00110  293 GFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQR 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 313 VVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINY 392
Cdd:PTZ00110  373 IMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINF 452
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1050399450 393 NFPPKAKLFLHRVGRVARAGRSGTAYSFIAPDE 425
Cdd:PTZ00110  453 DFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
99-267 5.22e-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: 211.72  E-value: 5.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  99 TPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHsaQTGVRGLILSPTRELALQTLKFTKELGKFTGLKTAL 178
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL--DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 179 ILGGDRMEDQFAALHeNPDIIIATPGRLMHVAIEMNlKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFSA 258
Cdd:pfam00270  79 LLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156

                  ....*....
gi 1050399450 259 TLPKMLLEF 267
Cdd:pfam00270 157 TLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
77-420 4.64e-62

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 219.82  E-value: 4.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTG-----VRGLIL 151
Cdd:PRK04537   11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADrkpedPRALIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 152 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADR 230
Cdd:PRK04537   91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIdYVKQHKVVSLHACEICVLDEADR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 231 LFEMGFAEQLQEIISRLPE--TRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLH 308
Cdd:PRK04537  171 MFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 309 LLRcvVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDN 388
Cdd:PRK04537  251 LLS--RSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1050399450 389 VINYNFPPKAKLFLHRVGRVARAGRSGTAYSF 420
Cdd:PRK04537  329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
77-421 1.22e-61

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 220.10  E-value: 1.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVrgLILSPTRE 156
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQI--LVLAPTRE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGK-FTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMG 235
Cdd:PRK11634   86 LAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 236 FAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLRcvVK 315
Cdd:PRK11634  166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLE--AE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 316 PQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFP 395
Cdd:PRK11634  244 DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIP 323
                         330       340
                  ....*....|....*....|....*.
gi 1050399450 396 PKAKLFLHRVGRVARAGRSGTAYSFI 421
Cdd:PRK11634  324 MDSESYVHRIGRTGRAGRAGRALLFV 349
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
77-278 1.32e-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: 201.39  E-value: 1.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHsaQTGVRGLILSPTRE 156
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN--PQRFFALVLAPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRLFEMG 235
Cdd:cd17954    80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVdHLENTKGFSLKSLKFLVMDEADRLLNMD 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1050399450 236 FAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17954   160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
94-278 1.97e-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: 200.51  E-value: 1.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  94 GYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRGLILSPTRELALQTLKFTKELGKFTG 173
Cdd:cd17957     9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLSKGTG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 174 LKTALILGGDR-MEDQFAALHENPDIIIATPGRLMHvAIEMNLK-LRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETR 251
Cdd:cd17957    89 LRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVF-LLKQGPIdLSSVEYLVLDEADKLFEPGFREQTDEILAACTNPN 167
                         170       180
                  ....*....|....*....|....*...
gi 1050399450 252 -QTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17957   168 lQRSLFSATIPSEVEELARSVMKDPIRI 195
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
77-278 2.02e-57

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: 195.52  E-value: 2.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSaqTGVRGLILSPTRE 156
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP--YGIFALVLTPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HV--AIEMNLKLRSVEYVVFDEADRLFE 233
Cdd:cd17955    79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLrsSDDTTKVLSRVKFLVLDEADRLLT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 234 MGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
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, ...
94-279 3.05e-57

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: 194.72  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  94 GYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQ---TGVRGLILSPTRELALQTLKFTKELGK 170
Cdd:cd17960     9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANlkkGQVGALIISPTRELATQIYEVLQSFLE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 171 FTG--LKTALILGGDRMEDQFAALHEN-PDIIIATPGRL--MHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIIS 245
Cdd:cd17960    89 HHLpkLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLeeLLSRKADKVKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050399450 246 RLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17960   169 KLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
81-278 1.56e-55

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 190.67  E-value: 1.56e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  81 GLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAH---SAQTGVRGLILSPTREL 157
Cdd:cd17953    18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpvKPGEGPIGLIMAPTREL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 158 ALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVaIEMN----LKLRSVEYVVFDEADRLFE 233
Cdd:cd17953    98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDI-LTANngrvTNLRRVTYVVLDEADRMFD 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 234 MGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17953   177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
88-278 2.99e-55

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: 189.04  E-value: 2.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  88 KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL--KAHSAQTGVRGLILSPTRELALQTLKFT 165
Cdd:cd17941     3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrERWTPEDGLGALIISPTRELAMQIFEVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 166 KELGKFTGLKTALILGGDRMEDQFAALHENpDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEII 244
Cdd:cd17941    83 RKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050399450 245 SRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17941   162 ENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
90-278 9.88e-55

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: 187.62  E-value: 9.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  90 VMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL---KAHSAQTGVRGLILSPTRELALQTLKFTK 166
Cdd:cd17952     5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVIVAPTRELAQQIYLEAK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 167 ELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISR 246
Cdd:cd17952    85 KFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH 164
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1050399450 247 LPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
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 ...
90-278 2.51e-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: 184.83  E-value: 2.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  90 VMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFE------KLKAHSAQTGVRGLILSPTRELALQTLK 163
Cdd:cd17945     5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisrlpPLDEETKDDGPYALILAPTRELAQQIEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 164 FTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEI 243
Cdd:cd17945    85 ETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKI 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1050399450 244 ISRLPET--------------------RQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17945   165 LDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
PTZ00424 PTZ00424
helicase 45; Provisional
45-426 4.27e-53

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 190.04  E-value: 4.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  45 FPTADAGSDSEAEPDTRELVRAqnkkkkksggFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSG 124
Cdd:PTZ00424    8 NQSEQVASTGTIESNYDEIVDS----------FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 125 KTACFLIPMFEKLKAHSAQTGVrgLILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPG 204
Cdd:PTZ00424   78 KTATFVIAALQLIDYDLNACQA--LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 205 RLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDT 284
Cdd:PTZ00424  156 RVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 285 KLSDQLKLSFFNVRVED-KPAVLLHLLRCVVKpqEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLF 363
Cdd:PTZ00424  236 LTLEGIRQFYVAVEKEEwKFDTLCDLYETLTI--TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREF 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1050399450 364 LHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYSFIAPDEI 426
Cdd:PTZ00424  314 RSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDI 376
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
77-262 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: 180.76  E-value: 5.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL--------KAHSAQTGVRG 148
Cdd:cd17967     2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAYPSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 149 LILSPTRELALQ----TLKFTKElgkfTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVaIEMN-LKLRSVEYV 223
Cdd:cd17967    82 LILAPTRELAIQiyeeARKFSYR----SGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDF-IERGrISLSSIKFL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1050399450 224 VFDEADRLFEMGFAEQLQEIISR----LPETRQTLLFSATLPK 262
Cdd:cd17967   157 VLDEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPR 199
DEXDc smart00487
DEAD-like helicases superfamily;
92-279 7.50e-52

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 180.00  E-value: 7.50e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450   92 KKGYKVPTPIQRKVVPVILDG-KDVVAMARTGSGKTACFLIPMFEKLKAHSaqtGVRGLILSPTRELALQTLKFTKELGK 170
Cdd:smart00487   3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK---GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  171 FTGLKTALILGGDRMEDQFAAL-HENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPE 249
Cdd:smart00487  80 SLGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
                          170       180       190
                   ....*....|....*....|....*....|
gi 1050399450  250 TRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFID 189
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
77-421 3.91e-51

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 187.69  E-value: 3.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFE-----KLKAHSAQTGVRGLIL 151
Cdd:PLN00206  123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctiRSGHPSEQRNPLAMVL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 152 SPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRL 231
Cdd:PLN00206  203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 232 FEMGFAEQLQEIISRLPeTRQTLLFSATLPKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLSFFNVRVEDKPAVLLHLLR 311
Cdd:PLN00206  283 LERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 312 CVVKPQEQTVIFVATKHHAEYLRELLDM-QGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVI 390
Cdd:PLN00206  362 SKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1050399450 391 NYNFPPKAKLFLHRVGRVARAGRSGTAYSFI 421
Cdd:PLN00206  442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
88-260 5.27e-51

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: 177.78  E-value: 5.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  88 KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKL---KAHSAQT-GVRGLILSPTRELALQTLK 163
Cdd:cd17961     7 KAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkaKAESGEEqGTRALILVPTRELAQQVSK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 164 FTKELGKFTG--LKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRS-VEYVVFDEADRLFEMGFAEQL 240
Cdd:cd17961    87 VLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEEDL 166
                         170       180
                  ....*....|....*....|
gi 1050399450 241 QEIISRLPETRQTLLFSATL 260
Cdd:cd17961   167 KSLLSYLPKNYQTFLMSATL 186
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
77-278 8.12e-51

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: 177.10  E-value: 8.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKahSAQTGVRGLILSPTRE 156
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID--PKKDVIQALILVPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGF 236
Cdd:cd17940    79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 237 AEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17940   159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
82-272 8.63e-51

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: 177.39  E-value: 8.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  82 LSYPVYKGVMKKGYKVPTPIQRKVVPVIL-DGKDVVAMARTGSGKTACFLIPMFEKL---KAHSAQTGVRGLILSPTREL 157
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntKPAGRRSGVSALIISPTREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 158 ALQTLK-FTKELGKFTGLKTALILGG-DRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLK-LRSVEYVVFDEADRLFE 233
Cdd:cd17964    81 ALQIAAeAKKLLQGLRKLRVQSAVGGtSRRAELNRLRRGRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEADRLLD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1050399450 234 MGFAEQLQEIISRLP----ETRQTLLFSATLPKMLLEFARAGL 272
Cdd:cd17964   161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTL 203
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
86-278 9.79e-49

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: 171.37  E-value: 9.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  86 VYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMF------EKLKAHSAQTGVRGLILSPTRELAL 159
Cdd:cd17951     1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 160 QTLK----FTKEL--GKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFE 233
Cdd:cd17951    81 QTHEvieyYCKALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 234 MGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17951   161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
80-278 3.88e-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: 169.43  E-value: 3.88e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  80 MGLSYPVYKGVMKKGYKVPTPI-QRKVVPvILDGKDVVAMARTGSGKTACFLIPMFEKLKahSAQTGVRGLILSPTRELA 158
Cdd:cd17939     2 MGLSEDLLRGIYAYGFEKPSAIqQRAIVP-IIKGRDVIAQAQSGTGKTATFSIGALQRID--TTVRETQALVLAPTRELA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 159 LQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAE 238
Cdd:cd17939    79 QQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKD 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1050399450 239 QLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17939   159 QIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
88-306 1.81e-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: 168.96  E-value: 1.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  88 KGVMKKGYKVPTPIQRKVVPV-ILDGKDVVAMARTGSGKTACFLIPMFEKL-------KAHSAQTGVRGLILSPTRELAL 159
Cdd:cd17946     3 RALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKPLRALILTPTRELAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 160 QTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNL---KLRSVEYVVFDEADRLFEMGF 236
Cdd:cd17946    83 QVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEKGH 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050399450 237 AEQLQEIISRLPET-------RQTLLFSATLpKMLLEFARAGLTEPVLIRLDVDTKLSDQLKLsffnVRVEDKPAVL 306
Cdd:cd17946   163 FAELEKILELLNKDragkkrkRQTFVFSATL-TLDHQLPLKLNSKKKKKKKEKKQKLELLIEK----VGFRKKPKVI 234
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
86-278 1.27e-46

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: 165.23  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  86 VYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAH---SAQTGVRGLILSPTRELALQTL 162
Cdd:cd17966     1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQpplERGDGPIVLVLAPTRELAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 163 KFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQE 242
Cdd:cd17966    81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1050399450 243 IISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17966   161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
92-278 2.22e-46

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


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 164.26  E-value: 2.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFekLKAHSAQTGVRGLILSPTRELALQTLKFTKELGK- 170
Cdd:cd17962     7 KAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI--IRCLTEHRNPSALILTPTRELAVQIEDQAKELMKg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 171 FTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPET 250
Cdd:cd17962    85 LPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
                         170       180
                  ....*....|....*....|....*...
gi 1050399450 251 RQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17962   165 HQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
86-278 3.92e-44

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 158.01  E-value: 3.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  86 VYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRG----LILSPTRELALQT 161
Cdd:cd17958     1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNgpgvLVLTPTRELALQI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 162 LKFTKELgKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQ 241
Cdd:cd17958    81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1050399450 242 EIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd17958   160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
290-421 5.30e-44

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: 154.97  E-value: 5.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 290 LKLSFFNVRVEDKPAVLLHLLrCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVR 369
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1050399450 370 ALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYSFI 421
Cdd:cd18787    80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
87-278 3.67e-43

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: 155.21  E-value: 3.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  87 YKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFE---KLKaHSAQTGVRGLILSPTRELALQTLK 163
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLK-FKPRNGTGVIIISPTRELALQIYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 164 FTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQE 242
Cdd:cd17942    81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1050399450 243 IISRLPETRQTLLFSATLPKMLLEFARAGL-TEPVLI 278
Cdd:cd17942   161 IIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYV 197
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
86-279 2.07e-42

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 152.80  E-value: 2.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  86 VYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVrgLILSPTRELALQTLKFT 165
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQV--LILAPTREIAVQIHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 166 KELG-KFTGLKTALILGGDRMEDQFAALhENPDIIIATPGRLMHVaIEMN-LKLRSVEYVVFDEADRLFEMGFAEQLQEI 243
Cdd:cd17943    79 KKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQL-IELGaLNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1050399450 244 ISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17943   157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
77-260 2.51e-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: 150.16  E-value: 2.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKlkahsaqtgVRGLILSPTRE 156
Cdd:cd17938     1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI---------VVALILEPSRE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTG---LKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFE 233
Cdd:cd17938    72 LAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLS 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050399450 234 MGFAEQLQEIISRLP-----ETR-QTLLFSATL 260
Cdd:cd17938   152 QGNLETINRIYNRIPkitsdGKRlQVIVCSATL 184
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
77-261 5.52e-41

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: 151.27  E-value: 5.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAH----SAQTGVR---GL 149
Cdd:cd18052    45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltaSSFSEVQepqAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 150 ILSPTRELALQTLkftKELGKF---TGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFD 226
Cdd:cd18052   125 IVAPTRELANQIF---LEARKFsygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1050399450 227 EADRLFEMGFAEQLQEIISRL----PETRQTLLFSATLP 261
Cdd:cd18052   202 EADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFP 240
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
94-279 1.65e-40

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: 148.50  E-value: 1.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  94 GYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQ----TGVRGLILSPTRELALQTLK-FTKEL 168
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsDGTLALVLVPTRELALQIYEvLEKLL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 169 GKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRL 247
Cdd:cd17949    90 KPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050399450 248 -------------PETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17949   170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
95-269 2.25e-39

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 146.34  E-value: 2.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  95 YKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIP----MFEKLKAHSAQTGVRG----------LILSPTRELALQ 160
Cdd:cd18051    41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsqIYEQGPGESLPSESGYygrrkqyplaLVLAPTRELASQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 161 TLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQL 240
Cdd:cd18051   121 IYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQI 200
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050399450 241 QEIISR--LPET--RQTLLFSATLPKMLLEFAR 269
Cdd:cd18051   201 RRIVEQdtMPPTgeRQTLMFSATFPKEIQMLAR 233
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
77-278 4.79e-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: 140.68  E-value: 4.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTgvRGLILSPTRE 156
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRET--QALILSPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGF 236
Cdd:cd18045    79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 237 AEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd18045   159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
82-279 5.97e-38

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: 140.40  E-value: 5.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  82 LSYPVYKGVMKKGYKVPTPIQRKVVPVILDG--KDVVAMARTGSGKTACFLIPMFEKLKAHSAQTgvRGLILSPTRELAL 159
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSP--QALCLAPTRELAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 160 QTLKFTKELGKFTGLKTALIL------GGDRMEDQfaalhenpdIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFE 233
Cdd:cd17963    79 QIGEVVEKMGKFTGVKVALAVpgndvpRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1050399450 234 M-GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd17963   150 TqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
77-278 6.21e-37

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: 137.58  E-value: 6.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTgvRGLILSPTRE 156
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT--QALVLAPTRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 157 LALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGF 236
Cdd:cd18046    79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 237 AEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLI 278
Cdd:cd18046   159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
83-280 2.48e-36

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: 137.06  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  83 SYPVY--KGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAH---SAQTGVRGLILSPTREL 157
Cdd:cd18049    30 NFPANvmDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpflERGDGPICLVLAPTREL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 158 ALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFA 237
Cdd:cd18049   110 AQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1050399450 238 EQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRL 280
Cdd:cd18049   190 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
76-280 1.36e-34

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 133.21  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  76 GFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAH---SAQTGVRGLILS 152
Cdd:cd18050    63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylERGDGPICLVLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 153 PTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLF 232
Cdd:cd18050   143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 222
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050399450 233 EMGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRL 280
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 ...
100-269 4.72e-34

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: 129.58  E-value: 4.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 100 PIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSaQTGVRG-----LILSPTRELALQTLKFTKELGKftGL 174
Cdd:cd17944    15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQ-QPRKRGrapkvLVLAPTRELANQVTKDFKDITR--KL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 175 KTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIIS----RLPET 250
Cdd:cd17944    92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykKDSED 171
                         170       180
                  ....*....|....*....|
gi 1050399450 251 R-QTLLFSATLPKMLLEFAR 269
Cdd:cd17944   172 NpQTLLFSATCPDWVYNVAK 191
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
92-266 7.00e-33

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: 127.10  E-value: 7.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGV-----RGLILSPTRELALQTLKFTK 166
Cdd:cd17948     7 RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfnapRGLVITPSRELAEQIGSVAQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 167 ELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISR 246
Cdd:cd17948    87 SLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1050399450 247 LP--ETR-----------QTLLFSATLPKMLLE 266
Cdd:cd17948   167 FPlaSRRsentdgldpgtQLVLVSATMPSGVGE 199
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
74-262 1.89e-31

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: 122.07  E-value: 1.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  74 SGGFQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVrgLILSP 153
Cdd:cd17950     1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSV--LVICH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 154 TRELALQTLKFTKELGKF-TGLKTALILGGDRMEDQFAALHEN-PDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRL 231
Cdd:cd17950    79 TRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1050399450 232 FE-MGFAEQLQEIISRLPETRQTLLFSATLPK 262
Cdd:cd17950   159 LEqLDMRRDVQEIFRATPHDKQVMMFSATLSK 190
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
92-260 2.63e-29

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: 116.58  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDG---------KDVVAMARTGSGKTACFLIPMFEKLKAHSAqTGVRGLILSPTRELALQTL 162
Cdd:cd17956     7 NNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVV-PRLRALIVVPTKELVQQVY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 163 KFTKELGKFTGLKTALiLGGDR---------MEDQFAALHENPDIIIATPGRLM-HVAIEMNLKLRSVEYVVFDEADRL- 231
Cdd:cd17956    86 KVFESLCKGTGLKVVS-LSGQKsfkkeqkllLVDTSGRYLSRVDILVATPGRLVdHLNSTPGFTLKHLRFLVIDEADRLl 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1050399450 232 ---FEmGFAEQLQEIISRLPETR-----------------QTLLFSATL 260
Cdd:cd17956   165 nqsFQ-DWLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATL 212
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
301-412 1.19e-25

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: 101.90  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 301 DKPAVLLHLLRCvvKPQEQTVIFVATKHHAEyLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARG 380
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1050399450 381 IDIPMLDNVINYNFPPKAKLFLHRVGRVARAG 412
Cdd:pfam00271  78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
77-280 5.16e-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: 104.33  E-value: 5.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVILDG--KDVVAMARTGSGKTACFLIPMFEKLKAHsaQTGVRGLILSPT 154
Cdd:cd18048    20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL--KLYPQCLCLSPT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKF-TGLKTALILGGDR------MEDQfaalhenpdIIIATPGRLMHVAIEMNL-KLRSVEYVVFD 226
Cdd:cd18048    98 FELALQTGKVVEEMGKFcVGIQVIYAIRGNRpgkgtdIEAQ---------IVIGTPGTVLDWCFKLRLiDVTNISVFVLD 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1050399450 227 EADRLFEM-GFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIRL 280
Cdd:cd18048   169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL 223
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
77-264 2.41e-23

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: 100.14  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLsYPVYKGVMKK----------GYKVPTPIQRKVVPVIL------------DGKD-----VVAmARTGSGKTACF 129
Cdd:cd17965     1 FDQLKL-LPSVREAIIKeilkgsnktdEEIKPSPIQTLAIKKLLktlmrkvtkqtsNEEPklevfLLA-AETGSGKTLAY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 130 LIPMFEKLKAHSAQTG---------------VRGLILSPTRELALQTLKFTKELGKFTGLKTALILG--GDRMEDQFAAL 192
Cdd:cd17965    79 LAPLLDYLKRQEQEPFeeaeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAF 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1050399450 193 HENPDIIIATPGRLMHVA-IEMNLkLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFSATLPKML 264
Cdd:cd17965   159 KGRIDILVTTPGKLASLAkSRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEF 230
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
115-424 2.58e-22

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 102.03  E-value: 2.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 115 VVAMArTGSGKT--ACFLIpmfeklkaHSAQTGVRGLILSPTRELALQTLKftkELGKFTGLKtalILGGDRMEDQFaal 192
Cdd:COG1061   104 LVVAP-TGTGKTvlALALA--------AELLRGKRVLVLVPRRELLEQWAE---ELRRFLGDP---LAGGGKKDSDA--- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 193 henpDIIIATPGRLMHVAIEMNLKlRSVEYVVFDEADRLFemgfAEQLQEIISRLPETRqTLLFSAT------LPKMLLE 266
Cdd:COG1061   166 ----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAG----APSYRRILEAFPAAY-RLGLTATpfrsdgREILLFL 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 267 F------------ARAG-LTEPVLIRLDVD--------TKLSDQL--KLSFFNVRvedKPAVLLHLLRcVVKPQEQTVIF 323
Cdd:COG1061   236 FdgivyeyslkeaIEDGyLAPPEYYGIRVDltderaeyDALSERLreALAADAER---KDKILRELLR-EHPDDRKTLVF 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 324 VATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVInYNFPPKAK-LFL 402
Cdd:COG1061   312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrEFI 390
                         330       340
                  ....*....|....*....|....*
gi 1050399450 403 HRVGRVARAGRSGTA---YSFIAPD 424
Cdd:COG1061   391 QRLGRGLRPAPGKEDalvYDFVGND 415
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
77-279 1.04e-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: 94.02  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  77 FQSMGLSYPVYKGVMKKGYKVPTPIQRKVVPVIL--DGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTgvRGLILSPT 154
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYP--QCLCLSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 155 RELALQTLKFTKELGKF-TGLKTALILGGDRMEdqfAALHENPDIIIATPGRLMHVAIEMNL-KLRSVEYVVFDEADRLF 232
Cdd:cd18047    81 YELALQTGKVIEQMGKFyPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKLKFiDPKKIKVFVLDEADVMI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050399450 233 -EMGFAEQLQEIISRLPETRQTLLFSATLPKMLLEFARAGLTEPVLIR 279
Cdd:cd18047   158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DBP10CT pfam08147
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ...
679-739 9.80e-20

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


Pssm-ID: 462373 [Multi-domain]  Cd Length: 66  Bit Score: 83.49  E-value: 9.80e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 679 DLLGDHTEDLKKNKQVLK---WDRKKKKFVGTGGQED--KKKIKTESGRLISSSYKKNLYEGWKKK 739
Cdd:pfam08147   1 DLTGDDGQELNQQKQVQKkmrWDKKKKKFVKRSGNDEdgKKKIRTESGVKIPASYKSGRYDEWKKK 66
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
102-424 3.67e-19

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: 92.59  E-value: 3.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 102 QRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSaqtGVRGLILSPTRELA---LQTL-KFTKELGkfTGLKTA 177
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP---GATALYLYPTKALArdqLRRLrELAEALG--LGVRVA 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 178 lILGGDRMEDQFAALHENPDIIIATPGRLmHVAIemnLK--------LRSVEYVVFDEA---------------DRlfem 234
Cdd:COG1205   136 -TYDGDTPPEERRWIREHPDIVLTNPDML-HYGL---LPhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRR---- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 235 gfaeqLQEIISRLPETRQTLLFSATL--PKmllEFARAgLT-EPV-LIrlDVDTKLSDQLKLSFFNVRVEDKPA------ 304
Cdd:COG1205   207 -----LRRICRHYGSDPQFILASATIgnPA---EHAER-LTgRPVtVV--DEDGSPRGERTFVLWNPPLVDDGIrrsala 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 305 ----VLLHLLRCVVkpqeQTVIFVATKHHAE----YLRELLDMQGIPcSHI--YSS--LDQTARKINLGLFlHGKVRAll 372
Cdd:COG1205   276 eaarLLADLVREGL----RTLVFTRSRRGAEllarYARRALREPDLA-DRVaaYRAgyLPEERREIERGLR-SGELLG-- 347
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1050399450 373 vtdVAAR-----GIDIPMLDNVINYNFPPKAKLFLHRVGRVARAGRSGTAYsFIAPD 424
Cdd:COG1205   348 ---VVSTnalelGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGD 400
HELICc smart00490
helicase superfamily c-terminal domain;
331-412 6.75e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.87  E-value: 6.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  331 EYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVAR 410
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 1050399450  411 AG 412
Cdd:smart00490  81 AG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
112-259 3.71e-15

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 73.21  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 112 GKDVVAMARTGSGKTACFLIPMFEklkaHSAQTGVRGLILSPTRELALQTLKFTKELGKfTGLKTALILGGDRMEDQFAA 191
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALL----LLLKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKN 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1050399450 192 LHENPDIIIATPGRL-MHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQL--QEIISRLPETRQTLLFSAT 259
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 ...
109-228 8.27e-14

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: 70.31  E-value: 8.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 109 ILDGKDVVAMARTGSGKTACFLIPMFEKLkahSAQTGVRGLILSPTRELA---LQTL-KFTKELGkfTGLKTALILGGDR 184
Cdd:cd17923    12 ARAGRSVVVTTGTASGKSLCYQLPILEAL---LRDPGSRALYLYPTKALAqdqLRSLrELLEQLG--LGIRVATYDGDTP 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1050399450 185 MEDQFAALHENPDIIIATPGRLmHVAIemnLK--------LRSVEYVVFDEA 228
Cdd:cd17923    87 REERRAIIRNPPRILLTNPDML-HYAL---LPhhdrwarfLRNLRYVVLDEA 134
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
99-261 1.21e-13

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: 69.98  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  99 TPIQRKVV-PVILDGKDVVAMARTGSGKTACFLIPMFEKLkahsAQTGVRGLILSPTRELALQTLK-FTKELGKFtGLKT 176
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRAL----ATSGGKAVYIAPTRALVNQKEAdLRERFGPL-GKNV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 177 ALILGGDRMEDQFAAlheNPDIIIATPGRL--MHVAIEmNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLP---ETR 251
Cdd:cd17921    78 GLLTGDPSVNKLLLA---EADILVATPEKLdlLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNA 153
                         170
                  ....*....|
gi 1050399450 252 QTLLFSATLP 261
Cdd:cd17921   154 RFVGLSATLP 163
PRK13767 PRK13767
ATP-dependent helicase; Provisional
92-407 3.76e-13

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 73.38  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVPVILDGKDVVAMARTGSGKT-ACFLI---PMFEKLKAHSAQTGVRGLILSPTRELA-------LQ 160
Cdd:PRK13767   27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAiidELFRLGREGELEDKVYCLYVSPLRALNndihrnlEE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 161 TLKFTKELGKFTGLKTALILGGDRMEDQFAA-----LHENPDIIIATPGRLmhvAIEMNL-----KLRSVEYVVFDEADR 230
Cdd:PRK13767  107 PLTEIREIAKERGEELPEIRVAIRTGDTSSYekqkmLKKPPHILITTPESL---AILLNSpkfreKLRTVKWVIVDEIHS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 231 LFE-------MGFAEQLQEIISRlPETRQTLlfSATL-P-----KMLLEFARAGLTEPVLIrldVDTKLSDQLKLS---- 293
Cdd:PRK13767  184 LAEnkrgvhlSLSLERLEELAGG-EFVRIGL--SATIePleevaKFLVGYEDDGEPRDCEI---VDARFVKPFDIKvisp 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 294 ---FFNVRVEDKPAVLLHLLRCVVKPQEQTVIFVATKHHAE----YLRELL----DMQGIPCSHiySSLDQTAR-KINLG 361
Cdd:PRK13767  258 vddLIHTPAEEISEALYETLHELIKEHRTTLIFTNTRSGAErvlyNLRKRFpeeyDEDNIGAHH--SSLSREVRlEVEEK 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1050399450 362 LfLHGKVRALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGR 407
Cdd:PRK13767  336 L-KRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
92-343 2.23e-12

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 70.31  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  92 KKGYKVPTPIQRKVVP-VILDGKDVVAMARTGSGKTACFLIPMFeklkaHSAQTGVRGLILSPTRELALQ-TLKFTKELG 169
Cdd:COG1204    17 ERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAIL-----KALLNGGKALYIVPLRALASEkYREFKRDFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 170 KFtGLKTAlILGGDRMEDqfAALHENPDIIIATPGR---LMHVAIEMnlkLRSVEYVVFDEA------DRlfemGFaeQL 240
Cdd:COG1204    92 EL-GIKVG-VSTGDYDSD--DEWLGRYDILVATPEKldsLLRNGPSW---LRDVDLVVVDEAhliddeSR----GP--TL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 241 QEIISRL----PETrQTLLFSATLPKMlLEFAR---AGLTE----PVLIRLDVdtklsdqlkLSFFNVRVEDKPAV---- 305
Cdd:COG1204   159 EVLLARLrrlnPEA-QIVALSATIGNA-EEIAEwldAELVKsdwrPVPLNEGV---------LYDGVLRFDDGSRRskdp 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 306 LLHLLRCVVKPQEQTVIFVATKHHAE----YLRELLDMQGIP 343
Cdd:COG1204   228 TLALALDLLEEGGQVLVFVSSRRDAEslakKLADELKRRLTP 269
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
95-407 5.62e-09

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 59.73  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  95 YKVPTPIQRKVVPVILDGKDVVAMARTGSGKT-ACFLIP---MFEKLKAHSAQTGVRGLILSPTRELA------LQTlkF 164
Cdd:COG1201    22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPAldeLARRPRPGELPDGLRVLYISPLKALAndiernLRA--P 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 165 TKELGKFTGLKTALILGGDRMED----QFAALHEN-PDIIIATP-----------GRLMhvaiemnlkLRSVEYVVFDEa 228
Cdd:COG1201   100 LEEIGEAAGLPLPEIRVGVRTGDtpasERQRQRRRpPHILITTPeslallltspdAREL---------LRGVRTVIVDE- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 229 drLFEMgfAE-----QLQEIISRL----PETRQTLLFSATL--PKMLLEF-ARAGLTEPVLIrldVDTKLSDQLKLSFFn 296
Cdd:COG1201   170 --IHAL--AGskrgvHLALSLERLralaPRPLQRIGLSATVgpLEEVARFlVGYEDPRPVTI---VDAGAGKKPDLEVL- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 297 VRVEDKPAVL-------LHLLRCV---VKPQEQTVIFVATKHHAE----YLRELLDMQGIP--CSHiySSLDQTAR-KIN 359
Cdd:COG1201   242 VPVEDLIERFpwaghlwPHLYPRVldlIEAHRTTLVFTNTRSQAErlfqRLNELNPEDALPiaAHH--GSLSREQRlEVE 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1050399450 360 LGLfLHGKVRALlvtdVAAR----GIDIPMLDNVINYNFPPKAKLFLHRVGR 407
Cdd:COG1201   320 EAL-KAGELRAV----VATSslelGIDIGDVDLVIQVGSPKSVARLLQRIGR 366
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
94-283 6.99e-09

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: 56.39  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  94 GYKVPTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIP--MFEKLkahsaqtgvrGLILSPTreLAL---QTLKFTKel 168
Cdd:cd17920     9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV----------TLVVSPL--ISLmqdQVDRLQQ-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 169 gkfTGLKTALILGG----DRMEDQFAALHENPDIIIATPGRLMHVAIEMNLK----LRSVEYVVFDEA--------DrlF 232
Cdd:cd17920    75 ---LGIRAAALNSTlspeEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAhcvsqwghD--F 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1050399450 233 --EMGfaeQLQEIISRLPETrQTLLFSATLPKMLLE--FARAGLTEPVLIRLDVD 283
Cdd:cd17920   150 rpDYL---RLGRLRRALPGV-PILALTATATPEVREdiLKRLGLRNPVIFRASFD 200
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
102-395 9.67e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 58.61  E-value: 9.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 102 QRKVVPVILDGKDVVAMARTGSGKTACFLIP--MFEKLkahsaqtgvrGLILSPTreLALqtlkftkelgkftglktali 179
Cdd:COG0514    22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGL----------TLVVSPL--IAL-------------------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 180 lggdrMEDQFAALHEN---------------------------PDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEA---- 228
Cdd:COG0514    70 -----MKDQVDALRAAgiraaflnsslsaeerrevlralrageLKLLYVAPERLLNPRFLELLRRLKISLFAIDEAhcis 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 229 --------DRLfemgfaeQLQEIISRLPEtRQTLLFSATlpkmllefAraglTEPVliRLDVDTKLSDQ----------- 289
Cdd:COG0514   145 qwghdfrpDYR-------RLGELRERLPN-VPVLALTAT--------A----TPRV--RADIAEQLGLEdprvfvgsfdr 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 290 --LKLSFFNVRVEDKPAVLLHLLRcvVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGK 367
Cdd:COG0514   203 pnLRLEVVPKPPDDKLAQLLDFLK--EHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDE 280
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1050399450 368 VRALlvtdVA--A--RGIDIPMLDNVINYNFP 395
Cdd:COG0514   281 VDVI----VAtiAfgMGIDKPDVRFVIHYDLP 308
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
115-260 7.16e-08

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: 52.31  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 115 VVAMArTGSGKTACfLIPMFEKLKAHsaqtgvRGLILSPTRELALQTLkftKELGKFTGLKTALILGGDRMEDQFAAlhe 194
Cdd:cd17926    22 ILVLP-TGSGKTLT-ALALIAYLKEL------RTLIVVPTDALLDQWK---ERFEDFLGDSSIGLIGGGKKKDFDDA--- 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 195 npDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLfemgFAEQLQEIISRLPETRQtLLFSATL 260
Cdd:cd17926    88 --NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHL----PAKTFSEILKELNAKYR-LGLTATP 146
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
101-203 1.46e-07

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: 52.74  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 101 IQRKVVPVILDG-KDVVAMARTGSGKTACFLIPMFEKLKAH--SAQTGVRGLILSPTRELALQTLKFTKElgKF--TGLK 175
Cdd:cd18023     5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERnpLPWGNRKVVYIAPIKALCSEKYDDWKE--KFgpLGLS 82
                          90       100
                  ....*....|....*....|....*...
gi 1050399450 176 TALILGGDRMEDQFAAlhENPDIIIATP 203
Cdd:cd18023    83 CAELTGDTEMDDTFEI--QDADIILTTP 108
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
100-260 2.43e-07

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 54.56  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 100 PIQRKVVPVILDGKDVVAMARTGSGKT--ACFLIpmFEKLkahsaQTGVRGLILSPTRELALQtlKFtKELGKFTGLKTA 177
Cdd:COG4581    28 PFQEEAILALEAGRSVLVAAPTGSGKTlvAEFAI--FLAL-----ARGRRSFYTAPIKALSNQ--KF-FDLVERFGAENV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 178 LILGGDRmedqfaalHENPD--IIIATpgrlmhvaIEM--NLKLR------SVEYVVFDE----ADRlfEMGFAeqLQEI 243
Cdd:COG4581    98 GLLTGDA--------SVNPDapIVVMT--------TEIlrNMLYRegadleDVGVVVMDEfhylADP--DRGWV--WEEP 157
                         170
                  ....*....|....*..
gi 1050399450 244 ISRLPETRQTLLFSATL 260
Cdd:COG4581   158 IIHLPARVQLVLLSATV 174
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
319-421 5.83e-07

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 49.56  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 319 QTVIFVATKHHAE----YLRELLDMQGIPCSHIYSS----LDQTARKINLGLFlHGKVRALLVTDVAARGIDIPMLDNVI 390
Cdd:cd18797    37 KTIVFCRSRKLAElllrYLKARLVEEGPLASKVASYragyLAEDRREIEAELF-NGELLGVVATNALELGIDIGGLDAVV 115
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1050399450 391 NYNFPPKAKLFLHRVGrvaRAGRSGTAYSFI 421
Cdd:cd18797   116 LAGYPGSLASLWQQAG---RAGRRGKDSLVI 143
PRK13766 PRK13766
Hef nuclease; Provisional
121-230 1.29e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 52.18  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 121 TGSGKTACFLIPMFEKLKAHsaqtGVRGLILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQfAALHENPDIII 200
Cdd:PRK13766   38 TGLGKTAIALLVIAERLHKK----GGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKR-AELWEKAKVIV 112
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1050399450 201 ATPgrlmHVaIEMNL-----KLRSVEYVVFDEADR 230
Cdd:PRK13766  113 ATP----QV-IENDLiagriSLEDVSLLIFDEAHR 142
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
113-228 2.64e-06

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: 48.80  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 113 KDVVAMARTGSGKT--ACFLIPMFEKLKAHSAQTGVRGLILSPTRELALQTlkfTKELGKFTGLKTALILGGDRMEDQ-- 188
Cdd:cd18034    17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQ---AEAIRSHTDLKVGEYSGEMGVDKWtk 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1050399450 189 --FAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEA 228
Cdd:cd18034    94 erWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
100-263 3.70e-06

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: 48.10  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 100 PIQRKVV-PVILDGKDVVAMARTGSGKTACFLIPMFeklkaHSAQTGVRGLILSPTRELALQTLKFTKELGKFtGLKTAL 178
Cdd:cd18028     4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMV-----NTLLEGGKALYLVPLRALASEKYEEFKKLEEI-GLKVGI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 179 ILGGDRMEDQFaaLHENpDIIIATPGR---LMHVAIEmnlKLRSVEYVVFDEADRLFEMGFAEQLQEIISRL----PETr 251
Cdd:cd18028    78 STGDYDEDDEW--LGDY-DIIVATYEKfdsLLRHSPS---WLRDVGVVVVDEIHLISDEERGPTLESIVARLrrlnPNT- 150
                         170
                  ....*....|..
gi 1050399450 252 QTLLFSATLPKM 263
Cdd:cd18028   151 QIIGLSATIGNP 162
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
275-392 3.98e-06

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 47.09  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 275 PVLIRLDVDTKLSdqlklsffnvrvedkpaVLLHLLRCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQT 354
Cdd:cd18793     2 PPKIEEVVSGKLE-----------------ALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSK 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1050399450 355 ARKINLGLFLHGK--VRALLVTDVAARGIDIPMLDNVINY 392
Cdd:cd18793    65 ERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILY 104
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
98-264 4.95e-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: 47.80  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  98 PTPIQRKVVPVIL-DGKDVVAMAR-----TGSGKTACFLIPMFEKLKAHSaqtgvRGLILSPTRELALQTLKFTKELgkF 171
Cdd:cd17918    16 LTKDQAQAIKDIEkDLHSPEPMDRllsgdVGSGKTLVALGAALLAYKNGK-----QVAILVPTEILAHQHYEEARKF--L 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 172 TGLKTALILGGDRMEDQfaalhENPDIIIATpgrlmHVAIEMNLKLRSVEYVVFDEADRlfemgFAEQLQEIISRLPETr 251
Cdd:cd17918    89 PFINVELVTGGTKAQIL-----SGISLLVGT-----HALLHLDVKFKNLDLVIVDEQHR-----FGVAQREALYNLGAT- 152
                         170
                  ....*....|....
gi 1050399450 252 QTLLFSAT-LPKML 264
Cdd:cd17918   153 HFLEATATpIPRTL 166
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
320-390 5.32e-06

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: 46.01  E-value: 5.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 320 TVIFVATKHHAEYLRELLDMQGIPCSHIYSslDQTARKINLG---LFLHG--KVRALLVTDVAARGIDIPMLDNVI 390
Cdd:cd18799     9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNS--DYSDRERGDEaliLLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
PRK00254 PRK00254
ski2-like helicase; Provisional
109-331 9.48e-06

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 49.43  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 109 ILDGKDVVAMARTGSGKTACFLIPMFEKLkahsAQTGVRGLILSPTRELALQTLKFTKELGKFtGLKTALILGGDRMEDQ 188
Cdd:PRK00254   36 VLEGKNLVLAIPTASGKTLVAEIVMVNKL----LREGGKAVYLVPLKALAEEKYREFKDWEKL-GLRVAMTTGDYDSTDE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 189 FAALHenpDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFSATL--PKMLLE 266
Cdd:PRK00254  111 WLGKY---DIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAE 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050399450 267 FARAGLT----EPVLIRLDVDTklsdQLKLSFFNVRVEDKPAVLLHLLRCVVKPQEQTVIFVATKHHAE 331
Cdd:PRK00254  188 WLNAELVvsdwRPVKLRKGVFY----QGFLFWEDGKIERFPNSWESLVYDAVKKGKGALVFVNTRRSAE 252
ResIII pfam04851
Type III restriction enzyme, res subunit;
115-259 1.04e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.51  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 115 VVAMArTGSGKTACFLIPMFEKLKAHSAQtgvRGLILSPTRELALQTLK-FTKELGKFTGLKTalILGGDRMEDQFaalh 193
Cdd:pfam04851  27 LIVMA-TGSGKTLTAAKLIARLFKKGPIK---KVLFLVPRKDLLEQALEeFKKFLPNYVEIGE--IISGDKKDESV---- 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1050399450 194 ENPDIIIATPGRLmHVAIEMNLKLRSVE---YVVFDEADRLfemgFAEQLQEIISRLPETRQtLLFSAT 259
Cdd:pfam04851  97 DDNKIVVTTIQSL-YKALELASLELLPDffdVIIIDEAHRS----GASSYRNILEYFKPAFL-LGLTAT 159
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
102-230 2.24e-05

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 45.97  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 102 QRKVVPVILDGKDVVAMArTGSGKTACFLIPMFEKLKahsaQTGVRGLILSPTRELALQTLKFTKELGKFTGLKTALIlg 181
Cdd:cd18035     7 QVLIAAVALNGNTLIVLP-TGLGKTIIAILVAADRLT----KKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT-- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1050399450 182 GDRMEDQFAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADR 230
Cdd:cd18035    80 GEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
306-411 3.45e-05

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 44.50  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 306 LLHLLRC--VVKPQEQTVIFVATKHHAEYLRELLDMQGIPCSHI---------------YSSLDQTARKINLGLFLHGKV 368
Cdd:cd18802    12 LIEILREyfPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIrcgfligrgnssqrkRSLMTQRKQKETLDKFRDGEL 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1050399450 369 RALLVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRvARA 411
Cdd:cd18802    92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
98-268 3.82e-05

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: 45.33  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  98 PTPIQRKVVPVILDGKDVVAMARTGSGKTAcflipMFEKLKAHSAQTGVRGLILSPTRELALQTLKFTKELGKFTGLKTa 177
Cdd:cd18027     9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTV-----VAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGLIT- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 178 lilgGDrmedqfAALHENPDIIIATPGRLMHVAIEMNLKLRSVEYVVFDEADRLFEMGFAEQLQEIISRLPETRQTLLFS 257
Cdd:cd18027    83 ----GD------VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLS 152
                         170
                  ....*....|.
gi 1050399450 258 ATLPKMlLEFA 268
Cdd:cd18027   153 ATVPNT-VEFA 162
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
320-419 1.41e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.02  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 320 TVIFVATKHHAE----YLRELLDMQG----IPCSHiySSLDQTARKINLGLFLHGKVRALLVTDVAARGIDIPMLDNVIN 391
Cdd:cd18796    41 TLVFTNTRSQAErlaqRLRELCPDRVppdfIALHH--GSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
                          90       100
                  ....*....|....*....|....*...
gi 1050399450 392 YNFPPKAKLFLHRVGrvaRAGRSGTAYS 419
Cdd:cd18796   119 IGSPKSVARLLQRLG---RSGHRPGAAS 143
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
374-412 1.62e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.77  E-value: 1.62e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1050399450 374 TDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARAG 412
Cdd:cd18785    29 TNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
112-227 1.94e-04

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


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 42.96  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 112 GKDVVAMARTGSGKTACFLIPMFEKLKAHSAQtGVRGLILSPTRELALQTLKFTKELGKFTGLK-TALILGGDRMEDQFA 190
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-GVQVLYISPLKALINDQERRLEEPLDEIDLEiPVAVRHGDTSQSEKA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1050399450 191 ALHEN-PDIIIATPGRL--MHVAIEMNLKLRSVEYVVFDE 227
Cdd:cd17922    80 KQLKNpPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
116-230 2.99e-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: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 116 VAMArTGSGKT--ACFLIPMFekLKAHSAQtgvRGLILSPTRELALQTLkftKELGKFTGLKTALILGGDRMEDQFAalh 193
Cdd:cd18032    25 LVMA-TGTGKTytAAFLIKRL--LEANRKK---RILFLAHREELLEQAE---RSFKEVLPDGSFGNLKGGKKKPDDA--- 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1050399450 194 enpDIIIATPGRLMHvaiEMNLKLRSVE---YVVFDEADR 230
Cdd:cd18032    93 ---RVVFATVQTLNK---RKRLEKFPPDyfdLIIIDEAHH 126
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
98-230 1.08e-03

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: 41.26  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  98 PTPIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFEKLKAHSAQTGVRGLILSPTRELALQTL-KFTKELGKfTGLKT 176
Cdd:cd17927     3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKeVFRKHFER-PGYKV 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1050399450 177 ALILGGDRMEDQFAALHENPDIIIATPGRLMHVAIEMNL-KLRSVEYVVFDEADR 230
Cdd:cd17927    82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
100-203 1.56e-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: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 100 PIQRKVVPVILDGKD-VVAMARTGSGKTAC--FLIpmfekLKAHSAQTGVRGLILSPTRELALQTL-----KFTKELGkf 171
Cdd:cd18021     6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCaeLAL-----LRHWRQNPKGRAVYIAPMQELVDARYkdwraKFGPLLG-- 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1050399450 172 tglKTALILGGDRMEDqfAALHENPDIIIATP 203
Cdd:cd18021    79 ---KKVVKLTGETSTD--LKLLAKSDVILATP 105
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
97-227 1.66e-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: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450  97 VPTPIQRKVVPVILDGKDVVAMARTGSGKT--ACFLIPMFEKLKAHSAQTGvRGLILSPTRELALQTL-KFTKELGKftG 173
Cdd:cd18036     2 ELRNYQLELVLPALRGKNTIICAPTGSGKTrvAVYICRHHLEKRRSAGEKG-RVVVLVNKVPLVEQQLeKFFKYFRK--G 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1050399450 174 LKTALILGGDRMEDQFAALHENPDIIIATP----GRLMHVAIEMNLKLRSVEYVVFDE 227
Cdd:cd18036    79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPqiliNNLLSGREEERVYLSDFSLLIFDE 136
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
287-421 4.82e-03

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 38.38  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 287 SDQLKLSFFNVRvedKPAVLLHLLRcVVKPQEQTVIFVATKHHAEYLRELLdmqGIPCshIYSSLDQTARKINLGLFLHG 366
Cdd:cd18789    23 RKRRLLAAMNPN---KLRALEELLK-RHEQGDKIIVFTDNVEALYRYAKRL---LKPF--ITGETPQSEREEILQNFREG 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1050399450 367 KVRALLVTDVAARGIDIPMLDNVINYNFPPKAKL-FLHRVGRVARAGRsGTAYSFI 421
Cdd:cd18789    94 EYNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRqEAQRLGRILRPKK-GGGKNAF 148
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
100-266 5.93e-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: 38.78  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 100 PIQRKVVPVILDGKDVVAMARTGSGKTACFLIPMFekLKAHsaQTGVRGLILSPTreLAL-----QTLKftkelgkfTGL 174
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRR--RGPGLTLVVSPL--IALmkdqvDALP--------RAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 175 KTALILGGDRMEDQFAALHE----NPDIIIATPGRLMHVA-IEMNLKLRSVEYVVFDEADRLFEMGFA-----EQLQEII 244
Cdd:cd18018    81 KAAALNSSLTREERRRILEKlragEVKILYVSPERLVNESfRELLRQTPPISLLVVDEAHCISEWSHNfrpdyLRLCRVL 160
                         170       180
                  ....*....|....*....|..
gi 1050399450 245 SRLPETRQTLLFSATLPKMLLE 266
Cdd:cd18018   161 RELLGAPPVLALTATATKRVVE 182
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
118-350 6.78e-03

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 40.06  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 118 MARTGSGKT-ACFLIpmfekLKAHSAQTGVRGLILS-PTRELALQTLkftKELGKFTGLKTALiLGGDRMEDQFAALHEN 195
Cdd:COG1203   153 TAPTGGGKTeAALLF-----ALRLAAKHGGRRIIYAlPFTSIINQTY---DRLRDLFGEDVLL-HHSLADLDLLEEEEEY 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 196 P---------------DIIIATPGRLMHVAIE----MNLKL----RSVeyVVFDEADrLFEMGFAEQLQEIISRLPETRQ 252
Cdd:COG1203   224 EsearwlkllkelwdaPVVVTTIDQLFESLFSnrkgQERRLhnlaNSV--IILDEVQ-AYPPYMLALLLRLLEWLKNLGG 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 253 TLLF-SATLPKmlleFARAGLTEPVLIRLDVDTKLSDQL-KLSFFNVRVEDKP---AVLLHLLRCVVKPQEQTVIFVATK 327
Cdd:COG1203   301 SVILmTATLPP----LLREELLEAYELIPDEPEELPEYFrAFVRKRVELKEGPlsdEELAELILEALHKGKSVLVIVNTV 376
                         250       260
                  ....*....|....*....|....*..
gi 1050399450 328 HHA----EYLRELLDMQGIpcsHIYSS 350
Cdd:COG1203   377 KDAqelyEALKEKLPDEEV---YLLHS 400
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
294-415 7.12e-03

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: 37.57  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 294 FFNVRVEDKPAVLLHLLRCVVK--PQEQTVIFVATKHHAEYLRELLDMQGIPCSHIYSSLDQTARKINLGLFLHGKVRAL 371
Cdd:cd18794     5 FYSVRPKDKKDEKLDLLKRIKVehLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1050399450 372 LVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGrvaRAGRSG 415
Cdd:cd18794    85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDG 125
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
100-132 7.80e-03

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: 38.50  E-value: 7.80e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1050399450 100 PIQRKVVPVILDGKDVVAMARTGSGKTACFLIP 132
Cdd:cd18015    21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLP 53
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
302-428 8.53e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 39.71  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 302 KPAVLLHLL--RCVVKPQEQTVIFVATKHHAEYLRELLDMQGIPC------SHIYSS--LDQTARKINLGLFLHGKVRAL 371
Cdd:COG1111   336 KLSKLREILkeQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVL 415
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050399450 372 LVTDVAARGIDIPMLDNVINYNFPPKAKLFLHRVGRVARaGRSGTAYSFIAP---DEIPY 428
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAKgtrDEAYY 474
 
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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