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Conserved domains on  [gi|124512888|ref|XP_001349800|]
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ATP-dependent RNA helicase DBP6, putative [Plasmodium falciparum 3D7]

Protein Classification

DEAD/DEAH box helicase domain-containing protein( domain architecture ID 1000559)

DEAD/DEAH box helicase domain-containing protein may function as an RNA helicase

EC:  3.6.4.-
Gene Ontology:  GO:0005524|GO:0004386|GO:0003676
PubMed:  20206133

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB super family cl33924
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
156-524 4.95e-64

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


The actual alignment was detected with superfamily member COG0513:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 216.94  E-value: 4.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEIfQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHTLIIVPTRELA 235
Cdd:COG0513    9 LSPPLLKALAEL-GYTTPTPIQAQAIPLILAGR---DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 236 NQIYNECKLLLTYkHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFEStylfNTL-FENLKMLIIDEADQLL 314
Cdd:COG0513   85 LQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKR-GVDIVVATPGRLLDLIER----GALdLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 315 STGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKmcksdyiYLNCVKDIS----KHTSDQLIQYVLF----HKaid 386
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKR-------YLKNPVRIEvapeNATAETIEQRYYLvdkrDK--- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 387 ttiilYNLLIEHMRLNQFtYKIIVFFPTARATSFYAQFFINQlKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDIS 466
Cdd:COG0513  229 -----LELLRRLLRDEDP-ERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 467 SRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIKDL 524
Cdd:COG0513  302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL 359
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
156-524 4.95e-64

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 216.94  E-value: 4.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEIfQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHTLIIVPTRELA 235
Cdd:COG0513    9 LSPPLLKALAEL-GYTTPTPIQAQAIPLILAGR---DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 236 NQIYNECKLLLTYkHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFEStylfNTL-FENLKMLIIDEADQLL 314
Cdd:COG0513   85 LQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKR-GVDIVVATPGRLLDLIER----GALdLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 315 STGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKmcksdyiYLNCVKDIS----KHTSDQLIQYVLF----HKaid 386
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKR-------YLKNPVRIEvapeNATAETIEQRYYLvdkrDK--- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 387 ttiilYNLLIEHMRLNQFtYKIIVFFPTARATSFYAQFFINQlKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDIS 466
Cdd:COG0513  229 -----LELLRRLLRDEDP-ERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 467 SRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIKDL 524
Cdd:COG0513  302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL 359
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
156-362 1.81e-52

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: 179.32  E-value: 1.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEiFQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILS----VHTLIIVPT 231
Cdd:cd17964    1 LDPSLLKALTR-MGFETMTPVQQKTLKPILSTGD--DVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgVSALIISPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 232 RELANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFNTlFENLKMLIIDEAD 311
Cdd:cd17964   78 RELALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKA-FTDLDYLVLDEAD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124512888 312 QLLSTGYENDIHRLLTYLP----SNRRNILLSATLGYNLDEIRKKMCKSDYIYLN 362
Cdd:cd17964  157 RLLDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
174-349 1.59e-42

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: 150.86  E-value: 1.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  174 TDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLlSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLtYKHNIN 253
Cdd:pfam00270   1 TPIQAEAIPAILEGR---DVLVQAPTGSGKTLAFLL-PALEALDKLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  254 VLTLTGGIKRRDDQLNIRriKPDIIICTVGRLLDHFESTylfnTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNR 333
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQER----KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKR 149
                         170
                  ....*....|....*.
gi 124512888  334 RNILLSATLGYNLDEI 349
Cdd:pfam00270 150 QILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
165-355 5.73e-37

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 136.85  E-value: 5.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888   165 LEIFQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVhtLIIVPTRELANQIYNECKL 244
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888   245 LLTYKhNINVLTLTGGIKRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHR 324
Cdd:smart00487  77 LGPSL-GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLS---LSNVDLVILDEAHRLLDGGFGDQLEK 152
                          170       180       190
                   ....*....|....*....|....*....|.
gi 124512888   325 LLTYLPSNRRNILLSATLGYNLDEIRKKMCK 355
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFLN 183
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
170-530 1.53e-36

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 142.63  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 170 YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAY---LLLSINdiikNKILSVHTLIIVPTRELANQIYNECKLLL 246
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGK---DVIAQAKTGSGKTAAFglgLLQKLD----VKRFRVQALVLCPTRELADQVAKEIRRLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 247 TYKHNINVLTLTGGIKRRdDQLNIRRIKPDIIICTVGRLLDHFESTYLfnTLfENLKMLIIDEADQLLSTGYENDIHRLL 326
Cdd:PRK11776  97 RFIPNIKVLTLCGGVPMG-PQIDSLEHGAHIIVGTPGRILDHLRKGTL--DL-DALNTLVLDEADRMLDMGFQDAIDAII 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 327 TYLPSNRRNILLSATLGynlDEIRKkmcKSDYIYLN--CVKDISKHTSDQLIQYvlFHKAIDT--TIILYNLLIEHMRLN 402
Cdd:PRK11776 173 RQAPARRQTLLFSATYP---EGIAA---ISQRFQRDpvEVKVESTHDLPAIEQR--FYEVSPDerLPALQRLLLHHQPES 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 403 qftykIIVFFPTARATSFYAQFFINQlKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVN 482
Cdd:PRK11776 245 -----CVVFCNTKKECQEVADALNAQ-GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 124512888 483 TPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIKDLNIQKLN 530
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
156-524 4.95e-64

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 216.94  E-value: 4.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEIfQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHTLIIVPTRELA 235
Cdd:COG0513    9 LSPPLLKALAEL-GYTTPTPIQAQAIPLILAGR---DVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 236 NQIYNECKLLLTYkHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFEStylfNTL-FENLKMLIIDEADQLL 314
Cdd:COG0513   85 LQVAEELRKLAKY-LGLRVATVYGGVSIGRQIRALKR-GVDIVVATPGRLLDLIER----GALdLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 315 STGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKmcksdyiYLNCVKDIS----KHTSDQLIQYVLF----HKaid 386
Cdd:COG0513  159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKR-------YLKNPVRIEvapeNATAETIEQRYYLvdkrDK--- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 387 ttiilYNLLIEHMRLNQFtYKIIVFFPTARATSFYAQFFINQlKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDIS 466
Cdd:COG0513  229 -----LELLRRLLRDEDP-ERAIVFCNTKRGADRLAEKLQKR-GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 467 SRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIKDL 524
Cdd:COG0513  302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKL 359
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
156-362 1.81e-52

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: 179.32  E-value: 1.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEiFQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILS----VHTLIIVPT 231
Cdd:cd17964    1 LDPSLLKALTR-MGFETMTPVQQKTLKPILSTGD--DVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgVSALIISPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 232 RELANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFNTlFENLKMLIIDEAD 311
Cdd:cd17964   78 RELALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENPGVAKA-FTDLDYLVLDEAD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124512888 312 QLLSTGYENDIHRLLTYLP----SNRRNILLSATLGYNLDEIRKKMCKSDYIYLN 362
Cdd:cd17964  157 RLLDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
170-355 9.73e-52

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: 176.86  E-value: 9.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 170 YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHT---LIIVPTRELANQIYNECKLLL 246
Cdd:cd00268   10 FEKPTPIQAQAIPLILSGR---DVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGpqaLVLAPTRELAMQIAEVARKLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 247 TYKhNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHRLL 326
Cdd:cd00268   87 KGT-GLKVAAIYGGAPIKKQIEALKK-GPDIVVGTPGRLLDLIERGKLD---LSNVKYLVLDEADRMLDMGFEEDVEKIL 161
                        170       180
                 ....*....|....*....|....*....
gi 124512888 327 TYLPSNRRNILLSATLGYNLDEIRKKMCK 355
Cdd:cd00268  162 SALPKDRQTLLFSATLPEEVKELAKKFLK 190
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
174-349 1.59e-42

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: 150.86  E-value: 1.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  174 TDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLlSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLtYKHNIN 253
Cdd:pfam00270   1 TPIQAEAIPAILEGR---DVLVQAPTGSGKTLAFLL-PALEALDKLDNGPQALVLAPTRELAEQIYEELKKLG-KGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  254 VLTLTGGIKRRDDQLNIRriKPDIIICTVGRLLDHFESTylfnTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNR 333
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK--GPDILVGTPGRLLDLLQER----KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKR 149
                         170
                  ....*....|....*.
gi 124512888  334 RNILLSATLGYNLDEI 349
Cdd:pfam00270 150 QILLLSATLPRNLEDL 165
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
162-351 2.13e-38

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: 140.79  E-value: 2.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 162 KSLLEIFQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYL--LLSI--NDIIKNKILSVHTLIIVPTRELANQ 237
Cdd:cd17960    2 LDVVAELGFTSMTPVQAATIPLFLSNK---DVVVEAVTGSGKTLAFLipVLEIllKRKANLKKGQVGALIISPTRELATQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 238 IYNECKLLLTYKHN-INVLTLTGGIKRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFNTlFENLKMLIIDEADQLLST 316
Cdd:cd17960   79 IYEVLQSFLEHHLPkLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVK-VKSLEVLVLDEADRLLDL 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 124512888 317 GYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRK 351
Cdd:cd17960  158 GFEADLNRILSKLPKQRRTGLFSATQTDAVEELIK 192
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
192-356 1.28e-37

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: 138.49  E-value: 1.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHT-----LIIVPTRELANQIYNECKLLLTY--KHnINVLTLTGGIKRr 264
Cdd:cd17961   33 DILARARTGSGKTAAYALPIIQKILKAKAESGEEqgtraLILVPTRELAQQVSKVLEQLTAYcrKD-VRVVNLSASSSD- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 265 DDQLNIRRIKPDIIICTVGRLLDHFESTYLFNTlfENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGY 344
Cdd:cd17961  111 SVQRALLAEKPDIVVSTPARLLSHLESGSLLLL--STLKYLVIDEADLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSE 188
                        170
                 ....*....|..
gi 124512888 345 NLDEIRKKMCKS 356
Cdd:cd17961  189 DVEALKKLVLHN 200
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
160-342 1.32e-37

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: 138.87  E-value: 1.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 160 VKKSLLEIFQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKIL---SVHT--LIIVPTREL 234
Cdd:cd17949    1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGR---DVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrSDGTlaLVLVPTREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 235 ANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIRRIKPdIIICTVGRLLDHFESTYLFNtlFENLKMLIIDEADQLL 314
Cdd:cd17949   78 ALQIYEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVN-ILIATPGRLLDHLKNTQSFD--VSNLRWLVLDEADRLL 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124512888 315 STGYENDIHRLLTYL-------------PSNRRNILLSATL 342
Cdd:cd17949  155 DMGFEKDITKILELLddkrskaggekskPSRRQTVLVSATL 195
DEXDc smart00487
DEAD-like helicases superfamily;
165-355 5.73e-37

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 136.85  E-value: 5.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888   165 LEIFQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVhtLIIVPTRELANQIYNECKL 244
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPALEALKRGKGGRV--LVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888   245 LLTYKhNINVLTLTGGIKRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHR 324
Cdd:smart00487  77 LGPSL-GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLS---LSNVDLVILDEAHRLLDGGFGDQLEK 152
                          170       180       190
                   ....*....|....*....|....*....|.
gi 124512888   325 LLTYLPSNRRNILLSATLGYNLDEIRKKMCK 355
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFLN 183
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
170-530 1.53e-36

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 142.63  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 170 YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAY---LLLSINdiikNKILSVHTLIIVPTRELANQIYNECKLLL 246
Cdd:PRK11776  24 YTEMTPIQAQSLPAILAGK---DVIAQAKTGSGKTAAFglgLLQKLD----VKRFRVQALVLCPTRELADQVAKEIRRLA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 247 TYKHNINVLTLTGGIKRRdDQLNIRRIKPDIIICTVGRLLDHFESTYLfnTLfENLKMLIIDEADQLLSTGYENDIHRLL 326
Cdd:PRK11776  97 RFIPNIKVLTLCGGVPMG-PQIDSLEHGAHIIVGTPGRILDHLRKGTL--DL-DALNTLVLDEADRMLDMGFQDAIDAII 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 327 TYLPSNRRNILLSATLGynlDEIRKkmcKSDYIYLN--CVKDISKHTSDQLIQYvlFHKAIDT--TIILYNLLIEHMRLN 402
Cdd:PRK11776 173 RQAPARRQTLLFSATYP---EGIAA---ISQRFQRDpvEVKVESTHDLPAIEQR--FYEVSPDerLPALQRLLLHHQPES 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 403 qftykIIVFFPTARATSFYAQFFINQlKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVN 482
Cdd:PRK11776 245 -----CVVFCNTKKECQEVADALNAQ-GFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 124512888 483 TPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIKDLNIQKLN 530
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
161-363 1.05e-34

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: 130.10  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 161 KKSLLEIfQYKEFTDVQRivyDNIIKEKKQNDLLIQAKTGTGKTIAYLLLSINDIIKNK---ILSVHTLIIVPTRELANQ 237
Cdd:cd17941    2 LKGLKEA-GFIKMTEIQR---DSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwtpEDGLGALIISPTRELAMQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 238 IYNECKLLLTYkHNINVLTLTGGIKRRDDQLNIRRIkpDIIICTVGRLLDHFESTYLFNTlfENLKMLIIDEADQLLSTG 317
Cdd:cd17941   78 IFEVLRKVGKY-HSFSAGLIIGGKDVKEEKERINRM--NILVCTPGRLLQHMDETPGFDT--SNLQMLVLDEADRILDMG 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124512888 318 YENDIHRLLTYLPSNRRNILLSATLGYNLDEIrKKMCKSDYIYLNC 363
Cdd:cd17941  153 FKETLDAIVENLPKSRQTLLFSATQTKSVKDL-ARLSLKNPEYISV 197
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
161-362 1.77e-34

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: 129.79  E-value: 1.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 161 KKSLLEiFQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKIL---SVHTLIIVPTRELANQ 237
Cdd:cd17942    2 LKAIEE-MGFTKMTEIQAKSIPPLLEGR---DVLGAAKTGSGKTLAFLIPAIELLYKLKFKprnGTGVIIISPTRELALQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 238 IYNECKLLLTYkHNINVLTLTGGIKRRDDqlnIRRIKP--DIIICTVGRLLDHFESTYLFntLFENLKMLIIDEADQLLS 315
Cdd:cd17942   78 IYGVAKELLKY-HSQTFGIVIGGANRKAE---AEKLGKgvNILVATPGRLLDHLQNTKGF--LYKNLQCLIIDEADRILE 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 124512888 316 TGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKMCKSDYIYLN 362
Cdd:cd17942  152 IGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKKPLYVG 198
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
157-522 1.23e-33

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 133.53  E-value: 1.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 157 DKDVKKSLLEIFQYKEFTDVQRIVYDNIIKEKKQNDLLIQAKTGTGKTIAYLLLSIN---DIIKNKILSVHTLIIVPTRE 233
Cdd:PRK11192   5 ELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhllDFPRRKSGPPRILILTPTRE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 234 LANQIYNECKLLLTYKHnINVLTLTGGIKrRDDQLNIRRIKPDIIICTVGRLLDHFESTyLFNTlfENLKMLIIDEADQL 313
Cdd:PRK11192  85 LAMQVADQARELAKHTH-LDIATITGGVA-YMNHAEVFSENQDIVVATPGRLLQYIKEE-NFDC--RAVETLILDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 314 LSTGYENDIHRLLTYLPSNRRNILLSATL-GYNLDEIRKKMCKsDYIYLNCvkDISKHTSDQLIQYVlfHKAID---TTI 389
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLN-DPVEVEA--EPSRRERKKIHQWY--YRADDlehKTA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 390 ILYNLLiehmRLNQFTyKIIVFFPT-ARATSFYAQFFINQLKISVYEihrkKEMAH--RQITANRFSMESVGILFTSDIS 466
Cdd:PRK11192 235 LLCHLL----KQPEVT-RSIVFVRTrERVHELAGWLRKAGINCCYLE----GEMVQakRNEAIKRLTDGRVNVLVATDVA 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124512888 467 SRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMAIILLNEADELFYQEIK 522
Cdd:PRK11192 306 ARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
191-541 8.03e-33

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 133.82  E-value: 8.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 191 NDLLIQAKTGTGKTIAYLLLSINDIiKNKILSVHTLIIVPTRELANQIYNECKLLLTYKHNINVLTLTGGiKRRDDQLNI 270
Cdd:PRK11634  44 RDVLGMAQTGSGKTAAFSLPLLHNL-DPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGG-QRYDVQLRA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 271 RRIKPDIIICTVGRLLDHFEStylfNTL-FENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEI 349
Cdd:PRK11634 122 LRQGPQIVVGTPGRLLDHLKR----GTLdLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRI 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 350 RKKMCKSD-----YIYLNCVKDISKhtSDQLIQYVLFHKAidttiilynlLIEHMRLNQFTYKIIvFFPTARATSFYAQf 424
Cdd:PRK11634 198 TRRFMKEPqevriQSSVTTRPDISQ--SYWTVWGMRKNEA----------LVRFLEAEDFDAAII-FVRTKNATLEVAE- 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 425 finQLKISVYE---IHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRTARSN 501
Cdd:PRK11634 264 ---ALERNGYNsaaLNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAG 340
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 124512888 502 KKGMAIILLNEADELFYQEIKdlNIQKLNAQNYTLKNTNL 541
Cdd:PRK11634 341 RAGRALLFVENRERRLLRNIE--RTMKLTIPEVELPNAEL 378
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
165-349 1.55e-32

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: 125.44  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 165 LEIFQYKEFTDVQRIVYDNIIKEKKQN------DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHTLIIVPTRELANQI 238
Cdd:cd17956    5 LQNNGITSAFPVQAAVIPWLLPSSKSTppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKELVQQV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 239 YNECKlLLTYKHNINVLTLTGGIKRRDDQLNIRRI-------KPDIIICTVGRLLDHFESTYLFNtlFENLKMLIIDEAD 311
Cdd:cd17956   85 YKVFE-SLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsRVDILVATPGRLVDHLNSTPGFT--LKHLRFLVIDEAD 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 312 QLLSTGYENDIHRLLTYL--------------------PSNRRNILLSATLGYNLDEI 349
Cdd:cd17956  162 RLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATLTRDPEKL 219
PTZ00110 PTZ00110
helicase; Provisional
192-510 1.68e-31

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 129.12  E-value: 1.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVH----TLIIVPTRELANQIYNECkLLLTYKHNINVLTLTGGIKRRDDQ 267
Cdd:PTZ00110 169 DMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpiVLVLAPTRELAEQIREQC-NKFGASSKIRNTVAYGGVPKRGQI 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 268 LNIRRiKPDIIICTVGRLLDHFESTYlfnTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLD 347
Cdd:PTZ00110 248 YALRR-GVEILIACPGRLIDFLESNV---TNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQ 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 348 EIRKKMCKSDYIYLNcVKDISKHTSDQLIQYVLFHKAIDTTIILYNLLIEHMRLNQftyKIIVFFPTARAtsfyAQFFIN 427
Cdd:PTZ00110 324 SLARDLCKEEPVHVN-VGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGD---KILIFVETKKG----ADFLTK 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 428 QLKISVYE---IHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKG 504
Cdd:PTZ00110 396 ELRLDGWPalcIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKG 475

                 ....*.
gi 124512888 505 MAIILL 510
Cdd:PTZ00110 476 ASYTFL 481
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
375-510 6.24e-31

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: 117.22  E-value: 6.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 375 LIQYVLFHKAIDTTIILYNLLIEHmrlnQFTYKIIVFFPTARATSFYAQFFiNQLKISVYEIHRKKEMAHRQITANRFSM 454
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEK----LKPGKAIIFVNTKKRVDRLAELL-EELGIKVAALHGDLSQEERERALKKFRS 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124512888 455 ESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMAIILL 510
Cdd:cd18787   76 GKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
189-532 4.25e-30

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 123.87  E-value: 4.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 189 KQNDLLIQAKTGTGKTIAYLLLSINDIIKNKILS------VHTLIIVPTRELANQIYNECKLLLTYKhNINVLTLTGGI- 261
Cdd:PRK01297 123 AGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKerymgePRALIIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMd 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 262 -KRRDDQLNIRRIkpDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHRLLTYLP--SNRRNILL 338
Cdd:PRK01297 202 fDKQLKQLEARFC--DILVATPGRLLDFNQRGEVH---LDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLF 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 339 SATLGYNLDEIRKKMCKSDYIylncVKDISKH-TSDQLIQYVLFHKAIDTTIILYNLliehmrLNQFTYKIIVFFPTARA 417
Cdd:PRK01297 277 SATFTDDVMNLAKQWTTDPAI----VEIEPENvASDTVEQHVYAVAGSDKYKLLYNL------VTQNPWERVMVFANRKD 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 418 TSFYAQFFINQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRT 497
Cdd:PRK01297 347 EVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRT 426
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 124512888 498 ARSNKKGMAIILLNEADELFYQEIKDLNIQKLNAQ 532
Cdd:PRK01297 427 GRAGASGVSISFAGEDDAFQLPEIEELLGRKISCE 461
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
197-342 2.15e-29

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: 115.49  E-value: 2.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 197 AKTGTGKTIAYLLLSINDIIKNKIlSVHTLIIVPTRELANQIYNECKLLLTyKHNINVLTLTGGIKRRDDQLNIRRiKPD 276
Cdd:cd17954   44 AETGSGKTAAFALPILQALLENPQ-RFFALVLAPTRELAQQISEQFEALGS-SIGLKSAVLVGGMDMMAQAIALAK-KPH 120
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124512888 277 IIICTVGRLLDHFESTYLFNtlFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATL 342
Cdd:cd17954  121 VIVATPGRLVDHLENTKGFS--LKSLKFLVMDEADRLLNMDFEPEIDKILKVIPRERTTYLFSATM 184
PTZ00424 PTZ00424
helicase 45; Provisional
192-522 4.81e-29

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 119.55  E-value: 4.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINdIIKNKILSVHTLIIVPTRELANQIYNECKLLLTYKhNINVLTLTGGIKRRDDqlnIR 271
Cdd:PTZ00424  67 DTIGQAQSGTGKTATFVIAALQ-LIDYDLNACQALILAPTRELAQQIQKVVLALGDYL-KVRCHACVGGTVVRDD---IN 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 272 RIKPDI--IICTVGRLLDHFESTYLfntLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEI 349
Cdd:PTZ00424 142 KLKAGVhmVVGTPGRVYDMIDKRHL---RVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILEL 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 350 RKKMCKSDYIYLNCVKDISKHTSDQLiqYVLFHK---AIDTTIILYnlliEHMRLNQftykIIVFFPTARATSFYAQFFI 426
Cdd:PTZ00424 219 TTKFMRDPKRILVKKDELTLEGIRQF--YVAVEKeewKFDTLCDLY----ETLTITQ----AIIYCNTRRKVDYLTKKMH 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 427 NQLkISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRTARSNKKGMA 506
Cdd:PTZ00424 289 ERD-FTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVA 367
                        330
                 ....*....|....*.
gi 124512888 507 IILLNEADELFYQEIK 522
Cdd:PTZ00424 368 INFVTPDDIEQLKEIE 383
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
196-507 8.46e-29

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 119.31  E-value: 8.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 196 QAKTGTGKTIAYL------LLSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLtyKHNINVLTLTGGIKRRDDQLN 269
Cdd:PRK04837  51 QAQTGTGKTMAFLtatfhyLLSHPAPEDRKVNQPRALIMAPTRELAVQIHADAEPLA--QATGLKLGLAYGGDGYDKQLK 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 270 IRRIKPDIIICTVGRLLDHFESTYlFNtlFENLKMLIIDEADQLLSTGYENDIHRLLTYLP--SNRRNILLSATLGYNLD 347
Cdd:PRK04837 129 VLESGVDILIGTTGRLIDYAKQNH-IN--LGAIQVVVLDEADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 348 EIR-KKMCKSDYIYlncVKDISKhTSdQLIQYVLFHKAIDTTIILYNLLIEHmrlnQFTYKIIVFFPTaratsfyaqffi 426
Cdd:PRK04837 206 ELAfEHMNNPEYVE---VEPEQK-TG-HRIKEELFYPSNEEKMRLLQTLIEE----EWPDRAIIFANT------------ 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 427 nqlKISVYEI--------HR----------KKemahRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISRE 488
Cdd:PRK04837 265 ---KHRCEEIwghlaadgHRvglltgdvaqKK----RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCE 337
                        330
                 ....*....|....*....
gi 124512888 489 QYIHRVGRTARSNKKGMAI 507
Cdd:PRK04837 338 DYVHRIGRTGRAGASGHSI 356
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
192-351 1.45e-28

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: 112.73  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDII--KNKILSVHTLIIVPTRELANQIYNECKLLLTYKHnINVLTLTGGIKRRDdQLN 269
Cdd:cd17947   29 DICASAVTGSGKTAAFLLPILERLLyrPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFTD-ITFALAVGGLSLKA-QEA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 270 IRRIKPDIIICTVGRLLDHFESTYLFNtlFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEI 349
Cdd:cd17947  107 ALRARPDIVIATPGRLIDHLRNSPSFD--LDSIEILVLDEADRMLEEGFADELKEILRLCPRTRQTMLFSATMTDEVKDL 184

                 ..
gi 124512888 350 RK 351
Cdd:cd17947  185 AK 186
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
170-510 3.60e-28

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 117.99  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 170 YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILS-----VHTLIIVPTRELANQIYNECKL 244
Cdd:PRK10590  21 YREPTPIQQQAIPAVLEGR---DLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrpVRALILTPTRELAAQIGENVRD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 245 LLTYKhNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLD--HFESTYLfntlfENLKMLIIDEADQLLSTGYENDI 322
Cdd:PRK10590  98 YSKYL-NIRSLVVFGGVSINPQMMKLRG-GVDVLVATPGRLLDleHQNAVKL-----DQVEILVLDEADRMLDMGFIHDI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 323 HRLLTYLPSNRRNILLSATLGynlDEIRKKMCKSDYIYLNcVKDISKHT-SDQLIQYVLFhkaIDTTII--LYNLLIEHM 399
Cdd:PRK10590 171 RRVLAKLPAKRQNLLFSATFS---DDIKALAEKLLHNPLE-IEVARRNTaSEQVTQHVHF---VDKKRKreLLSQMIGKG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 400 RLNQftykIIVFFPTARATSFYAQFfINQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLII 479
Cdd:PRK10590 244 NWQQ----VLVFTRTKHGANHLAEQ-LNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
                        330       340       350
                 ....*....|....*....|....*....|.
gi 124512888 480 QVNTPISREQYIHRVGRTARSNKKGMAIILL 510
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
192-507 1.03e-27

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 117.74  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILS------VHTLIIVPTRELANQIYNECkllLTYKHNINV-LTLTGGIKRR 264
Cdd:PRK04537  48 DVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrkpedPRALILAPTRELAIQIHKDA---VKFGADLGLrFALVYGGVDY 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 265 DDQLNIRRIKPDIIICTVGRLLDHFESTYLFNtlFENLKMLIIDEADQLLSTGYENDIHRLLTYLP--SNRRNILLSATL 342
Cdd:PRK04537 125 DKQRELLQQGVDVIIATPGRLIDYVKQHKVVS--LHACEICVLDEADRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATL 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 343 GYNLDEIRkkmcksdYIYLN----CVKDISKHTSDQLIQYVLFHKAIDTTIILYNLL--IEHMRLNQFTYKIIVFFPTAR 416
Cdd:PRK04537 203 SHRVLELA-------YEHMNepekLVVETETITAARVRQRIYFPADEEKQTLLLGLLsrSEGARTMVFVNTKAFVERVAR 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 417 ATSfyaqffINQLKISVY--EIHRKKemahRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRV 494
Cdd:PRK04537 276 TLE------RHGYRVGVLsgDVPQKK----RESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRI 345
                        330
                 ....*....|...
gi 124512888 495 GRTARSNKKGMAI 507
Cdd:PRK04537 346 GRTARLGEEGDAI 358
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
192-352 1.40e-27

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: 110.11  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAY--LLLSINDIIKNKIlsvHTLIIVPTRELANQIYNECKLLLTYKhNINVLTLTGGIKRRDDQlN 269
Cdd:cd17939   36 DVIAQAQSGTGKTATFsiGALQRIDTTVRET---QALVLAPTRELAQQIQKVVKALGDYM-GVKVHACIGGTSVREDR-R 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 270 IRRIKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEI 349
Cdd:cd17939  111 KLQYGPHIVVGTPGRVFDMLQRRSLR---TDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEV 187

                 ...
gi 124512888 350 RKK 352
Cdd:cd17939  188 TKK 190
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
184-361 2.42e-27

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: 110.27  E-value: 2.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 184 IIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHT---------LIIVPTRELANQIYNECKlLLTYKHNINV 254
Cdd:cd17967   33 IILAGR--DLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRgrrkaypsaLILAPTRELAIQIYEEAR-KFSYRSGVRS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 255 LTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHRLLTY--LPS- 331
Cdd:cd17967  110 VVVYGGADVVHQQLQLLR-GCDILVATPGRLVDFIERGRIS---LSSIKFLVLDEADRMLDMGFEPQIRKIVEHpdMPPk 185
                        170       180       190
                 ....*....|....*....|....*....|....
gi 124512888 332 -NRRNILLSATLGynlDEIrKKMCKS---DYIYL 361
Cdd:cd17967  186 gERQTLMFSATFP---REI-QRLAADflkNYIFL 215
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
146-348 5.49e-26

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: 105.77  E-value: 5.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 146 NKLLIESCchidkdvkKSLleifQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLlSINDIIKNKILSVHT 225
Cdd:cd17955    7 SSWLVKQC--------ASL----GIKEPTPIQKLCIPEILAGR---DVIGGAKTGSGKTAAFAL-PILQRLSEDPYGIFA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 226 LIIVPTRELANQIyNECKLLLTYKHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTYLFNTLFENLKML 305
Cdd:cd17955   71 LVLTPTRELAYQI-AEQFRALGAPLGLRCCVIVGGMDMVKQALELSK-RPHIVVATPGRLADHLRSSDDTTKVLSRVKFL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 124512888 306 IIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDE 348
Cdd:cd17955  149 VLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKA 191
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
169-361 5.62e-26

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: 107.36  E-value: 5.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 169 QYKEFTDVQRivYD-NIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKIL--------SVHTLIIVPTRELANQIY 239
Cdd:cd18052   62 GYEKPTPVQK--YAiPIILAGR--DLMACAQTGSGKTAAFLLPVLTGMMKEGLTassfsevqEPQALIVAPTRELANQIF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 240 NECKlLLTYKHNINVLTLTGGIKRrddQLNIRRIKP--DIIICTVGRLLDHFESTYLFntlFENLKMLIIDEADQLLSTG 317
Cdd:cd18052  138 LEAR-KFSYGTCIRPVVVYGGVSV---GHQIRQIEKgcHILVATPGRLLDFIGRGKIS---LSKLKYLILDEADRMLDMG 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124512888 318 YENDIHRLLTYL--PS--NRRNILLSATLGynlDEIRK---KMCKSDYIYL 361
Cdd:cd18052  211 FGPEIRKLVSEPgmPSkeDRQTLMFSATFP---EEIQRlaaEFLKEDYLFL 258
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
170-342 9.25e-26

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: 105.08  E-value: 9.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 170 YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDI-IKNKILSVHTLIIVPTRELANQIYNECKLLLTY 248
Cdd:cd17959   21 YKVPTPIQRKTIPLILDGR---DVVAMARTGSGKTAAFLIPMIEKLkAHSPTVGARALILSPTRELALQTLKVTKELGKF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 249 KhNINVLTLTGGiKRRDDQLNIRRIKPDIIICTVGRLLDHFESTylfNTLFENLKMLIIDEADQLLSTGYENDIHRLLTY 328
Cdd:cd17959   98 T-DLRTALLVGG-DSLEEQFEALASNPDIIIATPGRLLHLLVEM---NLKLSSVEYVVFDEADRLFEMGFAEQLHEILSR 172
                        170
                 ....*....|....
gi 124512888 329 LPSNRRNILLSATL 342
Cdd:cd17959  173 LPENRQTLLFSATL 186
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
192-353 4.60e-25

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: 102.73  E-value: 4.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSInDIIKNKILSVHTLIIVPTRELANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIR 271
Cdd:cd17943   29 DLIVQAKSGTGKTLVFVVIAL-ESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 272 RikPDIIICTVGRLLDHFESTYLfNTlfENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRK 351
Cdd:cd17943  108 G--CHIAVGTPGRIKQLIELGAL-NV--SHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLA 182

                 ..
gi 124512888 352 KM 353
Cdd:cd17943  183 RY 184
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
192-352 5.32e-25

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: 102.76  E-value: 5.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIiKNKILSVHTLIIVPTRELANQIYNECKLLltYKH-NINVLTLTGGIKRRDDQLNI 270
Cdd:cd17940   38 DILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELALQTSQVCKEL--GKHmGVKVMVTTGGTSLRDDIMRL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 271 RRiKPDIIICTVGRLLDHFESTYlfnTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIR 350
Cdd:cd17940  115 YQ-TVHVLVGTPGRILDLAKKGV---ADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFM 190

                 ..
gi 124512888 351 KK 352
Cdd:cd17940  191 DR 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
160-380 9.86e-25

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: 103.09  E-value: 9.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 160 VKKSLLEIfQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDII----KNKILSVHT----LIIVPT 231
Cdd:cd17946    1 ILRALADL-GFSEPTPIQALALPAAIRDGK--DVIGAAETGSGKTLAFGIPILERLLsqksSNGVGGKQKplraLILTPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 232 RELANQIYNECKLLLTYKhNINVLTLTGG--IKRRDDQLNIRrikPDIIICTVGRLLDHFESTYLFNTLFENLKMLIIDE 309
Cdd:cd17946   78 RELAVQVKDHLKAIAKYT-NIKIASIVGGlaVQKQERLLKKR---PEIVVATPGRLWELIQEGNEHLANLKSLRFLVLDE 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 310 ADQLLSTGYENDIHRLLTYLPSN-------RRNILLSATLGYNLDEIRKKMCKsdyiylncvKDISKHTSDQLIQYVL 380
Cdd:cd17946  154 ADRMLEKGHFAELEKILELLNKDragkkrkRQTFVFSATLTLDHQLPLKLNSK---------KKKKKKEKKQKLELLI 222
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
164-363 1.09e-24

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: 102.40  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 164 LLEIFQ---YKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHT-------LIIVPTRE 233
Cdd:cd17945    1 LLRVIRklgYKEPTPIQRQAIPIGLQNR---DIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETkddgpyaLILAPTRE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 234 LANQIYNECKLLLTYKhNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTYLfntLFENLKMLIIDEADQL 313
Cdd:cd17945   78 LAQQIEEETQKFAKPL-GIRVVSIVGGHSIEEQAFSLRN-GCEILIATPGRLLDCLERRLL---VLNQCTYVVLDEADRM 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 314 LSTGYENDIHRLLTYLPSN--------------------RRNILLSATLGYNLDEIRKKmcksdyiYLNC 363
Cdd:cd17945  153 IDMGFEPQVTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKG-------YLRR 215
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
192-341 5.39e-24

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: 99.85  E-value: 5.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLL-----LSINDIIKNKILSVHTLIIVPTRELANQIYNECKlllTYKHN-INVLTLTGGiKRRD 265
Cdd:cd17958   29 DLIGVAQTGTGKTLAYLLpgfihLDLQPIPREQRNGPGVLVLTPTRELALQIEAECS---KYSYKgLKSVCVYGG-GNRN 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512888 266 DQLNIRRIKPDIIICTVGRLLDhfestyLFNTLFENLK---MLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSAT 341
Cdd:cd17958  105 EQIEDLSKGVDIIIATPGRLND------LQMNNVINLKsitYLVLDEADRMLDMGFEPQIRKILLDIRPDRQTIMTSAT 177
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
157-352 6.03e-24

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: 99.83  E-value: 6.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 157 DKDVKKSLLE-IFQYKeFTDVQRIVYDNIIKEKKQNDLLIQAKTGTGKTiAYLLLSINDIIKNKILSVHTLIIVPTRELA 235
Cdd:cd18046    3 DMNLKESLLRgIYAYG-FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKT-ATFSISILQQIDTSLKATQALVLAPTRELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 236 NQIYNECKLLLTYKhNINVLTLTGGIKRRDDQlNIRRIKPDIIICTVGRLLDHFESTYLFNtlfENLKMLIIDEADQLLS 315
Cdd:cd18046   81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDA-QKLQAGPHIVVGTPGRVFDMINRRYLRT---DYIKMFVLDEADEMLS 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 124512888 316 TGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKK 352
Cdd:cd18046  156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTK 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
192-353 1.93e-23

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: 98.26  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVH----TLIIVPTRELANQIYNECKLLLTYkHNINVLTLTGGIKRRdDQ 267
Cdd:cd17952   29 DMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGegpiAVIVAPTRELAQQIYLEAKKFGKA-YNLRVVAVYGGGSKW-EQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 268 LNIRRIKPDIIICTVGRLLDHFEstyLFNTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLD 347
Cdd:cd17952  107 AKALQEGAEIVVATPGRLIDMVK---KKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGHVRPDRQTLLFSATFKKKIE 183

                 ....*.
gi 124512888 348 EIRKKM 353
Cdd:cd17952  184 QLARDI 189
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
192-356 3.65e-23

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: 97.66  E-value: 3.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIK-NKILSVHTLIIVPTRELANQIYNECKlLLTYKHNINVLTLTGGIKRRDDQLNI 270
Cdd:cd17957   29 DLLACAPTGSGKTLAFLIPILQKLGKpRKKKGLRALILAPTRELASQIYRELL-KLSKGTGLRIVLLSKSLEAKAKDGPK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 271 RRIKPDIIICTVGRLLDHFEStylfNTL-FENLKMLIIDEADQLLSTGYENDIHRLLTYLPS-NRRNILLSATLGYNLDE 348
Cdd:cd17957  108 SITKYDILVSTPLRLVFLLKQ----GPIdLSSVEYLVLDEADKLFEPGFREQTDEILAACTNpNLQRSLFSATIPSEVEE 183

                 ....*...
gi 124512888 349 irkkMCKS 356
Cdd:cd17957  184 ----LARS 187
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
192-356 8.17e-23

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: 96.62  E-value: 8.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLL--LSIndiiknkilsVHTLIIVPTRELANQIYNECKLLLTYKHN--INVLTLTGGIKRRDdQ 267
Cdd:cd17938   38 DVLMAAETGSGKTGAFCLpvLQI----------VVALILEPSRELAEQTYNCIENFKKYLDNpkLRVALLIGGVKARE-Q 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 268 LNIRRIKPDIIICTVGRLLDHFESTYLfntLFENLKMLIIDEADQLLSTGYENDIHRLLTYLP----SNRR--NILLSAT 341
Cdd:cd17938  107 LKRLESGVDIVVGTPGRLEDLIKTGKL---DLSSVRFFVLDEADRLLSQGNLETINRIYNRIPkitsDGKRlqVIVCSAT 183
                        170
                 ....*....|....*...
gi 124512888 342 LgyNLDEIRK---KMCKS 356
Cdd:cd17938  184 L--HSFEVKKladKIMHF 199
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
184-351 2.59e-21

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: 92.25  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 184 IIKEKKQNdLLIQAKTGTGKTIAYLLLSINDIiKNKILSVHTLIIVPTRELANQIYNECKLLLTYKhNINV-LTLTGGIK 262
Cdd:cd17963   28 ILSDPPEN-LIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQALCLAPTRELARQIGEVVEKMGKFT-GVKVaLAVPGNDV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 263 RRDdqlniRRIKPDIIICTVGRLLDhFESTYLFNTlfENLKMLIIDEADQLLST-GYENDIHRLLTYLPSNRRNILLSAT 341
Cdd:cd17963  105 PRG-----KKITAQIVIGTPGTVLD-WLKKRQLDL--KKIKILVLDEADVMLDTqGHGDQSIRIKRMLPRNCQILLFSAT 176
                        170
                 ....*....|
gi 124512888 342 lgYNlDEIRK 351
Cdd:cd17963  177 --FP-DSVRK 183
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
101-509 3.68e-21

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 97.79  E-value: 3.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 101 DNIIKEDLLYRKNNEKENEEVIKSNIDENKNVHMNDQNEQNKHCYNKLLIESCCHIDKDVKKSLLEIFQYKEFT------ 174
Cdd:COG1061    1 VLLRGIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEAsgtsfe 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 175 --DVQRIVYDNIIK--EKKQNDLLIQAKTGTGKTIAYLLlsindIIKNKILSVHTLIIVPTRELANQIYNECKLLLTYKH 250
Cdd:COG1061   81 lrPYQQEALEALLAalERGGGRGLVVAPTGTGKTVLALA-----LAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 251 NinvltlTGGIKRRDDqlnirrikpDIIICTVGRLLDHFEstylFNTLFENLKMLIIDEADQLLSTGYEndihRLLTYLP 330
Cdd:COG1061  156 A------GGGKKDSDA---------PITVATYQSLARRAH----LDELGDRFGLVIIDEAHHAGAPSYR----RILEAFP 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 331 SNRRnILLSATL------------------GYNLDE-IRKKMCKsDYIYLNCVKDISKHTSD-----QLIQYVLFHKAID 386
Cdd:COG1061  213 AAYR-LGLTATPfrsdgreillflfdgivyEYSLKEaIEDGYLA-PPEYYGIRVDLTDERAEydalsERLREALAADAER 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 387 TTIILYNLLIEHMRlnqfTYKIIVFFPTARATSFYAQFFiNQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDIS 466
Cdd:COG1061  291 KDKILRELLREHPD----DRKTLVFCSSVDHAEALAELL-NEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVL 365
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 124512888 467 SRGLNYPDITLIIQVnTPI-SREQYIHRVGRTAR-SNKKGMAIIL 509
Cdd:COG1061  366 NEGVDVPRLDVAILL-RPTgSPREFIQRLGRGLRpAPGKEDALVY 409
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
192-521 8.04e-21

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 96.40  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLlsinDIIKN--KILSVHT--------LIIVPTRELANQIYNECKLL---LTYKHNINVltlt 258
Cdd:PLN00206 160 SLLVSADTGSGKTASFLV----PIISRccTIRSGHPseqrnplaMVLTPTRELCVQVEDQAKVLgkgLPFKTALVV---- 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 259 GGikrrdDQL--NIRRIKP--DIIICTVGRLLDHFEStylFNTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLpSNRR 334
Cdd:PLN00206 232 GG-----DAMpqQLYRIQQgvELIVGTPGRLIDLLSK---HDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQ 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 335 NILLSATLGYNLDEIRKKMCKsDYIYLNCVKdiSKHTSDQLIQYVLFHKAIDTTIILYNLLiehMRLNQFTYKIIVFFPT 414
Cdd:PLN00206 303 VLLFSATVSPEVEKFASSLAK-DIILISIGN--PNRPNKAVKQLAIWVETKQKKQKLFDIL---KSKQHFKPPAVVFVSS 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 415 ARATSFYAQFFINQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRV 494
Cdd:PLN00206 377 RLGADLLANAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQI 456
                        330       340
                 ....*....|....*....|....*..
gi 124512888 495 GRTARSNKKGMAIILLNEADELFYQEI 521
Cdd:PLN00206 457 GRASRMGEKGTAIVFVNEEDRNLFPEL 483
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
168-353 3.16e-20

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: 89.06  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 168 FQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTiAYLLLSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLT 247
Cdd:cd18045   17 YGFEKPSAIQQRAIKPIIKGR---DVIAQSQSGTGKT-ATFSISVLQCLDIQVRETQALILSPTRELAVQIQKVLLALGD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 248 YKhNINVLTLTGGIKRRDDqlnIRRIKP--DIIICTVGRLLDHFESTYLfntLFENLKMLIIDEADQLLSTGYENDIHRL 325
Cdd:cd18045   93 YM-NVQCHACIGGTSVGDD---IRKLDYgqHIVSGTPGRVFDMIRRRSL---RTRHIKMLVLDEADEMLNKGFKEQIYDV 165
                        170       180
                 ....*....|....*....|....*....
gi 124512888 326 LTYLPSNRRNILLSATLGYN-LDEIRKKM 353
Cdd:cd18045  166 YRYLPPATQVVLVSATLPQDiLEMTNKFM 194
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
163-356 3.96e-20

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: 89.36  E-value: 3.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 163 SLLEIFQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHT----LIIVPTRELANQI 238
Cdd:cd17953   25 DLIKKLGYEKPTPIQAQALPAIMSGR---DVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEgpigLIMAPTRELALQI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 239 YNECKLLlTYKHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTylfNTLFENLK---MLIIDEADQLLS 315
Cdd:cd17953  102 YVECKKF-SKALGLRVVCVYGGSGISEQIAELKR-GAEIVVCTPGRMIDILTAN---NGRVTNLRrvtYVVLDEADRMFD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124512888 316 TGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKMCKS 356
Cdd:cd17953  177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHK 217
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
164-375 2.02e-19

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: 87.81  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 164 LLEIFQYKEF---TDVQRIVYDNIIKekkQNDLLIQAKTGTGKTIAYLLLSINDIIKNKIL------SVHTLIIVPTREL 234
Cdd:cd17948    1 LVEILQRQGItkpTTVQKQGIPSILR---GRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnAPRGLVITPSREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 235 ANQIYNECKlLLTYKHNINVLTLTGGIKRRdDQLNIRRIKPDIIICTVGRLL----DHFESTylfntlfENLKMLIIDEA 310
Cdd:cd17948   78 AEQIGSVAQ-SLTEGLGLKVKVITGGRTKR-QIRNPHFEEVDILVATPGALSklltSRIYSL-------EQLRHLVLDEA 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 311 DQLLSTGYENDIHRLLTYLPSNRRN-------------ILLSATLGYNLDEIRKKMCKSDyiylncvkDISKHTSDQL 375
Cdd:cd17948  149 DTLLDDSFNEKLSHFLRRFPLASRRsentdgldpgtqlVLVSATMPSGVGEVLSKVIDVD--------SIETVTSDKL 218
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
192-356 3.79e-19

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: 86.24  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTiAYLLLSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIR 271
Cdd:cd17950   41 DVLCQAKSGMGKT-AVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLK 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 272 RIKPDIIICTVGRLLDHFESTYLfNTlfENLKMLIIDEADQLL-STGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIR 350
Cdd:cd17950  120 NKCPHIVVGTPGRILALVREKKL-KL--SHVKHFVLDECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVC 196

                 ....*.
gi 124512888 351 KKMCKS 356
Cdd:cd17950  197 KKFMQD 202
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
192-341 4.23e-18

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: 82.80  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVH----TLIIVPTRELANQIYNECKlllTYKHNINVLT--LTGGIKRRD 265
Cdd:cd17966   29 DMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGdgpiVLVLAPTRELAQQIQQEAN---KFGGSSRLRNtcVYGGAPKGP 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512888 266 DQLNIRRiKPDIIICTVGRLLDHFESTYLfntlfeNLK---MLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSAT 341
Cdd:cd17966  106 QIRDLRR-GVEICIATPGRLIDFLDQGKT------NLRrvtYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSAT 177
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
191-341 2.51e-17

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 78.98  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 191 NDLLIQAKTGTGKTIAYLLLSINDIIKnKILSVhtLIIVPTRELANQIYNECKLLLtyKHNINVLTLTGGIKRRDDQLNI 270
Cdd:cd00046    2 ENVLITAPTGSGKTLAALLAALLLLLK-KGKKV--LVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSSAEEREKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124512888 271 RRiKPDIIICTVGRLLDHFESTYLFntLFENLKMLIIDEADQLLSTGYENDIHRL--LTYLPSNRRNILLSAT 341
Cdd:cd00046   77 LG-DADIIIATPDMLLNLLLREDRL--FLKDLKLIIVDEAHALLIDSRGALILDLavRKAGLKNAQVILLSAT 146
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
192-355 2.60e-17

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: 80.67  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIkNKILSVHTLIIVPTRELANQIYNECKLLLTYKHNINVLTLTGGIKRRDdqlNIR 271
Cdd:cd17962   29 DILASADTGSGKTAAFLLPVIIRCL-TEHRNPSALILTPTRELAVQIEDQAKELMKGLPPMKTALLVGGLPLPP---QLY 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 272 RIKP--DIIICTVGRLLDHFESTylfNTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEI 349
Cdd:cd17962  105 RLQQgvKVIIATPGRLLDILKQS---SVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTILVSATIPRGIEQL 181

                 ....*.
gi 124512888 350 RKKMCK 355
Cdd:cd17962  182 AGQLLQ 187
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
392-501 2.24e-16

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: 75.32  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  392 YNLLIEHMRLNQfTYKIIVFFPTARatSFYAQFFINQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLN 471
Cdd:pfam00271   3 LEALLELLKKER-GGKVLIFSQTKK--TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 124512888  472 YPDITLIIQVNTPISREQYIHRVGRTARSN 501
Cdd:pfam00271  80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
162-440 1.08e-15

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 80.32  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 162 KSLLEIFQYKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKT-IAYLllsindIIKNKILSVHT-LIIVPTRELANQIY 239
Cdd:COG1204   12 IEFLKERGIEELYPPQAEALEAGLLEGK--NLVVSAPTASGKTlIAEL------AILKALLNGGKaLYIVPLRALASEKY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 240 NECKLLLTyKHNINVLTLTGGIKRRDDQLNirriKPDIIICTVGRLLdhfeSTYLFNTLF-ENLKMLIIDEAdQLLSTG- 317
Cdd:COG1204   84 REFKRDFE-ELGIKVGVSTGDYDSDDEWLG----RYDILVATPEKLD----SLLRNGPSWlRDVDLVVVDEA-HLIDDEs 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 318 ----YENDIHRLLTYLPSNRRnILLSATLGyNLDEIRKkmcksdyiYLNCVKDISKHTSDQLIQYVLFHKAID------- 386
Cdd:COG1204  154 rgptLEVLLARLRRLNPEAQI-VALSATIG-NAEEIAE--------WLDAELVKSDWRPVPLNEGVLYDGVLRfddgsrr 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124512888 387 TTIILYNLLIEHMRLNQftyKIIVFFPTARATSFYAQFFINQLKISVYEIHRKK 440
Cdd:COG1204  224 SKDPTLALALDLLEEGG---QVLVFVSSRRDAESLAKKLADELKRRLTPEEREE 274
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
151-361 2.84e-15

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: 75.85  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 151 ESC-CHIDKDVKKSLLEIFQ-------YKEFTDVQRIVYDnIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKN---K 219
Cdd:cd18051   14 ENCpPHIETFSDLDLGEIIRnnielarYTKPTPVQKHAIP-IIKSKR--DLMACAQTGSGKTAAFLLPILSQIYEQgpgE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 220 ILSVHT------------LIIVPTRELANQIYNECKlLLTYKHNINVLTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLD 287
Cdd:cd18051   91 SLPSESgyygrrkqyplaLVLAPTRELASQIYDEAR-KFAYRSRVRPCVVYGGADIGQQMRDLER-GCHLLVATPGRLVD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512888 288 HFESTYLFntlFENLKMLIIDEADQLLSTGYENDIHRLL---TYLPSNRRNILL-SATLGYNLDEIRKKMCkSDYIYL 361
Cdd:cd18051  169 MLERGKIG---LDYCKYLVLDEADRMLDMGFEPQIRRIVeqdTMPPTGERQTLMfSATFPKEIQMLARDFL-DNYIFL 242
HELICc smart00490
helicase superfamily c-terminal domain;
425-499 5.83e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 70.32  E-value: 5.83e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124512888   425 FINQLKISVYEIHRKKEMAHRQITANRFSMESVGILFTSDISSRGLNYPDITLIIQVNTPISREQYIHRVGRTAR 499
Cdd:smart00490   6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
192-342 1.13e-14

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: 73.14  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAY----LLLSINDIIKNKILS---VHTLIIVPTRELANQIYNE----CKLLLTYKH-NINVLTLTG 259
Cdd:cd17951   29 DMIGIAFTGSGKTLVFtlplIMFALEQEKKLPFIKgegPYGLIVCPSRELARQTHEVieyyCKALQEGGYpQLRCLLCIG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 260 GIKRRDdQLNIRRIKPDIIICTVGRLLDhfestyLFNTLFENLKM---LIIDEADQLLSTGYENDIHRLLTYLPSNRRNI 336
Cdd:cd17951  109 GMSVKE-QLEVIRKGVHIVVATPGRLMD------MLNKKKINLDIcryLCLDEADRMIDMGFEEDIRTIFSYFKGQRQTL 181

                 ....*.
gi 124512888 337 LLSATL 342
Cdd:cd17951  182 LFSATM 187
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
192-362 1.25e-14

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: 72.96  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLL-----LSINDIIKNKILSVHTLIIVPTRELANQIYNECKlLLTYKhnINVLTLTGGIKrRDD 266
Cdd:cd17944   29 DLIAQARTGTGKTFSFAIpliekLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFK-DITRK--LSVACFYGGTP-YQQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 267 QLNIRRIKPDIIICTVGRLLDHFESTYLFNTlfeNLKMLIIDEADQLLSTGYENDIHRLLTYL-----PSNRRNILLSAT 341
Cdd:cd17944  105 QIFAIRNGIDILVGTPGRIKDHLQNGRLDLT---KLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDNPQTLLFSAT 181
                        170       180
                 ....*....|....*....|.
gi 124512888 342 LGYNLDEIRKKMCKSDYIYLN 362
Cdd:cd17944  182 CPDWVYNVAKKYMKSQYEQVD 202
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
182-353 1.94e-14

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: 73.56  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 182 DNIIKEKKQNDLLIQAKTGTGKTIAYLLLSINDI-----------------IKNKILsVHTLIIVPTRELANQIYNECKL 244
Cdd:cd17965   53 QTSNEEPKLEVFLLAAETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyesAKDTGR-PRSVILVPTHELVEQVYSVLKK 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 245 LLTY-KHNINVLTLTGGIKRRDDQLNIrRIKPDIIICTVGRLLDHFESTylfNTLFENLKMLIIDEADQLLSTGYENDIH 323
Cdd:cd17965  132 LSHTvKLGIKTFSSGFGPSYQRLQLAF-KGRIDILVTTPGKLASLAKSR---PKILSRVTHLVVDEADTLFDRSFLQDTT 207
                        170       180       190
                 ....*....|....*....|....*....|
gi 124512888 324 RLLTYLPSNRRNILLSATLGYNLDEIRKKM 353
Cdd:cd17965  208 SIIKRAPKLKHLILCSATIPKEFDKTLRKL 237
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
172-360 3.66e-14

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: 71.14  E-value: 3.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 172 EFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHtliIVPTRELANQIYNECKLLLTyKHN 251
Cdd:cd17921    1 LLNPIQREALRALYLSGD--SVLVSAPTSSGKTLIAELAILRALATSGGKAVY---IAPTRALVNQKEADLRERFG-PLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 252 INVLTLTGGIKRRDDQLnirrIKPDIIICTVGRLldHFESTYLFNTLFENLKMLIIDEAdQLLSTG-----YEnDIHRLL 326
Cdd:cd17921   75 KNVGLLTGDPSVNKLLL----AEADILVATPEKL--DLLLRNGGERLIQDVRLVVVDEA-HLIGDGergvvLE-LLLSRL 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 124512888 327 TYLPSNRRNILLSATLGyNLDEIRKKMCKSDYIY 360
Cdd:cd17921  147 LRINKNARFVGLSATLP-NAEDLAEWLGVEDLIR 179
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
162-362 4.58e-14

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: 71.96  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 162 KSLLEIFQYKEFTDVQRIVYDNIIKEKKQNDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVH----TLIIVPTRELANQ 237
Cdd:cd18049   33 ANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpiCLVLAPTRELAQQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 238 IYN-------ECKLLLTykhninvlTLTGGIKRRDDQLNIRRiKPDIIICTVGRLLDHFESTylfNTLFENLKMLIIDEA 310
Cdd:cd18049  113 VQQvaaeygrACRLKST--------CIYGGAPKGPQIRDLER-GVEICIATPGRLIDFLEAG---KTNLRRCTYLVLDEA 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124512888 311 DQLLSTGYENDIHRLLTYLPSNRRNILLSATLGYNLDEIRKKMCKsDYIYLN 362
Cdd:cd18049  181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLK-DYIHIN 231
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
191-351 5.50e-13

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: 67.22  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 191 NDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLTYKH-NINVLTLTG----GIKRRd 265
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDlEIPVAVRHGdtsqSEKAK- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 266 dqlnIRRIKPDIIICTVgrlldhfESTYL------FNTLFENLKMLIIDE---------ADQLLSTgyendIHRLLTYLP 330
Cdd:cd17922   81 ----QLKNPPGILITTP-------ESLELllvnkkLRELFAGLRYVVVDEihallgskrGVQLELL-----LERLRKLTG 144
                        170       180
                 ....*....|....*....|.
gi 124512888 331 SNRRNILLSATLGyNLDEIRK 351
Cdd:cd17922  145 RPLRRIGLSATLG-NLEEAAA 164
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
192-362 7.44e-13

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: 69.27  E-value: 7.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVH----TLIIVPTRELANQI------YNECKllltykhNINVLTLTGGI 261
Cdd:cd18050  101 DMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpiCLVLAPTRELAQQVqqvaddYGKSS-------RLKSTCIYGGA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 262 KRRDDQLNIRRiKPDIIICTVGRLLDHFESTylfNTLFENLKMLIIDEADQLLSTGYENDIHRLLTYLPSNRRNILLSAT 341
Cdd:cd18050  174 PKGPQIRDLER-GVEICIATPGRLIDFLEAG---KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSAT 249
                        170       180
                 ....*....|....*....|.
gi 124512888 342 LGYNLDEIRKKMCKsDYIYLN 362
Cdd:cd18050  250 WPKEVRQLAEDFLR-DYVQIN 269
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
177-342 4.87e-10

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: 58.09  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 177 QRIVYDNIIKEKKQNDLLIQAKTGTGKTIAYLLLSIndiiknKILSVHTLIIVPTRELANQIYNECKLLLTYKHnINVLt 256
Cdd:cd17926    5 QEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIA------YLKELRTLIVVPTDALLDQWKERFEDFLGDSS-IGLI- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 257 ltgGIKRRDDQLNIrrikpDIIICTVGRLLDHFESTYLFNTLFEnlkMLIIDEADQLLSTGYEndihRLLTYLPSNRRnI 336
Cdd:cd17926   77 ---GGGKKKDFDDA-----NVVVATYQSLSNLAEEEKDLFDQFG---LLIVDEAHHLPAKTFS----EILKELNAKYR-L 140

                 ....*.
gi 124512888 337 LLSATL 342
Cdd:cd17926  141 GLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
171-341 1.33e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 57.30  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  171 KEFTDVQRIVYDNIIK--EKKQNDLLIQAKTGTGKTiaYLLLSINDIIKNKILSVHTLIIVPTRELANQIYNECKLLLTY 248
Cdd:pfam04851   2 LELRPYQIEAIENLLEsiKNGQKRGLIVMATGSGKT--LTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888  249 KHNINvlTLTGGIKRRDDQLNIRrikpdIIICTVGRLLDHFESTYLFNtLFENLKMLIIDEADQLLSTGYENdihrLLTY 328
Cdd:pfam04851  80 YVEIG--EIISGDKKDESVDDNK-----IVVTTIQSLYKALELASLEL-LPDFFDVIIIDEAHRSGASSYRN----ILEY 147
                         170
                  ....*....|...
gi 124512888  329 LPSNRRnILLSAT 341
Cdd:pfam04851 148 FKPAFL-LGLTAT 159
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
192-515 3.33e-08

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 55.90  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 192 DLLIQAKTGTGKTIAYLLLSINDIIKNKILSVhtLIIVPTRELANQIYNECKLLLTYKHNINVLTLTGGIKRRDDQLNIR 271
Cdd:cd09639    1 LLVIEAPTGYGKTEAALLWALHSLKSQKADRV--IIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMGDSEEFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 272 RI-------------------KPDIIICTVGRLLDHFEsTYLFNTLFENlkmLIIDEADQLLSTGYENdIHRLLTYLPSN 332
Cdd:cd09639   79 HLfplyihsndtlfldpitvcTIDQVLKSVFGEFGHYE-FTLASIANSL---LIFDEVHFYDEYTLAL-ILAVLEVLKDN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 333 RRNILL-SATLGYNLDEIRKKMCksdyiylNCVKDISKHTSD-QLIQYVLFHKAIDTTIILYNLLIEHmrLNQFTYKIIV 410
Cdd:cd09639  154 DVPILLmSATLPKFLKEYAEKIG-------YVEENEPLDLKPnERAPFIKIESDKVGEISSLERLLEF--IKKGGSVAII 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 411 FFPTARATSFYAQF--FINQLKISVY-----EIHRKKEMAhrqITANRFSMESVGILFTSDISSRGLNYpDITLIIQVNT 483
Cdd:cd09639  225 VNTVDRAQEFYQQLkeKGPEEEIMLIhsrftEKDRAKKEA---ELLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELA 300
                        330       340       350
                 ....*....|....*....|....*....|...
gi 124512888 484 PISReqYIHRVGRTAR-SNKKGMAIILLNEADE 515
Cdd:cd09639  301 PIDS--LIQRLGRLHRyGEKNGEEVYIITDAPD 331
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
174-343 5.22e-08

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: 53.87  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 174 TDVQRIVYDNIIKEKKQNdLLIQAKTGTGKTIAYLLLSINDIIKNKILSvHTLIIVPTRELANQIYNECKLLLTYKHNIN 253
Cdd:cd18048   42 SKIQENALPMMLADPPQN-LIAQSQSGTGKTAAFVLAMLSRVDALKLYP-QCLCLSPTFELALQTGKVVEEMGKFCVGIQ 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 254 VLTLTGGIKRRDDQlnirRIKPDIIICTVGRLLDHFESTYLFNtlFENLKMLIIDEADQLLST-GYENDIHRLLTYLPSN 332
Cdd:cd18048  120 VIYAIRGNRPGKGT----DIEAQIVIGTPGTVLDWCFKLRLID--VTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKE 193
                        170
                 ....*....|.
gi 124512888 333 RRNILLSATLG 343
Cdd:cd18048  194 CQMLLFSATFE 204
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
172-309 7.21e-08

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: 52.80  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 172 EFTDVQRIVYDNIIKE---KKQNDLLIQAKTGTGKTIAYLLLSINDIIKNKilsvHTLIIVPTRELANQIYNECKlllTY 248
Cdd:cd17918   15 SLTKDQAQAIKDIEKDlhsPEPMDRLLSGDVGSGKTLVALGAALLAYKNGK----QVAILVPTEILAHQHYEEAR---KF 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124512888 249 KHNINVLTLTGGIKRRDDQlnirriKPDIIICTVGRLldHFEStylfntLFENLKMLIIDE 309
Cdd:cd17918   88 LPFINVELVTGGTKAQILS------GISLLVGTHALL--HLDV------KFKNLDLVIVDE 134
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
189-349 1.55e-07

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: 51.57  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 189 KQNDLLIQAKTGTGKTIAYLLLSINDIIKNKilsvHTLIIVPTRELANQIYNECKLLltYKHNINVLTLTGGIKRRDDQL 268
Cdd:cd18028   16 KGENLLISIPTASGKTLIAEMAMVNTLLEGG----KALYLVPLRALASEKYEEFKKL--EEIGLKVGISTGDYDEDDEWL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 269 NirriKPDIIICTVGRL--LDHFESTYLfntlfENLKMLIIDEADQLLSTG----YENDIHRLLTYLPsNRRNILLSATL 342
Cdd:cd18028   90 G----DYDIIVATYEKFdsLLRHSPSWL-----RDVGVVVVDEIHLISDEErgptLESIVARLRRLNP-NTQIIGLSATI 159

                 ....*..
gi 124512888 343 GyNLDEI 349
Cdd:cd18028  160 G-NPDEL 165
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
174-342 1.76e-07

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: 52.03  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 174 TDVQRIVYDNIIKEKKQNdLLIQAKTGTGKTIAYLLLSINDIIKNKILSvHTLIIVPTRELANQIYNECKLLLTYKHNIn 253
Cdd:cd18047   25 SKIQENALPLMLAEPPQN-LIAQSQSGTGKTAAFVLAMLSQVEPANKYP-QCLCLSPTYELALQTGKVIEQMGKFYPEL- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 254 vlTLTGGIKRRDDQLNIrRIKPDIIICTVGRLLDHFESTYLFNTlfENLKMLIIDEADQLLST-GYENDIHRLLTYLPSN 332
Cdd:cd18047  102 --KLAYAVRGNKLERGQ-KISEQIVIGTPGTVLDWCSKLKFIDP--KKIKVFVLDEADVMIATqGHQDQSIRIQRMLPRN 176
                        170
                 ....*....|
gi 124512888 333 RRNILLSATL 342
Cdd:cd18047  177 CQMLLFSATF 186
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
191-310 2.48e-06

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: 48.35  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 191 NDLLIQAKTGTGKTIAYLLLSINDIIKNKilSVHTLIIVPTRELAN-QIYNECKLLLTYKHNINVLTLTGGIKRRDDQlN 269
Cdd:cd17923   16 RSVVVTTGTASGKSLCYQLPILEALLRDP--GSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDGDTPREERR-A 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 124512888 270 IRRIKPDIIIcTVGRLLDH--FESTYLFNTLFENLKMLIIDEA 310
Cdd:cd17923   93 IIRNPPRILL-TNPDMLHYalLPHHDRWARFLRNLRYVVLDEA 134
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
156-309 9.75e-06

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 47.14  E-value: 9.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEIFQYkEFTDVQRIVYDNIIKEKKQNDL---LIQAKTGTGKTIAYLLLSINdIIKNkilSVHTLIIVPTR 232
Cdd:cd17992   30 ISGELLKKFLEALPF-ELTGAQKRVIDEILRDLASEKPmnrLLQGDVGSGKTVVAALAMLA-AVEN---GYQVALMAPTE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 233 ELANQIYNECKLLLTyKHNINVLTLTGGIK---RRDDQLNIRRIKPDIIICTvgrlldHfestYLF--NTLFENLKMLII 307
Cdd:cd17992  105 ILAEQHYDSLKKLLE-PLGIRVALLTGSTKakeKREILEKIASGEIDIVIGT------H----ALIqeDVEFHNLGLVII 173

                 ..
gi 124512888 308 DE 309
Cdd:cd17992  174 DE 175
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
191-343 2.61e-05

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: 47.52  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 191 NDLLIQAKTGTGKTIAYLLLSINDIIKNKilSVHTLIIVPTRELANQIYNEC-KLLLTYKHNINVLTLTGGI---KRRDd 266
Cdd:COG1205   72 KNVVIATPTASGKSLAYLLPVLEALLEDP--GATALYLYPTKALARDQLRRLrELAEALGLGVRVATYDGDTppeERRW- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 267 qlnIRRiKPDIIICT-----VGRLLDHFEstylFNTLFENLKMLIIDEAdqllstgyendiH------------------ 323
Cdd:COG1205  149 ---IRE-HPDIVLTNpdmlhYGLLPHHTR----WARFFRNLRYVVIDEA------------Htyrgvfgshvanvlrrlr 208
                        170       180
                 ....*....|....*....|
gi 124512888 324 RLLTYLPSNRRNILLSATLG 343
Cdd:COG1205  209 RICRHYGSDPQFILASATIG 228
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
193-342 4.78e-05

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 44.59  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 193 LLIQAKTGTGKTIAYLLLSINDIIKNKILSVhtLIIVPTRELANQIYNE-CKLLLTYKHNINVLTLTGG----------- 260
Cdd:cd17930    4 VILEAPTGSGKTEAALLWALKLAARGGKRRI--IYALPTRATINQMYERiREILGRLDDEDKVLLLHSKaalellesdee 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 261 ------IKRRDDQLNIRRIKPDIIICTVgrllDHFESTYLFNTLFE----NL--KMLIIDEAdQLLSTGYENDIHRLLTY 328
Cdd:cd17930   82 pdddpvEAVDWALLLKRSWLAPIVVTTI----DQLLESLLKYKHFErrlhGLanSVVVLDEV-QAYDPEYMALLLKALLE 156
                        170
                 ....*....|....*.
gi 124512888 329 LPS--NRRNILLSATL 342
Cdd:cd17930  157 LLGelGGPVVLMTATL 172
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
195-342 5.83e-05

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 44.24  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 195 IQAKTGTGKTIAYLLLSINDIIKNKilsvHTLIIVPTRELANQIYNECKLLLTYKH-NINVLTLTGGIKRRDDQLNIRRI 273
Cdd:cd17924   37 IIAPTGVGKTTFGLATSLYLASKGK----RSYLIFPTKSLVKQAYERLSKYAEKAGvEVKILVYHSRLKKKEKEELLEKI 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124512888 274 KP---DIIICTVGRLLDHFE--STYLFNTLFenlkmliIDEADQLLSTGyeNDIHRLLtYLPSNRRNILLSATL 342
Cdd:cd17924  113 EKgdfDILVTTNQFLSKNFDllSNKKFDFVF-------VDDVDAVLKSS--KNIDRLL-KLLGFGQLVVSSATG 176
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
155-342 6.04e-05

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: 45.84  E-value: 6.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 155 HIDKDVKKSLLEIFQ-YKEFTDVQRIVYDNIIK--EKKQNDLLIQAKTGTGKTIAYLLLSINDIIKNKILSVhtLIIVPT 231
Cdd:COG1203  109 LLAERLERLLPKKSKpRTPINPLQNEALELALEaaEEEPGLFILTAPTGGGKTEAALLFALRLAAKHGGRRI--IYALPF 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 232 RELANQIYNECKLLLtykhNINVLTLTGGI------KRRDDQLNIRRIKP-------DIIICTVgrllDHFestylFNTL 298
Cdd:COG1203  187 TSIINQTYDRLRDLF----GEDVLLHHSLAdldlleEEEEYESEARWLKLlkelwdaPVVVTTI----DQL-----FESL 253
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 124512888 299 FEN-----LKM-------LIIDEAdQLLSTGYENDIHRLLTYLPS-NRRNILLSATL 342
Cdd:COG1203  254 FSNrkgqeRRLhnlansvIILDEV-QAYPPYMLALLLRLLEWLKNlGGSVILMTATL 309
PRK13767 PRK13767
ATP-dependent helicase; Provisional
169-239 8.27e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 45.65  E-value: 8.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124512888 169 QYKEFTDVQRIVydnIIKEKKQNDLLIQAKTGTGKTIAYLLLSINDII---KNKIL--SVHTLIIVPTRELANQIY 239
Cdd:PRK13767  29 KFGTFTPPQRYA---IPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFrlgREGELedKVYCLYVSPLRALNNDIH 101
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
188-310 1.89e-03

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: 39.94  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 188 KKQNdLLIQAKTGTGKT-IAYLLL----SINDIIKN--KIlsvhTLIIVPTRELANQIYNECKLLLTYKhninVLTLTGG 260
Cdd:cd18034   15 LKRN-TIVVLPTGSGKTlIAVMLIkemgELNRKEKNpkKR----AVFLVPTVPLVAQQAEAIRSHTDLK----VGEYSGE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124512888 261 I---KRRDDQLNIRRIKPDIIICTVGRLLDHFESTYLFntlFENLKMLIIDEA 310
Cdd:cd18034   86 MgvdKWTKERWKEELEKYDVLVMTAQILLDALRHGFLS---LSDINLLIFDEC 135
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
180-209 2.34e-03

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 41.06  E-value: 2.34e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 124512888 180 VYDNIikeKKQNDLLIQAKTGTGKTIAYLL 209
Cdd:COG1199   26 VARAL---AEGRHLLIEAGTGTGKTLAYLV 52
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
156-281 4.15e-03

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 40.26  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 156 IDKDVKKSLLEIFqyKEFTDVQRIVYDNIIKEKKqnDLLIQAKTGTGKTIAYLLLSINDIIKNKilsVHTLIIVPTRELA 235
Cdd:COG1202  195 LPPELKDLLEGRG--EELLPVQSLAVENGLLEGK--DQLVVSATATGKTLIGELAGIKNALEGK---GKMLFLVPLVALA 267
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 124512888 236 NQIYNECKllLTYKHNINVLTLTGGIKRRDDQLNiRRIKPDIIICT 281
Cdd:COG1202  268 NQKYEDFK--DRYGDGLDVSIRVGASRIRDDGTR-FDPNADIIVGT 310
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
161-310 4.70e-03

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: 38.67  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 161 KKSLLEIFQYKEFTDVQRIVYDNIIKEKkqnDLLIQAKTGTGKTIAYLLLSindIIKNKIlsvhTLIIVPTREL-ANQIY 239
Cdd:cd17920    1 EQILKEVFGYDEFRPGQLEAINAVLAGR---DVLVVMPTGGGKSLCYQLPA---LLLDGV----TLVVSPLISLmQDQVD 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512888 240 nECKLLltykhNINVLTLTGGIK---RRDDQLNIRRIKPDIIICTVGRLLdhfeSTYLFNTL-----FENLKMLIIDEA 310
Cdd:cd17920   71 -RLQQL-----GIRAAALNSTLSpeeKREVLLRIKNGQYKLLYVTPERLL----SPDFLELLqrlpeRKRLALIVVDEA 139
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
140-309 6.70e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 39.36  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 140 QNKHCYNKLLIESCCHIDKDVKKSLLEI--FqykEFTDVQRIVYDNIIkekkqNDL--------LIQAKTGTGKTI-Ayl 208
Cdd:PRK10917 230 LLLRAGRRSKKAGPLPYDGELLKKFLASlpF---ELTGAQKRVVAEIL-----ADLaspkpmnrLLQGDVGSGKTVvA-- 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512888 209 LLSINDIIKNKILSVhtlIIVPTRELANQIYNECKLLLTyKHNINVLTLTGGIK---RRDDQLNIRRIKPDIIICTvgrl 285
Cdd:PRK10917 300 ALAALAAIEAGYQAA---LMAPTEILAEQHYENLKKLLE-PLGIRVALLTGSLKgkeRREILEAIASGEADIVIGT---- 371
                        170       180
                 ....*....|....*....|....*.
gi 124512888 286 ldHfestYLF--NTLFENLKMLIIDE 309
Cdd:PRK10917 372 --H----ALIqdDVEFHNLGLVIIDE 391
 
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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