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Conserved domains on  [gi|13540304|gb|AAK29402|]
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nucleolar protein GU2 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423699)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
139-526 1.66e-147

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 436.89  E-value: 1.66e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 218
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 296
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 297 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 376
Cdd:COG0513 159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 377 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 450
Cdd:COG0513 231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13540304 451 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 526
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
568-659 6.71e-49

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


:

Pssm-ID: 240593  Cd Length: 93  Bit Score: 166.86  E-value: 6.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 568 HISGASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAE 647
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 13540304 648 WHDS-DWILSVPA 659
Cdd:cd12936  81 WHDSrRWQLSVAT 93
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
139-526 1.66e-147

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 436.89  E-value: 1.66e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 218
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 296
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 297 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 376
Cdd:COG0513 159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 377 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 450
Cdd:COG0513 231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13540304 451 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 526
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
148-349 2.66e-141

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: 412.70  E-value: 2.66e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 227
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 307
Cdd:cd17944  81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13540304 308 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 349
Cdd:cd17944 161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-518 2.03e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 293.25  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  138 AFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 217
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  218 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:PRK11776  79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  293 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 371
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  372 SQRPAVIGDVLQVYSGSEgrAIIFCETKKNVTEMA--MNpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 449
Cdd:PRK11776 227 DERLPALQRLLLHHQPES--CVVFCNTKKECQEVAdaLN-AQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13540304  450 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPS 518
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
162-336 6.98e-52

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: 177.43  E-value: 6.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 239
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   240 VACFYGGTSYQSQINHIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 319
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 13540304   320 PQTLLFSATCPQWVYKV 336
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
568-659 6.71e-49

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


Pssm-ID: 240593  Cd Length: 93  Bit Score: 166.86  E-value: 6.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 568 HISGASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAE 647
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 13540304 648 WHDS-DWILSVPA 659
Cdd:cd12936  81 WHDSrRWQLSVAT 93
DEXDc smart00487
DEAD-like helicases superfamily;
152-342 6.82e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 159.58  E-value: 6.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304    152 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304    231 FKDITRK--LSVACFYGGTSYQSQINHIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 307
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13540304    308 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:smart00487 154 LKLLPK-----NVQLLLLSATPPEEIENLLELFLN 183
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
571-665 2.51e-35

GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein family.


Pssm-ID: 462378  Cd Length: 96  Bit Score: 128.81  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   571 GASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHD 650
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 13540304   651 SD-WILSVPAKLPEIE 665
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
391-484 6.03e-05

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 46.52  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   391 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 466
Cdd:TIGR00631 444 RVLVTTLTKKmaeDLTDYLKELGIK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 519
                          90       100
                  ....*....|....*....|...
gi 13540304   467 qDVESYIhRSGRT-----GRAGR 484
Cdd:TIGR00631 520 -DKEGFL-RSERSliqtiGRAAR 540
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
139-526 1.66e-147

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 436.89  E-value: 1.66e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 218
Cdd:COG0513   4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 296
Cdd:COG0513  79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 297 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 376
Cdd:COG0513 159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 377 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 450
Cdd:COG0513 231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13540304 451 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 526
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
148-349 2.66e-141

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: 412.70  E-value: 2.66e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 227
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 307
Cdd:cd17944  81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13540304 308 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 349
Cdd:cd17944 161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
138-518 2.03e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 293.25  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  138 AFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 217
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  218 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:PRK11776  79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  293 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 371
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  372 SQRPAVIGDVLQVYSGSEgrAIIFCETKKNVTEMA--MNpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 449
Cdd:PRK11776 227 DERLPALQRLLLHHQPES--CVVFCNTKKECQEVAdaLN-AQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13540304  450 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPS 518
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
148-342 6.12e-85

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 266.62  E-value: 6.12e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 227
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVE 305
Cdd:cd00268  79 AEVARKLGKgtGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 13540304 306 DIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd00268 159 KILSALPK-----DRQTLLFSATLPEEVKELAKKFLK 190
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
136-518 4.94e-78

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 262.86  E-value: 4.94e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  136 EGAFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVL 215
Cdd:PRK11634   5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD------PELKAPQIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  216 VLAPTRELANQVAK---DFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:PRK11634  79 VLAPTRELAVQVAEamtDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  293 DQMLDLGFAEQVEDIIHESyktdsEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQvdlvgkMTQKAATTVEHLAiQCHWS 372
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQI-----PEGHQTALFSATMPEAIRRITRRFMKEPQEV------RIQSSVTTRPDIS-QSYWT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  373 QRPAVIGDVLQVYSGSEG--RAIIFCETKKNVTEMAMN-PHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 449
Cdd:PRK11634 227 VWGMRKNEALVRFLEAEDfdAAIIFVRTKNATLEVAEAlERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13540304  450 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPS 518
Cdd:PRK11634 307 RGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPN 375
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
93-508 1.40e-68

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 233.27  E-value: 1.40e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   93 RKDLPNGDIDEYEKKSKRVSSLdtsthkssdnKLEETLTrEQKEGA--FSNFPISEETIKLLKGRGVTYLFPIQVKTFGP 170
Cdd:PRK01297  52 RAEKPKKDKPRRERKPKPASLW----------KLEDFVV-EPQEGKtrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  171 VYEGKDLIAQARTGTGKTFSFAIPLIERLQrnQETIKKSR---SPKVLVLAPTRELANQVAKDFKDITR--KLSVACFYG 245
Cdd:PRK01297 121 TLAGHDAIGRAQTGTGKTAAFLISIINQLL--QTPPPKERymgEPRALIIAPTRELVVQIAKDAAALTKytGLNVMTFVG 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  246 GTSYQSQINHIR-NGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHEsykTDSEDNPQTLL 324
Cdd:PRK01297 199 GMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQ---TPRKEERQTLL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  325 FSATCPQWVYKVAKKYMksrYEQVDLVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVlqVYSGSEGRAIIFCETKKNVTE 404
Cdd:PRK01297 276 FSATFTDDVMNLAKQWT---TDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNL--VTQNPWERVMVFANRKDEVRR 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  405 MamNPHIKQ---NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGR 481
Cdd:PRK01297 351 I--EERLVKdgiNAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGR 428
                        410       420
                 ....*....|....*....|....*..
gi 13540304  482 AGRTGICICFYQPRERGQLRYVEQKAG 508
Cdd:PRK01297 429 AGASGVSISFAGEDDAFQLPEIEELLG 455
PTZ00110 PTZ00110
helicase; Provisional
140-494 2.15e-67

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 231.97  E-value: 2.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  140 SNFPisEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqRNQETIKKSRSPKVLVLAP 219
Cdd:PTZ00110 135 TSFP--DYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI-NAQPLLRYGDGPIVLVLAP 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  220 TRELANQV---AKDFKDITrKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 296
Cdd:PTZ00110 212 TRELAEQIreqCNKFGASS-KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  297 DLGFAEQVEDIIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSRYEQVDlVGKMTQKAATTVEHLAIQCHWSQR 374
Cdd:PTZ00110 291 DMGFEPQIRKIV-------SQIRPdrQTLMWSATWPKEVQSLARDLCKEEPVHVN-VGSLDLTACHNIKQEVFVVEEHEK 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  375 PAVIGDVLQVYSGSEGRAIIFCETKKN----VTEMAMN--PhikqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVA 448
Cdd:PTZ00110 363 RGKLKMLLQRIMRDGDKILIFVETKKGadflTKELRLDgwP-----ALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 13540304  449 ARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQP 494
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
139-506 8.06e-66

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 224.44  E-value: 8.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQ---RnqetiKKSRSPKVL 215
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfpR-----RKSGPPRIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  216 VLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVD 293
Cdd:PRK11192  78 ILTPTRELAMQVADQARELAKhtHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  294 QMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP-QWVYKVAKKYMK---------SRYEQvdlvGKMTQ--KAATT 361
Cdd:PRK11192 158 RMLDMGFAQDIETIAAE-----TRWRKQTLLFSATLEgDAVQDFAERLLNdpveveaepSRRER----KKIHQwyYRADD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  362 VEH-LAIQCHWSQRPAVigdvlqvysgseGRAIIFCETKKNVTEMAMNPHiKQNAQC--LHGDIAQSQREITLKGFREGS 438
Cdd:PRK11192 229 LEHkTALLCHLLKQPEV------------TRSIVFVRTRERVHELAGWLR-KAGINCcyLEGEMVQAKRNEAIKRLTDGR 295
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13540304  439 FKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQL----RYVEQK 506
Cdd:PRK11192 296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLgkieRYIEEP 367
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
133-491 7.99e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 221.38  E-value: 7.99e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  133 EQKegaFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL-QRNQETIKKSRS 211
Cdd:PRK04837   7 EQK---FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlSHPAPEDRKVNQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  212 PKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVL 289
Cdd:PRK04837  84 PRALIMAPTRELAVQIHADAEPLAQatGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  290 DEVDQMLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKS-RYEQVDlvgkMTQKAATTV-EHL-- 365
Cdd:PRK04837 164 DEADRMFDLGF---IKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVE----PEQKTGHRIkEELfy 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  366 ------------AIQCHWSQrpavigdvlqvysgsegRAIIFCETKKNVTE----MAMNPHikqNAQCLHGDIAQSQREI 429
Cdd:PRK04837 237 psneekmrllqtLIEEEWPD-----------------RAIIFANTKHRCEEiwghLAADGH---RVGLLTGDVAQKKRLR 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13540304  430 TLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICF 491
Cdd:PRK04837 297 ILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
144-349 1.97e-59

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: 199.73  E-value: 1.97e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 144 ISEETIKLLKGRGVTYLFPIQVKTFGPVYE-GKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSpKVLVLAPTRE 222
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGV-SALIISPTRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 223 LANQVAKDFKDIT---RKLSVACFYGGTSYQSQIN-HIRNGIDILVGTPGRIKDHL--QSGRLDLSKLRHVVLDEVDQML 296
Cdd:cd17964  80 LALQIAAEAKKLLqglRKLRVQSAVGGTSRRAELNrLRRGRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRLL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13540304 297 DLGFAEQVEDIIhESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 349
Cdd:cd17964 160 DMGFRPDLEQIL-RHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
PTZ00424 PTZ00424
helicase 45; Provisional
163-505 1.06e-58

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 204.29  E-value: 1.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  163 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC 242
Cdd:PTZ00424  54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD------LNACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  243 F--YGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQvediIHESYKTDSEDnP 320
Cdd:PTZ00424 128 HacVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQ----IYDVFKKLPPD-V 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  321 QTLLFSATCPQWVYKVAKKYMKsryeqvDLVGKMTQKAATTVE-----HLAIQCHwSQRPAVIGDVLQVYSGSEgrAIIF 395
Cdd:PTZ00424 203 QVALFSATMPNEILELTTKFMR------DPKRILVKKDELTLEgirqfYVAVEKE-EWKFDTLCDLYETLTITQ--AIIY 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  396 CETKKNVTEMAMNPHIKQ-NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIH 474
Cdd:PTZ00424 274 CNTRRKVDYLTKKMHERDfTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIH 353
                        330       340       350
                 ....*....|....*....|....*....|.
gi 13540304  475 RSGRTGRAGRTGICICFYQPRERGQLRYVEQ 505
Cdd:PTZ00424 354 RIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
139-506 5.31e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 204.03  E-value: 5.31e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL-QRNQETIKKSRSPKVLVL 217
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlSRPALADRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  218 APTRELANQVAKDFKDITRKLSV--ACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQ 294
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADLGLrfALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEADR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  295 MLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKsryEQVDLVGKMTQKAATTVEHlaiQCHWSQR 374
Cdd:PRK04537 171 MFDLGF---IKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMN---EPEKLVVETETITAARVRQ---RIYFPAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  375 PAVIGDVLQVYSGSEG-RAIIFCETKKNVTEMAMNphIKQNAQ---CLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 450
Cdd:PRK04537 242 EEKQTLLLGLLSRSEGaRTMVFVNTKAFVERVART--LERHGYrvgVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  451 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQL----RYVEQK 506
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLpdieAYIEQK 379
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
138-517 3.74e-54

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 193.49  E-value: 3.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  138 AFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVL 217
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  218 APTRELANQVAKDFKDITRKLSVACF--YGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQM 295
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLvvFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  296 LDLGFaeqvediIHESYKTDSEDNP--QTLLFSATCPQWVYKVAKKYMKSRyEQVDLVgkmtqKAATTVEHLAIQCHWSQ 373
Cdd:PRK10590 162 LDMGF-------IHDIRRVLAKLPAkrQNLLFSATFSDDIKALAEKLLHNP-LEIEVA-----RRNTASEQVTQHVHFVD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  374 R-------PAVIGDvlqvysGSEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFK 440
Cdd:PRK10590 229 KkrkrellSQMIGK------GNWQQVLVFTRTKHGANHLA-----EQlnkdgiRSAAIHGNKSQGARTRALADFKSGDIR 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13540304  441 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVP 517
Cdd:PRK10590 298 VLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
162-336 6.98e-52

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: 177.43  E-value: 6.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 239
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   240 VACFYGGTSYQSQINHIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 319
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 13540304   320 PQTLLFSATCPQWVYKV 336
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
162-342 1.32e-51

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: 178.83  E-value: 1.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRS----PKVLVLAPTRELANQVakdfKDITRK 237
Cdd:cd17967  25 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkayPSALILAPTRELAIQI----YEEARK 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 238 LS------VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHES 311
Cdd:cd17967 101 FSyrsgvrSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVEHP 180
                       170       180       190
                ....*....|....*....|....*....|.
gi 13540304 312 YKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd17967 181 DMPPKGER-QTLMFSATFPREIQRLAADFLK 210
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
568-659 6.71e-49

RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH-II/Gualpha and RH-II/Gubeta, two paralogues found in vertebrates. RH-II/Gualpha, also termed nucleolar RNA helicase 2, or DEAD box protein 21, or nucleolar RNA helicase Gu, is a bifunctional enzyme that displays independent RNA-unwinding and RNA-folding activities. It unwinds double-stranded RNA in the 5' to 3' direction in the presence of Mg2+ through the domains in its N-terminal region. In contrast, it folds single-stranded RNA in an ATP-dependent manner and its C-terminal region is responsible for the Mg2+ independent RNA-foldase activity. RH-II/Gualpha consists of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain (helicase_C), and a GUCT followed by three FRGQR repeats and one PRGQR sequence. The DEAD and helicase_C domains may play critical roles in the RNA-helicase activity of RH-II/Gualpha. The function of GUCT domain remains unclear. The C-terminal region responsible for the RNA-foldase activity does not overlap with the GUCT domain. RH-II/Gubeta, also termed ATP-dependent RNA helicase DDX50, or DEAD box protein 50, or nucleolar protein Gu2, shows significant sequence homology with RH-II/Gualpha. It contains a DEAD domain, a helicase_C domain, and a GUCT domain followed by an arginine-serine-rich sequence but not (F/P)RGQR repeats in RH-II/Gualpha. Both RH-II/Gualpha and RH-II/Gubeta localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity.


Pssm-ID: 240593  Cd Length: 93  Bit Score: 166.86  E-value: 6.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 568 HISGASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAE 647
Cdd:cd12936   1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                        90
                ....*....|...
gi 13540304 648 WHDS-DWILSVPA 659
Cdd:cd12936  81 WHDSrRWQLSVAT 93
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
137-330 1.28e-47

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: 167.48  E-value: 1.28e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 137 GAFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKV-- 214
Cdd:cd17959   1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVga 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 215 --LVLAPTRELANQVAKDFKDITRK--LSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLD 290
Cdd:cd17959  73 raLILSPTRELALQTLKVTKELGKFtdLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 13540304 291 EVDQMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP 330
Cdd:cd17959 153 EADRLFEMGFAEQLHEILSR-----LPENRQTLLFSATLP 187
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
162-491 1.34e-47

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 176.52  E-value: 1.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIER--LQRNQEtIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 238
Cdd:PLN00206 146 PIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGH-PSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLp 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  239 -SVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHesyktdSE 317
Cdd:PLN00206 225 fKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ------AL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  318 DNPQTLLFSATCPQWVYKVAKKYMKSRYeqVDLVGKmTQKAATTVEHLAIQCHWSQRPAVIGDVLQ----------VYSG 387
Cdd:PLN00206 299 SQPQVLLFSATVSPEVEKFASSLAKDII--LISIGN-PNRPNKAVKQLAIWVETKQKKQKLFDILKskqhfkppavVFVS 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  388 SEGRAIIFCETKKNVTEMamnphikqNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQ 467
Cdd:PLN00206 376 SRLGADLLANAITVVTGL--------KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPN 447
                        330       340
                 ....*....|....*....|....
gi 13540304  468 DVESYIHRSGRTGRAGRTGICICF 491
Cdd:PLN00206 448 TIKEYIHQIGRASRMGEKGTAIVF 471
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
362-492 5.24e-47

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 162.68  E-value: 5.24e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 362 VEHLAIQCHWSQRPAVIGdVLQVYSGSEGRAIIFCETKKNVTEMAMN-PHIKQNAQCLHGDIAQSQREITLKGFREGSFK 440
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELlEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13540304 441 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFY 492
Cdd:cd18787  80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
162-345 3.14e-45

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


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 162.83  E-value: 3.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS---RSPKVLVLAPTRELANQVAKDfkdiTRKL 238
Cdd:cd18052  68 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFsevQEPQALIVAPTRELANQIFLE----ARKF 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 239 S-------VACfYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhES 311
Cdd:cd18052 144 SygtcirpVVV-YGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLV-SE 221
                       170       180       190
                ....*....|....*....|....*....|....
gi 13540304 312 YKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRY 345
Cdd:cd18052 222 PGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
DEXDc smart00487
DEAD-like helicases superfamily;
152-342 6.82e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 159.58  E-value: 6.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304    152 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 230
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304    231 FKDITRK--LSVACFYGGTSYQSQINHIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 307
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13540304    308 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:smart00487 154 LKLLPK-----NVQLLLLSATPPEEIENLLELFLN 183
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
162-343 7.14e-45

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: 160.18  E-value: 7.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQR--NQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 238
Cdd:cd17945  15 PIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDGPYALILAPTRELAQQIEEETQKFAKPLg 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 239 -SVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIH----ESYK 313
Cdd:cd17945  95 iRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDampvSNKK 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 13540304 314 TDSEDNP-----------QTLLFSATCPQWVYKVAKKYMKS 343
Cdd:cd17945 175 PDTEEAEklaasgkhryrQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
162-346 1.39e-44

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: 158.62  E-value: 1.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 239
Cdd:cd17940  24 PIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID------PKKDVIQALILVPTRELALQTSQVCKELGKhmGVK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 240 VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 319
Cdd:cd17940  98 VMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPK-----E 172
                       170       180
                ....*....|....*....|....*..
gi 13540304 320 PQTLLFSATCPQWVYKVAKKYMKSRYE 346
Cdd:cd17940 173 RQILLFSATFPLTVKNFMDRHMHNPYE 199
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
149-348 1.46e-44

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 158.69  E-value: 1.46e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 149 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVA 228
Cdd:cd17966   2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN-AQPPLERGDGPIVLVLAPTRELAQQIQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 229 KDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVED 306
Cdd:cd17966  81 QEANKFGGssRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13540304 307 IIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSrYEQV 348
Cdd:cd17966 161 IV-------DQIRPdrQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
163-341 2.27e-44

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: 158.26  E-value: 2.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 163 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSV-- 240
Cdd:cd17939  23 IQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV------RETQALVLAPTRELAQQIQKVVKALGDYMGVkv 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 241 ACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedNP 320
Cdd:cd17939  97 HACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPP-----ET 171
                       170       180
                ....*....|....*....|.
gi 13540304 321 QTLLFSATCPQWVYKVAKKYM 341
Cdd:cd17939 172 QVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
151-328 1.95e-43

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: 155.49  E-value: 1.95e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 151 LLKG---RGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqeTIKKSRSPKVLVLAPTRELANQV 227
Cdd:cd17947   1 LLRAlssLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY---RPKKKAATRVLVLVPTRELAMQC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AK------DFKDITRKLSVacfyGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGF 300
Cdd:cd17947  78 FSvlqqlaQFTDITFALAV----GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                       170       180
                ....*....|....*....|....*...
gi 13540304 301 AEQVEDIIHESYKTDsednpQTLLFSAT 328
Cdd:cd17947 154 ADELKEILRLCPRTR-----QTMLFSAT 176
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
144-346 2.02e-42

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: 153.30  E-value: 2.02e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 144 ISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTREL 223
Cdd:cd17953  19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-DQRPVKPGEGPIGLIMAPTREL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 224 ANQVAKDFKDITRKLS--VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHL--QSGRL-DLSKLRHVVLDEVDQMLDL 298
Cdd:cd17953  98 ALQIYVECKKFSKALGlrVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMFDM 177
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 13540304 299 GFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSRYE 346
Cdd:cd17953 178 GFEPQIMKIV-NNIRPDR----QTVLFSATFPRKVEALARKVLHKPIE 220
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
162-342 2.47e-42

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: 152.36  E-value: 2.47e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LS 239
Cdd:cd17957  15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP----RKKKGLRALILAPTRELASQIYRELLKLSKGtgLR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 240 VACFYGGTSYQSQINHI-RNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIihesYKTDSED 318
Cdd:cd17957  91 IVLLSKSLEAKAKDGPKsITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI----LAACTNP 166
                       170       180
                ....*....|....*....|....
gi 13540304 319 NPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd17957 167 NLQRSLFSATIPSEVEELARSVMK 190
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
163-338 5.66e-41

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: 149.27  E-value: 5.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 163 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRK---LS 239
Cdd:cd17949  17 IQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLLKPfhwIV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 240 VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGFAEQVEDII-------HES 311
Cdd:cd17949  97 PGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKILellddkrSKA 176
                       170       180
                ....*....|....*....|....*...
gi 13540304 312 YKTDSEDNP-QTLLFSATCPQWVYKVAK 338
Cdd:cd17949 177 GGEKSKPSRrQTVLVSATLTDGVKRLAG 204
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
148-338 3.20e-40

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: 146.28  E-value: 3.20e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikKSRSPKVLVLAPTRELANQV 227
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWT--PEDGLGALIISPTRELAMQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AKDFKDITRK--LSVACFYGGTSYQSQINHIrNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQMLDLGFAEQV 304
Cdd:cd17941  79 FEVLRKVGKYhsFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETL 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 13540304 305 EDIIHESYKTDsednpQTLLFSATCPQWVYKVAK 338
Cdd:cd17941 158 DAIVENLPKSR-----QTLLFSATQTKSVKDLAR 186
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
162-342 5.19e-39

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


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 142.99  E-value: 5.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIP-LIERLQrnQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRK-L 238
Cdd:cd17958  15 PIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDL--QPIPREQRnGPGVLVLTPTRELALQIEAECSKYSYKgL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 239 SVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhesykTDSED 318
Cdd:cd17958  93 KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKIL-----LDIRP 167
                       170       180
                ....*....|....*....|....
gi 13540304 319 NPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd17958 168 DRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
139-342 5.35e-39

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 142.97  E-value: 5.35e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLA 218
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS------LKATQALVLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAK------DFKDITrklSVACFyGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:cd18046  75 PTRELAQQIQKvvmalgDYMGIK---CHACI-GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13540304 293 DQMLDLGFAEQvediIHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd18046 151 DEMLSRGFKDQ----IYDIFQKLPPDT-QVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
162-328 2.39e-38

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: 141.57  E-value: 2.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDIT----RK 237
Cdd:cd17961  19 LIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVLEQLTaycrKD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 238 LSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtds 316
Cdd:cd17961  99 VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLPK--- 175
                       170
                ....*....|..
gi 13540304 317 edNPQTLLFSAT 328
Cdd:cd17961 176 --NYQTFLMSAT 185
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
162-338 4.90e-38

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: 140.24  E-value: 4.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 239
Cdd:cd17952  15 PIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-DQRELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKayNLR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 240 VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHEsyktdSEDN 319
Cdd:cd17952  94 VVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH-----VRPD 168
                       170
                ....*....|....*....
gi 13540304 320 PQTLLFSATCPQWVYKVAK 338
Cdd:cd17952 169 RQTLLFSATFKKKIEQLAR 187
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
140-350 2.39e-37

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: 139.76  E-value: 2.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 140 SNFPisEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAP 219
Cdd:cd18049  29 ANFP--ANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLERGDGPICLVLAP 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 220 TRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLD 297
Cdd:cd18049 106 TRELAQQVQQVAAEYGRacRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 185
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13540304 298 LGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSrYEQVDL 350
Cdd:cd18049 186 MGFEPQIRKIV-DQIRPDR----QTLMWSATWPKEVRQLAEDFLKD-YIHINI 232
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
139-328 6.02e-37

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: 137.36  E-value: 6.02e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikkSRSPK---VL 215
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---------SEDPYgifAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 216 VLAPTRELANQVAKDFKDITRKLSVAC--FYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSG---RLDLSKLRHVVLD 290
Cdd:cd17955  72 VLTPTRELAYQIAEQFRALGAPLGLRCcvIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLD 151
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13540304 291 EVDQMLDLGFAEQVEDIIHESYKTdsednPQTLLFSAT 328
Cdd:cd17955 152 EADRLLTGSFEDDLATILSALPPK-----RQTLLFSAT 184
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
100-350 4.02e-36

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: 137.45  E-value: 4.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 100 DIDEYEKKSKRVSSLDTSTHKSSDNKLEETltREQKE------------GAF--SNFPisEETIKLLKGRGVTYLFPIQV 165
Cdd:cd18050  15 DLSELPKFEKNFYVEHPEVARMTQYDVEEL--RRKKEitirgvgcpkpvFAFhqANFP--QYVMDVLLDQNFKEPTPIQC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 166 KTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQV---AKDFKDITRkLSVAC 242
Cdd:cd18050  91 QGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLERGDGPICLVLAPTRELAQQVqqvADDYGKSSR-LKSTC 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 243 FYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhESYKTDSednpQT 322
Cdd:cd18050 169 IYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV-DQIRPDR----QT 243
                       250       260
                ....*....|....*....|....*...
gi 13540304 323 LLFSATCPQWVYKVAKKYMKSrYEQVDL 350
Cdd:cd18050 244 LMWSATWPKEVRQLAEDFLRD-YVQINI 270
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
148-328 6.22e-36

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: 134.41  E-value: 6.22e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 227
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK--FKPRNGTGVIIISPTRELALQI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 228 AKDFKDITRKLSVAC--FYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSK-LRHVVLDEVDQMLDLGFAEQV 304
Cdd:cd17942  79 YGVAKELLKYHSQTFgiVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEM 158
                       170       180
                ....*....|....*....|....
gi 13540304 305 EDIIHESYKTDsednpQTLLFSAT 328
Cdd:cd17942 159 RQIIKLLPKRR-----QTMLFSAT 177
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
148-338 1.68e-35

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: 133.09  E-value: 1.68e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 148 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKsrsPKV--LVLAPTRELAN 225
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKK---GQVgaLIISPTRELAT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 226 Q---VAKDF-KDITRKLSVACFYGGTSYQSQI-NHIRNGIDILVGTPGRIKDHLQS--GRLDLSKLRHVVLDEVDQMLDL 298
Cdd:cd17960  78 QiyeVLQSFlEHHLPKLKCQLLIGGTNVEEDVkKFKRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 13540304 299 GFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAK 338
Cdd:cd17960 158 GFEADLNRILSKLPK-----QRRTGLFSATQTDAVEELIK 192
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
152-343 1.99e-35

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: 132.77  E-value: 1.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 152 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDF 231
Cdd:cd17943   5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLER------RHPQVLILAPTREIAVQIHDVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 232 KDITRK---LSVACFYGGTSYQSQINHIrNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 308
Cdd:cd17943  79 KKIGKKlegLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 13540304 309 HESYKtdsedNPQTLLFSATCPQWVYKVAKKYMKS 343
Cdd:cd17943 158 SSLPK-----NKQVIAFSATYPKNLDNLLARYMRK 187
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
571-665 2.51e-35

GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein family.


Pssm-ID: 462378  Cd Length: 96  Bit Score: 128.81  E-value: 2.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   571 GASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHD 650
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 13540304   651 SD-WILSVPAKLPEIE 665
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
152-342 8.09e-35

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: 131.13  E-value: 8.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 152 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERlqrnqeTIKKSRSPKVLVLAPTRELANQVAKDF 231
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR------CLTEHRNPSALILTPTRELAVQIEDQA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 232 KDITRKL---SVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 308
Cdd:cd17962  79 KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 13540304 309 HesyktDSEDNPQTLLFSATCPQWVYKVAKKYMK 342
Cdd:cd17962 159 E-----NISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
139-338 9.98e-35

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: 131.28  E-value: 9.98e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIkksrspKVLVLA 218
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF------FALVLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAKDFKDI--TRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQM 295
Cdd:cd17954  76 PTRELAQQISEQFEALgsSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRL 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 13540304 296 LDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQwvyKVAK 338
Cdd:cd17954 156 LNMDFEPEIDKILKVIPR-----ERTTYLFSATMTT---KVAK 190
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
162-328 1.37e-34

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: 131.59  E-value: 1.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGP-VYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQET---IKKSRSPKVLVLAPTRELANQVAKDFKDITR- 236
Cdd:cd17946  15 PIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvGGKQKPLRALILTPTRELAVQVKDHLKAIAKy 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 237 -KLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHV---VLDEVDQMLDLG-FAEqVEDIIHES 311
Cdd:cd17946  95 tNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEKGhFAE-LEKILELL 173
                       170
                ....*....|....*....
gi 13540304 312 YKTDSEDNP--QTLLFSAT 328
Cdd:cd17946 174 NKDRAGKKRkrQTFVFSAT 192
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
149-338 1.52e-34

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: 130.54  E-value: 1.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 149 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIerLQRNQETIK----KSRSPKVLVLAPTRELA 224
Cdd:cd17951   2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI--MFALEQEKKlpfiKGEGPYGLIVCPSRELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 225 NQVAKDFKDITRKLS--------VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 296
Cdd:cd17951  80 RQTHEVIEYYCKALQeggypqlrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13540304 297 DLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAK 338
Cdd:cd17951 160 DMGFEEDIRTIF-SYFKGQR----QTLLFSATMPKKIQNFAK 196
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
139-346 7.48e-33

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: 125.92  E-value: 7.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 139 FSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKksrspkVLVLA 218
Cdd:cd17950   4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS------VLVIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 219 PTRELANQVAKDFKDITRKL---SVACFYGGTSYQSQINHIRNGI-DILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQ 294
Cdd:cd17950  78 HTRELAFQISNEYERFSKYMpnvKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13540304 295 ML-DLGFAEQVEDIihesYKTDSEDNpQTLLFSATCPQWVYKVAKKYMKSRYE 346
Cdd:cd17950 158 MLeQLDMRRDVQEI----FRATPHDK-QVMMFSATLSKEIRPVCKKFMQDPLE 205
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
175-342 1.56e-32

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 124.61  E-value: 1.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 175 KDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFY--------GG 246
Cdd:cd17963  34 ENLIAQSQSGTGKTAAFVLAMLSRVDPT------LKSPQALCLAPTRELARQIGEVVEKMGKFTGVKVALavpgndvpRG 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 247 TSYQSQInhirngidiLVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLF 325
Cdd:cd17963 108 KKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRI-----KRMLPRNCQILLF 173
                       170
                ....*....|....*..
gi 13540304 326 SATCPQWVYKVAKKYMK 342
Cdd:cd17963 174 SATFPDSVRKFAEKIAP 190
GUCT cd12929
RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes ...
586-658 1.79e-32

RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes vertebrate RNA helicase II/Gualpha (RH-II/Gualpha) and RNA helicase II/Gubeta (RH-II/Gubeta), both of which consist of a DEAD box helicase domain (DEAD), a helicase conserved C-terminal domain, and a Gu C-terminal (GUCT) domain. They localize to nucleoli, suggesting roles in ribosomal RNA production, but RH-II/Gubeta also localizes to nuclear speckles containing the splicing factor SC35, suggesting its possible involvement in pre-mRNA splicing. In contrast to RH-II/Gualpha, RH-II/Gubeta has RNA-unwinding activity, but no RNA-folding activity. The family also contains plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75), Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins. RH7 is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with the typical GUCT domain found in the RNA helicase II/Gu protein family.


Pssm-ID: 240592  Cd Length: 72  Bit Score: 120.12  E-value: 1.79e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13540304 586 GFVTMTLESLEEIQDVSCAWKELNRKLSSNaVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHDSDWILSVP 658
Cdd:cd12929   1 GWVTYKLEGPRLIQSLSRLVALLKRQLLSN-VSEVGKVAELEGNGGFYFDVRPEARERLQAEPEVAGLRLEVA 72
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
373-483 3.17e-32

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: 120.39  E-value: 3.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   373 QRPAVIGDVLQVYSGseGRAIIFCETKKNVTEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGL 452
Cdd:pfam00271   1 EKLEALLELLKKERG--GKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 13540304   453 DIPEVDLVIQSSPPQDVESYIHRSGRTGRAG 483
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
152-330 6.10e-32

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: 124.02  E-value: 6.10e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 152 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS-RSPKVLVLAPTRELANQVAKD 230
Cdd:cd17948   5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfNAPRGLVITPSRELAEQIGSV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 231 FKDITRKLS--VACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI- 307
Cdd:cd17948  85 AQSLTEGLGlkVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFl 164
                       170       180       190
                ....*....|....*....|....*....|
gi 13540304 308 ----IHESYKTDSEDNP---QTLLFSATCP 330
Cdd:cd17948 165 rrfpLASRRSENTDGLDpgtQLVLVSATMP 194
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
162-341 6.78e-32

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: 124.38  E-value: 6.78e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 162 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRN-------QETIKKSRS---PKVLVLAPTRELANQV---A 228
Cdd:cd18051  46 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpSESGYYGRRkqyPLALVLAPTRELASQIydeA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 229 KDFKdiTRKLSVAC-FYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 307
Cdd:cd18051 126 RKFA--YRSRVRPCvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRI 203
                       170       180       190
                ....*....|....*....|....*....|....
gi 13540304 308 IHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYM 341
Cdd:cd18051 204 VEQDTMPPTGER-QTLMFSATFPKEIQMLARDFL 236
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
163-341 1.14e-31

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 122.19  E-value: 1.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 163 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLierLQRNQETIkksRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC 242
Cdd:cd18045  25 IQQRAIKPIIKGRDVIAQSQSGTGKTATFSISV---LQCLDIQV---RETQALILSPTRELAVQIQKVLLALGDYMNVQC 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 243 F--YGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIihesYKTdSEDNP 320
Cdd:cd18045  99 HacIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDV----YRY-LPPAT 173
                       170       180
                ....*....|....*....|.
gi 13540304 321 QTLLFSATCPQWVYKVAKKYM 341
Cdd:cd18045 174 QVVLVSATLPQDILEMTNKFM 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
149-328 5.23e-31

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: 121.20  E-value: 5.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 149 IKLLKGRGVTYLFPIQVKT---------FGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetiKKSRSPKVLVLAP 219
Cdd:cd17956   2 LKNLQNNGITSAFPVQAAVipwllpsskSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSK-----RVVPRLRALIVVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 220 TRELANQVAKDFKDITR--KLSVAC------FYGGTSYQSQINHIR--NGIDILVGTPGRIKDHLQSGR-LDLSKLRHVV 288
Cdd:cd17956  77 TKELVQQVYKVFESLCKgtGLKVVSlsgqksFKKEQKLLLVDTSGRylSRVDILVATPGRLVDHLNSTPgFTLKHLRFLV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13540304 289 LDEVDQMLDLGF---AEQVEDIIHESYKTD------------SEDNPQTLLFSAT 328
Cdd:cd17956 157 IDEADRLLNQSFqdwLETVMKALGRPTAPDlgsfgdanllerSVRPLQKLLFSAT 211
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
174-343 1.04e-29

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: 116.65  E-value: 1.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 174 GKDLIAQARTGTGKTFSFAIPLIERLQrnqetikksrspkVLVLAPTRELANQVAKDFKDITR-----KLSVACFYGGTS 248
Cdd:cd17938  36 GGDVLMAAETGSGKTGAFCLPVLQIVV-------------ALILEPSRELAEQTYNCIENFKKyldnpKLRVALLIGGVK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 249 YQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYK-TDSEDNPQTLLFSA 327
Cdd:cd17938 103 AREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPKiTSDGKRLQVIVCSA 182
                       170
                ....*....|....*..
gi 13540304 328 TCPQW-VYKVAKKYMKS 343
Cdd:cd17938 183 TLHSFeVKKLADKIMHF 199
HELICc smart00490
helicase superfamily c-terminal domain;
414-483 2.46e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 99.98  E-value: 2.46e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304    414 NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAG 483
Cdd:smart00490  13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
174-328 3.06e-24

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: 99.01  E-value: 3.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 174 GKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQSQ 252
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLL--------LKKGKKVLVLVPTKALALQTAERLRELfGPGIRVAVLVGGSSAEER 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13540304 253 INHIRNGIDILVGTPGRI-KDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsEDNPQTLLFSAT 328
Cdd:cd00046  73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG---LKNAQVILLSAT 146
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
177-345 9.50e-22

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 95.14  E-value: 9.50e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 177 LIAqARTGTGKTFSFAIPLIERLQRNQ-----------ETIKKSRSPKVLVLAPTRELANQVAKDFKDI--TRKLSVACF 243
Cdd:cd17965  65 LLA-AETGSGKTLAYLAPLLDYLKRQEqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLshTVKLGIKTF 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 244 YG--GTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDsednpQ 321
Cdd:cd17965 144 SSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLK-----H 218
                       170       180
                ....*....|....*....|....
gi 13540304 322 TLLFSATCPqwvyKVAKKYMKSRY 345
Cdd:cd17965 219 LILCSATIP----KEFDKTLRKLF 238
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
131-489 2.65e-20

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: 96.06  E-value: 2.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 131 TREQKEGAFSNFP--ISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikk 208
Cdd:COG1205  26 TIPAREARYAPWPdwLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED------ 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 209 sRSPKVLVLAPTRELAN-QVAKdFKDITRKL----SVACFYGGTSyQSQINHIRNGIDILVGTP-----GRIKDHLQSGR 278
Cdd:COG1205 100 -PGATALYLYPTKALARdQLRR-LRELAEALglgvRVATYDGDTP-PEERRWIREHPDIVLTNPdmlhyGLLPHHTRWAR 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 279 LdLSKLRHVVLDE-----------VDQMLD--LGFAEQvediihesYKTDsednPQTLLFSATcpqwvykVAkkymksry 345
Cdd:COG1205 177 F-FRNLRYVVIDEahtyrgvfgshVANVLRrlRRICRH--------YGSD----PQFILASAT-------IG-------- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 346 EQVDLVGKMTQKAATTVE---------HLAIqchWsqRPAVIGDVLQVYSGSEG------------RAIIFCETKKNV-- 402
Cdd:COG1205 229 NPAEHAERLTGRPVTVVDedgsprgerTFVL---W--NPPLVDDGIRRSALAEAarlladlvreglRTLVFTRSRRGAel 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 403 -----TEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSG 477
Cdd:COG1205 304 laryaRRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAG 383
                       410
                ....*....|..
gi 13540304 478 RTGRAGRTGICI 489
Cdd:COG1205 384 RAGRRGQDSLVV 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
146-490 1.41e-16

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 83.41  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 146 EETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikksrsPKVLVLAPTRELA 224
Cdd:COG1204   9 EKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG---------GKALYIVPLRALA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 225 NQVAKDFKDITRKL--SVACFYGGtsYQSQINHIRNGiDILVGTPGRIkDHLQSGRLD-LSKLRHVVLDEVdQMLDlgfA 301
Cdd:COG1204  80 SEKYREFKRDFEELgiKVGVSTGD--YDSDDEWLGRY-DILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-HLID---D 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 302 EQ----VEDIIheSYKTDSEDNPQTLLFSATCP------QWvykVAKKYMKSRYEQVDL-VGKMTQKAAttvehlaiqcH 370
Cdd:COG1204 152 ESrgptLEVLL--ARLRRLNPEAQIVALSATIGnaeeiaEW---LDAELVKSDWRPVPLnEGVLYDGVL----------R 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 371 WSQRPAVIGDVLQVY----SGSEGRAIIFCETKKNVTEMA------MNPHIKQN-------------------------A 415
Cdd:COG1204 217 FDDGSRRSKDPTLALaldlLEEGGQVLVFVSSRRDAESLAkkladeLKRRLTPEereeleelaeellevseethtneklA 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 416 QCL-------HGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPeVDLVIqssppqdVESYiHRSGRT--------- 479
Cdd:COG1204 297 DCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVI-------IRDT-KRGGMVpipvlefkq 367
                       410       420
                ....*....|....*....|
gi 13540304 480 --GRAGRTG-------ICIC 490
Cdd:COG1204 368 maGRAGRPGydpygeaILVA 387
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
173-478 3.56e-16

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 82.38  E-value: 3.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 173 EGKDLIAQARTGTGKTFsFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKditRKLSVACFYGGtsyqsq 252
Cdd:COG1061  99 GGGRGLVVAPTGTGKTV-LALALAAELLRGK---------RVLVLVPRRELLEQWAEELR---RFLGDPLAGGG------ 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 253 inHIRNGIDILVGTPGRIKDHLQSGRLDlSKLRHVVLDEVdqmldlgfaeqvediiH----ESYKT--DSEDNPQTLLFS 326
Cdd:COG1061 160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEA----------------HhagaPSYRRilEAFPAAYRLGLT 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 327 ATcP-----QWVYkvAKKYMKSRYE--------------------QVDLVGKMTQKAATTVEHLAIQCHWSQR-PAVIGD 380
Cdd:COG1061 221 AT-PfrsdgREIL--LFLFDGIVYEyslkeaiedgylappeyygiRVDLTDERAEYDALSERLREALAADAERkDKILRE 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 381 VLQVYsGSEGRAIIFCETKKNVTEMA-MNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDL 459
Cdd:COG1061 298 LLREH-PDDRKTLVFCSSVDHAEALAeLLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
                       330
                ....*....|....*....
gi 13540304 460 VIQSSPPQDVESYIHRSGR 478
Cdd:COG1061 377 AILLRPTGSPREFIQRLGR 395
GUCT_RH7_like cd12937
RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar ...
578-662 1.07e-15

RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH7 and similar proteins. RH7, also termed plant RNA helicase 75 (PRH75), is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. RH7 is RNA specific and harbors two possible RNA-binding motifs, the helicase motif VI (HRIGRTGR) and the C-terminal glycine-rich GYR domain.


Pssm-ID: 240594  Cd Length: 86  Bit Score: 72.60  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 578 RSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHDSDWI-LS 656
Cdd:cd12937   1 RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSAWVDKRGVtLE 80

                ....*.
gi 13540304 657 VPAKLP 662
Cdd:cd12937  81 VATELP 86
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
175-339 2.31e-14

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: 73.13  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 175 KDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKdfkdITRKLSVACFYGGTSYQSQIN 254
Cdd:cd18048  58 QNLIAQSQSGTGKTAAFVLAMLSRVDALK------LYPQCLCLSPTFELALQTGK----VVEEMGKFCVGIQVIYAIRGN 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 255 HIRNGID----ILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLFSAT 328
Cdd:cd18048 128 RPGKGTDieaqIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMINVqGHSDHSVRV-----KRSMPKECQMLLFSAT 202
                       170
                ....*....|.
gi 13540304 329 CPQWVYKVAKK 339
Cdd:cd18048 203 FEDSVWAFAER 213
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
389-492 2.99e-14

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 69.93  E-value: 2.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 389 EGRAIIFCETKKNVTEMAMnpHIKQN---AQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSP 465
Cdd:cd18794  30 GGSGIIYCLSRKECEQVAA--RLQSKgisAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSL 107
                        90       100
                ....*....|....*....|....*..
gi 13540304 466 PQDVESYIHRSGRTGRAGRTGICICFY 492
Cdd:cd18794 108 PKSMESYYQESGRAGRDGLPSECILFY 134
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
389-483 1.99e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.00  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 389 EGRAIIFCE---TKKNVTEMAMNPHIK------QNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDL 459
Cdd:COG1111 353 DSRIIVFTQyrdTAEMIVEFLSEPGIKagrfvgQASKEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432
                        90       100
                ....*....|....*....|....*..
gi 13540304 460 VIQSSPpqdVES---YIHRSGRTGRAG 483
Cdd:COG1111 433 VIFYEP---VPSeirSIQRKGRTGRKR 456
PRK13766 PRK13766
Hef nuclease; Provisional
391-489 1.10e-12

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 71.44  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  391 RAIIFCE---TKKNVTEMAMNPHIK------QNAQclHGDIAQSQRE--ITLKGFREGSFKVLVATNVAARGLDIPEVDL 459
Cdd:PRK13766 367 RIIVFTQyrdTAEKIVDLLEKEGIKavrfvgQASK--DGDKGMSQKEqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                         90       100       110
                 ....*....|....*....|....*....|.
gi 13540304  460 VIQSSP-PQDVESyIHRSGRTGRaGRTGICI 489
Cdd:PRK13766 445 VIFYEPvPSEIRS-IQRKGRTGR-QEEGRVV 473
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
159-331 1.79e-12

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 66.52  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 159 YLFPIQVKTFGPVY-EGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrsPKVLVLAPTRELANQVAKDFKDITRK 237
Cdd:cd17921   1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSG--------GKAVYIAPTRALVNQKEADLRERFGP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 238 L--SVACFYGGTSyqSQINHIRNGiDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVdQMLDLG-FAEQVEDIIheSYK 313
Cdd:cd17921  73 LgkNVGLLTGDPS--VNKLLLAEA-DILVATPEKLDLLLrNGGERLIQDVRLVVVDEA-HLIGDGeRGVVLELLL--SRL 146
                       170
                ....*....|....*...
gi 13540304 314 TDSEDNPQTLLFSATCPQ 331
Cdd:cd17921 147 LRINKNARFVGLSATLPN 164
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
380-482 3.18e-12

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 64.53  E-value: 3.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 380 DVLQVYSGSEG--RAIIFCETKknVTEMAMNPHIKQNAQCLHG------------------DIAQSQREITLKGFREGSF 439
Cdd:cd18802  14 EILREYFPKTPdfRGIIFVERR--ATAVVLSRLLKEHPSTLAFircgfligrgnssqrkrsLMTQRKQKETLDKFRDGEL 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13540304 440 KVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRtGRA 482
Cdd:cd18802  92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
387-486 3.56e-12

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


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 64.30  E-value: 3.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 387 GSEGRAIIFCETKKNVTEMA-----MNPHIK-------QNAQCLHGdIAQSQREITLKGFREGSFKVLVATNVAARGLDI 454
Cdd:cd18801  28 GSDTRVIIFSEFRDSAEEIVnflskIRPGIRatrfigqASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDI 106
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13540304 455 PEVDLVI----QSSPPQdvesYIHRSGRTGRaGRTG 486
Cdd:cd18801 107 GEVDLIIcydaSPSPIR----MIQRMGRTGR-KRQG 137
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
438-492 1.31e-10

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 57.71  E-value: 1.31e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13540304 438 SFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAG-RTGICICFY 492
Cdd:cd18785  22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
419-481 2.25e-10

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 59.59  E-value: 2.25e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13540304 419 HGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGR 481
Cdd:cd18796  75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
390-484 5.50e-10

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 58.41  E-value: 5.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 390 GRAIIFCETKKNVTEMAmnphIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQ-SSPPQD 468
Cdd:cd18789  50 DKIIVFTDNVEALYRYA----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQiSGHGGS 125
                        90
                ....*....|....*.
gi 13540304 469 VESYIHRSGRTGRAGR 484
Cdd:cd18789 126 RRQEAQRLGRILRPKK 141
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
164-291 6.13e-10

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: 59.14  E-value: 6.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 164 QVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrspKVLVLAPTRELANQVAKDFKDITR----KLS 239
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-------RALYLYPTKALAQDQLRSLRELLEqlglGIR 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13540304 240 VACFYGGTSYQSQINHIRNGIDILVGTP-----GRIKDHLQSGRLdLSKLRHVVLDE 291
Cdd:cd17923  78 VATYDGDTPREERRAIIRNPPRILLTNPdmlhyALLPHHDRWARF-LRNLRYVVLDE 133
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
393-502 2.60e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 60.15  E-value: 2.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 393 IIFCETKKNVTEMAmnPHIKQN---AQCLHGDIAQSQREITLKGFREGSFKVLVATNvaARGL--DIPEVDLVIQSSPPQ 467
Cdd:COG0514 234 IVYCLSRKKVEELA--EWLREAgirAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFGMgiDKPDVRFVIHYDLPK 309
                        90       100       110
                ....*....|....*....|....*....|....*
gi 13540304 468 DVESYIHRSGRTGRAGRTGICICFYQPRERGQLRY 502
Cdd:COG0514 310 SIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRF 344
PRK00254 PRK00254
ski2-like helicase; Provisional
143-478 2.61e-08

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 57.52  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  143 PISEETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetikksRSPKVLVLAPTR 221
Cdd:PRK00254   7 RVDERIKRVLKERGIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR--------EGGKAVYLVPLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  222 ELANQVAKDFKDITR-KLSVACFYGgtSYQSQINHIrNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGF 300
Cdd:PRK00254  79 ALAEEKYREFKDWEKlGLRVAMTTG--DYDSTDEWL-GKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  301 AEQVEDIIhesykTDSEDNPQTLLFSATC------PQWvykVAKKYMKSRYEQVDLVGKMTQKAATTVEHLAIQCHWSQR 374
Cdd:PRK00254 156 GATLEMIL-----THMLGRAQILGLSATVgnaeelAEW---LNAELVVSDWRPVKLRKGVFYQGFLFWEDGKIERFPNSW 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  375 PAVIGDVLQVYSGsegrAIIFCETKKNVTEMAM---------------------------NPHIKQNAQCLHGDIA---- 423
Cdd:PRK00254 228 ESLVYDAVKKGKG----ALVFVNTRRSAEKEALelakkikrfltkpelralkeladsleeNPTNEKLKKALRGGVAfhha 303
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13540304  424 ---QSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSS-----------PPQDVESYIHRSGR 478
Cdd:PRK00254 304 glgRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTkrysnfgwediPVLEIQQMMGRAGR 372
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
175-292 3.04e-08

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


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 54.58  E-value: 3.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 175 KDLIAQARTGTGKTFsFAIPLIERLQRnqETIKKSRSPKVLV-LAPTRELANQVAKDFKDITrKLSVACFYGGTSYQSQI 253
Cdd:cd18034  17 RNTIVVLPTGSGKTL-IAVMLIKEMGE--LNRKEKNPKKRAVfLVPTVPLVAQQAEAIRSHT-DLKVGEYSGEMGVDKWT 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 13540304 254 NHIRNG----IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:cd18034  93 KERWKEelekYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
ResIII pfam04851
Type III restriction enzyme, res subunit;
175-292 3.40e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 53.44  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   175 KDLIAQARTGTGKTF-SFAIplIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC-FYGGTSYqsq 252
Cdd:pfam04851  24 KRGLIVMATGSGKTLtAAKL--IARL------FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGeIISGDKK--- 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 13540304   253 iNHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVL--DEV 292
Cdd:pfam04851  93 -DESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEA 133
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
181-500 4.91e-08

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 56.86  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   181 ARTGTGKTFSFAIPLIERLQRNQ----ETIKKSRSPKVLVLAPTRELANQVAKDFK--------------DITRKLSVAC 242
Cdd:PRK09751    3 APTGSGKTLAAFLYALDRLFREGgedtREAHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderrrrgETEVNLRVGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   243 FYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQS-GRLDLSKLRHVVLDEVDQM--------LDLGFaEQVEDIIHESyk 313
Cdd:PRK09751   83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLTSrARETLRGVETVIIDEVHAVagskrgahLALSL-ERLDALLHTS-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   314 tdsednPQTLLFSATCpQWVYKVAK-----------KYMKSRYEQVDLV---GKMTQKAATTVEHlAIQCH-------WS 372
Cdd:PRK09751  160 ------AQRIGLSATV-RSASDVAAflggdrpvtvvNPPAMRHPQIRIVvpvANMDDVSSVASGT-GEDSHagregsiWP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   373 QRPAVIGDvlQVYSGsegRAIIFCETKKNVTE-------------MAMNPHIKQN----------------------AQC 417
Cdd:PRK09751  232 YIETGILD--EVLRH---RSTIVFTNSRGLAEkltarlnelyaarLQRSPSIAVDaahfestsgatsnrvqssdvfiARS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   418 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTG-RAGrtGICICFYQPRE 496
Cdd:PRK09751  307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPRT 384

                  ....
gi 13540304   497 RGQL 500
Cdd:PRK09751  385 RRDL 388
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
164-291 5.89e-08

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 53.59  E-value: 5.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 164 QVKTFGPVYEGKDLIAQARTGTGKTFsFAIPLIERLQRNqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LSVA 241
Cdd:cd17927   7 QLELAQPALKGKNTIICLPTGSGKTF-VAVLICEHHLKK---FPAGRKGKVVFLANKVPLVEQQKEVFRKHFERpgYKVT 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13540304 242 CFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 291
Cdd:cd17927  83 GLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDE 133
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
175-339 9.34e-08

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: 53.19  E-value: 9.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 175 KDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRklsvacFYGGTS--YQSQ 252
Cdd:cd18047  41 QNLIAQSQSGTGKTAAFVLAMLSQVE------PANKYPQCLCLSPTYELALQTGKVIEQMGK------FYPELKlaYAVR 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 253 INHIRNGI----DILVGTPGRIKDH-LQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIIHESYKtdsedNPQTLLFS 326
Cdd:cd18047 109 GNKLERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPR-----NCQMLLFS 183
                       170
                ....*....|...
gi 13540304 327 ATCPQWVYKVAKK 339
Cdd:cd18047 184 ATFEDSVWKFAQK 196
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
123-297 1.35e-07

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 55.28  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 123 DNKLEETLTR---------EQKEGAFSNFPISEETIKLLKGRGvTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFA 192
Cdd:COG1202 165 SGRLDPDLTKfdeisattdEVDTVPVDDLDLPPELKDLLEGRG-EELLPVQSLAVeNGLLEGKDQLVVSATATGKTLIGE 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 193 IPLIERLQRNQEtikksrspKVLVLAPTRELANQVAKDFKDITRK-LSVACFYGgtsyQSQI-----NHIRNGiDILVGT 266
Cdd:COG1202 244 LAGIKNALEGKG--------KMLFLVPLVALANQKYEDFKDRYGDgLDVSIRVG----ASRIrddgtRFDPNA-DIIVGT 310
                       170       180       190
                ....*....|....*....|....*....|..
gi 13540304 267 PGRIkDH-LQSGRlDLSKLRHVVLDEVdQMLD 297
Cdd:COG1202 311 YEGI-DHaLRTGR-DLGDIGTVVIDEV-HMLE 339
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
183-292 7.52e-07

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: 49.23  E-value: 7.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 183 TGTGKTFsFAIPLIERLqrnqetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGtsyqsqINHIRNGIDI 262
Cdd:cd17926  27 TGSGKTL-TALALIAYL----------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG------KKKDFDDANV 89
                        90       100       110
                ....*....|....*....|....*....|
gi 13540304 263 LVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:cd17926  90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
160-292 1.40e-06

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


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 49.78  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 160 LFPIQVKTFGPVYEGKDLIAQARTGTGKTFSfAIPLIER-LQRNQETIKKSRspkVLVLAPTRELANQVA-KDFKDITRK 237
Cdd:cd18036   3 LRNYQLELVLPALRGKNTIICAPTGSGKTRV-AVYICRHhLEKRRSAGEKGR---VVVLVNKVPLVEQQLeKFFKYFRKG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13540304 238 LSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSG----RLDLSKLRHVVLDEV 292
Cdd:cd18036  79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDEC 137
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
177-233 2.95e-06

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 50.61  E-value: 2.95e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13540304 177 LIAQArTGTGKTFSfAIPLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKD 233
Cdd:COG4096 182 LLVMA-TGTGKTRT-AIALIYRL------LKAGRAKRILFLADRNALVDQAKNAFKP 230
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
384-461 2.99e-06

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 46.78  E-value: 2.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 384 VYSGSEGRAIIFCETKKNVTEMA-----MNPhikqNAQCLHGDIAQSQRE---ITLKGFREGSFKVLVATNVAARGLDIP 455
Cdd:cd18799   1 PYKYVEIKTLIFCVSIEHAEFMAeafneAGI----DAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIP 76

                ....*.
gi 13540304 456 EVDLVI 461
Cdd:cd18799  77 EVDNVV 82
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
173-291 3.89e-06

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


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 47.89  E-value: 3.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 173 EGKDLIAqARTGTGKTFSFAIPLIERLQRnqetiKKSrspKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQS 251
Cdd:cd18035  16 NGNTLIV-LPTGLGKTIIAILVAADRLTK-----KGG---KVLILAPSRPLVEQHAENLKRVlNIPDKITSLTGEVKPEE 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13540304 252 QINHIRNGiDILVGTPGRIKDHLQSGRLDLSKLRHVVLDE 291
Cdd:cd18035  87 RAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDE 125
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
393-501 3.96e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 50.10  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304  393 IIFCETKKNVTEMA---MNPHIKQNAqcLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDV 469
Cdd:PRK11057 240 IIYCNSRAKVEDTAarlQSRGISAAA--YHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
                         90       100       110
                 ....*....|....*....|....*....|..
gi 13540304  470 ESYIHRSGRTGRAGRTGICICFYQPRERGQLR 501
Cdd:PRK11057 318 ESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
GUCT_Hera cd12938
RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase ...
577-647 4.68e-06

RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) and similar proteins; This subfamily corresponds to the Gu C-terminal (GUCT)-like domain of Hera and similar proteins. Thermus thermophilus Hera is a DEAD box helicase that binds fragments of 23S rRNA and RNase P RNA via its C-terminal domain. It contains a helicase core that harbors two RecA-like domains termed RecA_N and RecA_C, a dimerization domain (DD), and a C-terminal RNA-binding domain (RBD) that reveals a compact, RRM-like fold and shows sequence similarity with GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA helicase II/Gubeta (RH-II/Gubeta) and plant DEAD-box ATP-dependent RNA helicase 7 (RH7 or PRH75).


Pssm-ID: 240595  Cd Length: 74  Bit Score: 44.98  E-value: 4.68e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13540304 577 PRSLITSDKGFVTMTL--ESLEEIQDVSCAWKELNRKLSSNavsqITRMCLLKGNMGVCFDVPTTESERLQAE 647
Cdd:cd12938   1 PRSLLTGEEGWTTLQLtgSRLLPPGSVRRAVGLLSRAAADG----VGKIRILADAGGAVFDLPEEIAKELLAK 69
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
391-484 5.10e-06

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 47.24  E-value: 5.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 391 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 466
Cdd:cd18790  29 RVLVTTLTKRmaeDLTEYLQELGVK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 104
                        90       100
                ....*....|....*....|...
gi 13540304 467 qDVESYIhRSGRT-----GRAGR 484
Cdd:cd18790 105 -DKEGFL-RSETSliqtiGRAAR 125
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
160-500 8.58e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 49.33  E-value: 8.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 160 LFPIQVKTFGPVYEGKD-LIAqARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANqvakdfkDITRKL 238
Cdd:COG1201  25 PTPPQREAWPAIAAGEStLLI-APTGSGKTLAAFLPALDELARRPRPGELPDGLRVLYISPLKALAN-------DIERNL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 239 SVACFYGGTSYQSQINHIRNGI------------------DILVGTPGRIkdHL----QSGRLDLSKLRHVVLDEV---- 292
Cdd:COG1201  97 RAPLEEIGEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTPESL--ALlltsPDARELLRGVRTVIVDEIhala 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 293 -----DQ-MLDLgfaEQVEDIihesyktdSEDNPQTLLFSATC--PQwvyKVAkkymksRYeqvdLVGKMTQKAATTVE- 363
Cdd:COG1201 175 gskrgVHlALSL---ERLRAL--------APRPLQRIGLSATVgpLE---EVA------RF----LVGYEDPRPVTIVDa 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 364 ------HLAIQChwsqrPAVIGDVLQVYSGSEGRA---------------IIFCETKKnVTEM------AMNPHIKQNAQ 416
Cdd:COG1201 231 gagkkpDLEVLV-----PVEDLIERFPWAGHLWPHlyprvldlieahrttLVFTNTRS-QAERlfqrlnELNPEDALPIA 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 417 CLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQ-SSPPQdVESYIHRSGRTG-RAGRT--GICIcfy 492
Cdd:COG1201 305 AHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQvGSPKS-VARLLQRIGRAGhRVGEVskGRLV--- 380

                ....*...
gi 13540304 493 qPRERGQL 500
Cdd:COG1201 381 -PTHRDEL 387
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
391-484 1.12e-05

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 45.71  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 391 RAIIFCETKKNVTEM-----AMNPHIKQNAQCLH----GDIAQSQREITlKGFREGSFKVLVATNVAARGLDIPEVDLVI 461
Cdd:cd18797  37 KTIVFCRSRKLAELLlrylkARLVEEGPLASKVAsyraGYLAEDRREIE-AELFNGELLGVVATNALELGIDIGGLDAVV 115
                        90       100
                ....*....|....*....|...
gi 13540304 462 QSSPPQDVESYIHRSGRTGRAGR 484
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGK 138
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
174-297 2.48e-05

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: 45.27  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 174 GKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrSPKVLVLAPTRELANQVAKDFK----DITRKLSVACFYGGTSY 249
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-----GVQVLYISPLKALINDQERRLEepldEIDLEIPVAVRHGDTSQ 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13540304 250 QSQINHIRNGIDILVGTPGRIKDHLQSGRLD--LSKLRHVVLDEVDQMLD 297
Cdd:cd17922  76 SEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALLG 125
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
418-501 2.93e-05

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 44.64  E-value: 2.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 418 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICICFYQPR- 495
Cdd:cd18810  57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQlRGRVGRSKERAYAYFLYPDQk 136

                ....*....
gi 13540304 496 ---ERGQLR 501
Cdd:cd18810 137 kltEDALKR 145
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
418-501 3.66e-05

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 44.57  E-value: 3.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 418 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICICFYQPR- 495
Cdd:cd18792  66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQlRGRVGRGKHQSYCYLLYPDPk 145

                ....*....
gi 13540304 496 ---ERGQLR 501
Cdd:cd18792 146 kltETAKKR 154
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
177-292 4.16e-05

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


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 44.47  E-value: 4.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 177 LIAQArTGTGKTFSfAIPLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSvACFYGGTSYQSQinhi 256
Cdd:cd18032  24 LLVMA-TGTGKTYT-AAFLIKRL------LEANRKKRILFLAHREELLEQAERSFKEVLPDGS-FGNLKGGKKKPD---- 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13540304 257 rnGIDILVGT----PGRIKDHLQS-GRLDLsklrhVVLDEV 292
Cdd:cd18032  91 --DARVVFATvqtlNKRKRLEKFPpDYFDL-----IIIDEA 124
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
393-492 5.28e-05

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 46.81  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   393 IIFCETK---KNVTEMAMnpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDV 469
Cdd:PLN03137  684 IIYCLSRmdcEKVAERLQ--EFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
                          90       100
                  ....*....|....*....|...
gi 13540304   470 ESYIHRSGRTGRAGRTGICICFY 492
Cdd:PLN03137  762 EGYHQECGRAGRDGQRSSCVLYY 784
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
391-484 6.03e-05

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 46.52  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   391 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 466
Cdd:TIGR00631 444 RVLVTTLTKKmaeDLTDYLKELGIK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 519
                          90       100
                  ....*....|....*....|...
gi 13540304   467 qDVESYIhRSGRT-----GRAGR 484
Cdd:TIGR00631 520 -DKEGFL-RSERSliqtiGRAAR 540
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
173-238 1.80e-04

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 44.92  E-value: 1.80e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13540304 173 EGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrspKVLVLAPTRELANQ-VAKDFKDITRKL 238
Cdd:COG1199  32 EGRHLLIEAGTGTGKTLAYLVPALLAARETGK--------KVVISTATKALQEQlVEKDLPLLRKAL 90
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
431-506 2.73e-04

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 42.29  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 431 LKGFREGSFKVLVAT----NVAARGLDIPE-VDLVIQSSPPqdVESYIHRSGRTGR--AGR--TGICICFYQPRE----- 496
Cdd:cd18798  65 LEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPElfeal 142
                        90
                ....*....|..
gi 13540304 497 --RGQLRYVEQK 506
Cdd:cd18798 143 kkRLKLILDEFI 154
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
204-290 2.74e-04

U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.


Pssm-ID: 373164  Cd Length: 250  Bit Score: 43.31  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304   204 ETIKKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGG-TSYQSQINHIR-NGIDILVGTPGRIKDHLQSGRLD 280
Cdd:pfam14617 117 QRPKSNGSPHTLVLTIAALRAADVLRPLKKLqTKGFKVAKLFAKhIKLEEHITYCKaSRIGIGVGTPGRIADLLENESLS 196
                          90
                  ....*....|
gi 13540304   281 LSKLRHVVLD 290
Cdd:pfam14617 197 VDNLKYIILD 206
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
159-292 3.83e-04

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: 41.94  E-value: 3.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 159 YLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRK 237
Cdd:cd18028   1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---------KALYLVPLRALASEKYEEFKKLEEI 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13540304 238 -LSVACFYGgtSYQSQINHIRNgIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 292
Cdd:cd18028  72 gLKVGISTG--DYDEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEI 124
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
176-328 4.32e-04

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: 42.02  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 176 DLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSYQsqinh 255
Cdd:cd17918  38 DRLLSGDVGSGKTLVALGAALLAYKNGK---------QVAILVPTEILAHQHYEEARKFLPFINVELVTGGTKAQ----- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 256 IRNGIDILVGTpgrikdhlqsgrldlsklrHVVLDEVDQMLDLGFAeqvedIIHESYKTDSED--------NPQTLLFSA 327
Cdd:cd17918 104 ILSGISLLVGT-------------------HALLHLDVKFKNLDLV-----IVDEQHRFGVAQrealynlgATHFLEATA 159

                .
gi 13540304 328 T 328
Cdd:cd17918 160 T 160
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
418-494 4.94e-04

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 41.18  E-value: 4.94e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13540304 418 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICICFYQP 494
Cdd:cd18811  67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQlRGRVGRGDHQSYCLLVYKD 144
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
392-487 6.14e-04

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 41.00  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 392 AIIFCETKKNVTEMAMN-----PHikqnaqclHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPeVDLVIqsspp 466
Cdd:cd18795  46 VLVFCSSRKECEKTAKDlagiaFH--------HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVI----- 111
                        90       100       110
                ....*....|....*....|....*....|....
gi 13540304 467 qdVESYIHRSGRT-------------GRAGRTGI 487
Cdd:cd18795 112 --IKGTQRYDGKGyrelspleylqmiGRAGRPGF 143
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
170-291 7.44e-04

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 41.34  E-value: 7.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 170 PVYEGKDLIAQARTGTGKTF-SFAIplierLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL--SVACFYGG 246
Cdd:cd18073  13 PAMKGKNTIICAPTGCGKTFvSLLI-----CEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHgyRVTGISGA 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13540304 247 TSYQSQINHIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 291
Cdd:cd18073  88 TAENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
418-460 1.87e-03

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 41.57  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13540304  418 LHGDIAQSQR-EItLKGFREGSFKVLVATNVAARGLDIPEVDLV 460
Cdd:PRK05298 476 LHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
417-492 2.24e-03

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 39.44  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 417 CLHGDIAQS-QREI---TLKGFRegsfKVLVATNVAARGLDIPEVDLVIqssppqD-----VESYIHRSG---------- 477
Cdd:cd18791  79 PLHSSLPPEeQQRVfepPPPGVR----KVVLATNIAETSITIPGVVYVI------DsglvkEKVYDPRTGlsslvtvwis 148
                        90       100
                ....*....|....*....|...
gi 13540304 478 ------RTGRAGRT--GICICFY 492
Cdd:cd18791 149 kasaeqRAGRAGRTrpGKCYRLY 171
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
418-460 2.39e-03

Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 41.15  E-value: 2.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 13540304 418 LHGDIAQSQR-EItLKGFREGSFKVLVATNVAARGLDIPEVDLV 460
Cdd:COG0556 473 LHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDLPEVSLV 515
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
441-486 4.02e-03

C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved 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: 350171 [Multi-domain]  Cd Length: 59  Bit Score: 36.37  E-value: 4.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 13540304 441 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTG 486
Cdd:cd09300   8 VLIAVN*ALTGFDAPELNTIIVDKNLRSYRGLNQAFGRANRIYTFG 53
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
163-292 5.59e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 38.88  E-value: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13540304 163 IQVKTFGPVYEG-KDLIAQARTGTGKT--FSFAIplierLQRNQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRKL 238
Cdd:cd18023   5 IQSEVFPDLLYSdKNFVVSAPTGSGKTvlFELAI-----LRLLKERNPLPWgNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13540304 239 SVAC--FYGGTSYQSqINHIRNgIDILVGTPG-------RIKDHlqsGRLdLSKLRHVVLDEV 292
Cdd:cd18023  80 GLSCaeLTGDTEMDD-TFEIQD-ADIILTTPEkwdsmtrRWRDN---GNL-VQLVALVLIDEV 136
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
183-233 6.94e-03

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 39.65  E-value: 6.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13540304  183 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 233
Cdd:PRK05298  41 TGSGKTFTMA-NVIARLQR-----------PTLVLAHNKTLAAQLYSEFKE 79
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
183-233 7.47e-03

DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like 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: 350674 [Multi-domain]  Cd Length: 299  Bit Score: 39.11  E-value: 7.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 13540304 183 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 233
Cdd:cd17916  37 TGSGKTFTIA-NVIAQVNK-----------PTLVIAHNKTLAAQLYSEFKE 75
 
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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