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Conserved domains on  [gi|1720362776|ref|XP_030101267|]
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ATP-dependent RNA helicase DDX50 isoform X2 [Mus musculus]

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];
71-458 1.88e-148

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.27  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 150
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:COG0513    79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 229 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 308
Cdd:COG0513   159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 309 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 382
Cdd:COG0513   231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362776 383 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 458
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 ...
500-591 4.30e-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: 166.47  E-value: 4.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 500 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 579
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                          90
                  ....*....|...
gi 1720362776 580 WHDS-DWILSVPA 591
Cdd:cd12936    81 WHDSrRWQLSVAT 93
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
71-458 1.88e-148

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.27  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 150
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:COG0513    79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 229 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 308
Cdd:COG0513   159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 309 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 382
Cdd:COG0513   231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362776 383 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 458
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 ...
80-281 7.13e-143

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: 414.24  E-value: 7.13e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 159
Cdd:cd17944     1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AKDFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 239
Cdd:cd17944    81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720362776 240 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 281
Cdd:cd17944   161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
70-450 3.98e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 290.55  E-value: 3.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  70 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 149
Cdd:PRK11776    5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 150 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:PRK11776   79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 225 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 303
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 304 SQRPAVIGDVLQVYSGSEgrAIIFCETKKNVTEMA--MNpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 381
Cdd:PRK11776  227 DERLPALQRLLLHHQPES--CVVFCNTKKECQEVAdaLN-AQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362776 382 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 450
Cdd:PRK11776  304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
94-268 3.47e-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: 3.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 171
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTSYQSQINQIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 251
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 1720362776 252 PQTLLFSATCPQWVYKV 268
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 ...
500-591 4.30e-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: 166.47  E-value: 4.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 500 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 579
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                          90
                  ....*....|...
gi 1720362776 580 WHDS-DWILSVPA 591
Cdd:cd12936    81 WHDSrRWQLSVAT 93
DEXDc smart00487
DEAD-like helicases superfamily;
84-274 1.99e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.35  E-value: 1.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776   84 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 162
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  163 FKDITRK--LSVACFYGGTSYQSQINQIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 239
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720362776  240 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 274
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 ...
503-597 2.00e-36

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: 131.51  E-value: 2.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 503 GASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHD 582
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 1720362776 583 SD-WILSVPAKLPEIE 597
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
323-416 4.54e-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: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 323 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 398
Cdd:TIGR00631 444 RVLVTTLTKKmaeDLTDYLKELGIK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 519
                          90       100
                  ....*....|....*....|...
gi 1720362776 399 qDVESYIhRSGRT-----GRAGR 416
Cdd:TIGR00631 520 -DKEGFL-RSERSliqtiGRAAR 540
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
71-458 1.88e-148

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 437.27  E-value: 1.88e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 150
Cdd:COG0513     4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:COG0513    79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 229 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 308
Cdd:COG0513   159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 309 VIGDVLQVYSgsEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 382
Cdd:COG0513   231 LLRRLLRDED--PERAIVFCNTKRGADRLA-----EKlqkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362776 383 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 458
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 ...
80-281 7.13e-143

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: 414.24  E-value: 7.13e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 159
Cdd:cd17944     1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AKDFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 239
Cdd:cd17944    81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720362776 240 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 281
Cdd:cd17944   161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
70-450 3.98e-91

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 290.55  E-value: 3.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  70 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 149
Cdd:PRK11776    5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 150 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:PRK11776   79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 225 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 303
Cdd:PRK11776  157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 304 SQRPAVIGDVLQVYSGSEgrAIIFCETKKNVTEMA--MNpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 381
Cdd:PRK11776  227 DERLPALQRLLLHHQPES--CVVFCNTKKECQEVAdaLN-AQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362776 382 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 450
Cdd:PRK11776  304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
80-274 1.34e-86

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


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 269.31  E-value: 1.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 159
Cdd:cd00268     1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVE 237
Cdd:cd00268    79 AEVARKLGKgtGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720362776 238 DIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd00268   159 KILSALPK-----DRQTLLFSATLPEEVKELAKKFLK 190
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
68-450 2.95e-79

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 264.40  E-value: 2.95e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  68 EGAFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVL 147
Cdd:PRK11634    5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD------PELKAPQIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 148 VLAPTRELANQVAK---DFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:PRK11634   79 VLAPTRELAVQVAEamtDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 225 DQMLDLGFAEQVEDIIHESyktdsEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQvdlvgkMTQKAATTVEHLAiQCHWS 304
Cdd:PRK11634  159 DEMLRMGFIEDVETIMAQI-----PEGHQTALFSATMPEAIRRITRRFMKEPQEV------RIQSSVTTRPDIS-QSYWT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 305 QRPAVIGDVLQVYSGSEG--RAIIFCETKKNVTEMAMN-PHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA 381
Cdd:PRK11634  227 VWGMRKNEALVRFLEAEDfdAAIIFVRTKNATLEVAEAlERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362776 382 RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 450
Cdd:PRK11634  307 RGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPN 375
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
60-440 7.15e-69

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 232.50  E-value: 7.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  60 ETLTREQKEGA--FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnQET 137
Cdd:PRK01297   76 EDFVVEPQEGKtrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLL--QTP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 138 IKKSR---SPKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIR-NGIDILVGTPGRIKDHLQSGRL 211
Cdd:PRK01297  154 PPKERymgEPRALIIAPTRELVVQIAKDAAALTKytGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEV 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 212 DLSKLRHVVLDEVDQMLDLGFAEQVEDIIHEsykTDSEDNPQTLLFSATCPQWVYKVAKKYMksrYEQVDLVGKMTQKAA 291
Cdd:PRK01297  234 HLDMVEVMVLDEADRMLDMGFIPQVRQIIRQ---TPRKEERQTLLFSATFTDDVMNLAKQWT---TDPAIVEIEPENVAS 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 292 TTVEHLAIQCHWSQRPAVIGDVlqVYSGSEGRAIIFCETKKNVTEMamNPHIKQ---NAQCLHGDIAQSQREITLKGFRE 368
Cdd:PRK01297  308 DTVEQHVYAVAGSDKYKLLYNL--VTQNPWERVMVFANRKDEVRRI--EERLVKdgiNAAQLSGDVPQHKRIKTLEGFRE 383
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362776 369 GSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAG 440
Cdd:PRK01297  384 GKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLG 455
PTZ00110 PTZ00110
helicase; Provisional
81-426 3.66e-68

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 232.36  E-value: 3.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  81 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqRNQETIKKSRSPKVLVLAPTRELANQV- 159
Cdd:PTZ00110  142 LKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI-NAQPLLRYGDGPIVLVLAPTRELAEQIr 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 --AKDFKDITrKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVE 237
Cdd:PTZ00110  221 eqCNKFGASS-KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 238 DIIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSRYEQVDlVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVLQ 315
Cdd:PTZ00110  300 KIV-------SQIRPdrQTLMWSATWPKEVQSLARDLCKEEPVHVN-VGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQ 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 316 VYSGSEGRAIIFCETKKN----VTEMAMN--PhikqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEV 389
Cdd:PTZ00110  372 RIMRDGDKILIFVETKKGadflTKELRLDgwP-----ALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720362776 390 DLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQP 426
Cdd:PTZ00110  447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
71-438 1.38e-66

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 225.21  E-value: 1.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQ---RnqetiKKSRSPKVL 147
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfpR-----RKSGPPRIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 148 VLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVD 225
Cdd:PRK11192   78 ILTPTRELAMQVADQARELAKhtHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 226 QMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP-QWVYKVAKKYMK---------SRYEQvdlvGKMTQ--KAATT 293
Cdd:PRK11192  158 RMLDMGFAQDIETIAAE-----TRWRKQTLLFSATLEgDAVQDFAERLLNdpveveaepSRRER----KKIHQwyYRADD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 294 VEH-LAIQCHWSQRPAVigdvlqvysgseGRAIIFCETKKNVTEMAMNPHiKQNAQC--LHGDIAQSQREITLKGFREGS 370
Cdd:PRK11192  229 LEHkTALLCHLLKQPEV------------TRSIVFVRTRERVHELAGWLR-KAGINCcyLEGEMVQAKRNEAIKRLTDGR 295
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362776 371 FKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQL----RYVEQK 438
Cdd:PRK11192  296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLgkieRYIEEP 367
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
65-423 5.84e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 220.61  E-value: 5.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  65 EQKegaFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL-QRNQETIKKSRS 143
Cdd:PRK04837    7 EQK---FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlSHPAPEDRKVNQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 144 PKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVL 221
Cdd:PRK04837   84 PRALIMAPTRELAVQIHADAEPLAQatGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 222 DEVDQMLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKS-RYEQVDlvgkMTQKAATTV-EHL-- 297
Cdd:PRK04837  164 DEADRMFDLGF---IKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVE----PEQKTGHRIkEELfy 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 298 ------------AIQCHWSQrpavigdvlqvysgsegRAIIFCETKKNVTE----MAMNPHikqNAQCLHGDIAQSQREI 361
Cdd:PRK04837  237 psneekmrllqtLIEEEWPD-----------------RAIIFANTKHRCEEiwghLAADGH---RVGLLTGDVAQKKRLR 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362776 362 TLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCF 423
Cdd:PRK04837  297 ILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
76-281 9.52e-60

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: 199.35  E-value: 9.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  76 ISEETIKLLKGRGVTYLFPIQVKTFGPVYE-GKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSpKVLVLAPTRE 154
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGV-SALIISPTRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 155 LANQVAKDFKDIT---RKLSVACFYGGTSYQSQINQI-RNGIDILVGTPGRIKDHL--QSGRLDLSKLRHVVLDEVDQML 228
Cdd:cd17964    80 LALQIAAEAKKLLqglRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 229 DLGFAEQVEDIIhESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 281
Cdd:cd17964   160 DMGFRPDLEQIL-RHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
PTZ00424 PTZ00424
helicase 45; Provisional
95-437 1.99e-59

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 205.06  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  95 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC 174
Cdd:PTZ00424   54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD------LNACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 175 F--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQvediIHESYKTDSEDnP 252
Cdd:PTZ00424  128 HacVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQ----IYDVFKKLPPD-V 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 253 QTLLFSATCPQWVYKVAKKYMKsryeqvDLVGKMTQKAATTVE-----HLAIQCHwSQRPAVIGDVLQVYSGSEgrAIIF 327
Cdd:PTZ00424  203 QVALFSATMPNEILELTTKFMR------DPKRILVKKDELTLEgirqfYVAVEKE-EWKFDTLCDLYETLTITQ--AIIY 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 328 CETKKNVTEMAMNPHIKQ-NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIH 406
Cdd:PTZ00424  274 CNTRRKVDYLTKKMHERDfTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIH 353
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720362776 407 RSGRTGRAGRTGICVCFYQPRERGQLRYVEQ 437
Cdd:PTZ00424  354 RIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
71-438 3.69e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 203.26  E-value: 3.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL-QRNQETIKKSRSPKVLVL 149
Cdd:PRK04537   11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlSRPALADRKPEDPRALIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 150 APTRELANQVAKDFKDITRKLSV--ACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQ 226
Cdd:PRK04537   91 APTRELAIQIHKDAVKFGADLGLrfALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEADR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 227 MLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKsryEQVDLVGKMTQKAATTVEHlaiQCHWSQR 306
Cdd:PRK04537  171 MFDLGF---IKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMN---EPEKLVVETETITAARVRQ---RIYFPAD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 307 PAVIGDVLQVYSGSEG-RAIIFCETKKNVTEMAMNphIKQNAQ---CLHGDIAQSQREITLKGFREGSFKVLVATNVAAR 382
Cdd:PRK04537  242 EEKQTLLLGLLSRSEGaRTMVFVNTKAFVERVART--LERHGYrvgVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 383 GLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQL----RYVEQK 438
Cdd:PRK04537  320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLpdieAYIEQK 379
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
70-449 4.90e-55

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 194.64  E-value: 4.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  70 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVL 149
Cdd:PRK10590    2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 150 APTRELANQVAKDFKDITRKLSVACF--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQM 227
Cdd:PRK10590   82 TPTRELAAQIGENVRDYSKYLNIRSLvvFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 228 LDLGFaeqvediIHESYKTDSEDNP--QTLLFSATCPQWVYKVAKKYMKSRyEQVDLVgkmtqKAATTVEHLAIQCHWSQ 305
Cdd:PRK10590  162 LDMGF-------IHDIRRVLAKLPAkrQNLLFSATFSDDIKALAEKLLHNP-LEIEVA-----RRNTASEQVTQHVHFVD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 306 R-------PAVIGDvlqvysGSEGRAIIFCETKKNVTEMAmnphiKQ------NAQCLHGDIAQSQREITLKGFREGSFK 372
Cdd:PRK10590  229 KkrkrellSQMIGK------GNWQQVLVFTRTKHGANHLA-----EQlnkdgiRSAAIHGNKSQGARTRALADFKSGDIR 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 373 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTG-----ICVcfyqpRERGQLRYVEQKAGITFKRVG 447
Cdd:PRK10590  298 VLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGealslVCV-----DEHKLLRDIEKLLKKEIPRIA 372

                  ..
gi 1720362776 448 VP 449
Cdd:PRK10590  373 IP 374
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
94-274 9.08e-53

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 181.15  E-value: 9.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRS----PKVLVLAPTRELANQVakdfKDITRK 169
Cdd:cd17967    25 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkayPSALILAPTRELAIQI----YEEARK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 170 LS------VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHES 243
Cdd:cd17967   101 FSyrsgvrSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVEHP 180
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720362776 244 YKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd17967   181 DMPPKGER-QTLMFSATFPREIQRLAADFLK 210
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
94-268 3.47e-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: 3.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 171
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTSYQSQINQIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 251
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 1720362776 252 PQTLLFSATCPQWVYKV 268
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 ...
500-591 4.30e-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: 166.47  E-value: 4.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 500 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 579
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                          90
                  ....*....|...
gi 1720362776 580 WHDS-DWILSVPA 591
Cdd:cd12936    81 WHDSrRWQLSVAT 93
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
69-262 2.39e-48

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: 168.64  E-value: 2.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  69 GAFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKV-- 146
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVga 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 147 --LVLAPTRELANQVAKDFKDITRK--LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLD 222
Cdd:cd17959    73 raLILSPTRELALQTLKVTKELGKFtdLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720362776 223 EVDQMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP 262
Cdd:cd17959   153 EADRLFEMGFAEQLHEILSR-----LPENRQTLLFSATLP 187
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
94-423 1.39e-47

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 175.36  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIER--LQRNQEtIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 170
Cdd:PLN00206  146 PIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGH-PSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLp 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 -SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHesyktdSE 249
Cdd:PLN00206  225 fKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ------AL 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 250 DNPQTLLFSATCPQWVYKVAKKYMKSRYeqVDLVGKmTQKAATTVEHLAIQCHWSQRPAVIGDVLQ----------VYSG 319
Cdd:PLN00206  299 SQPQVLLFSATVSPEVEKFASSLAKDII--LISIGN-PNRPNKAVKQLAIWVETKQKKQKLFDILKskqhfkppavVFVS 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 320 SEGRAIIFCETKKNVTEMamnphikqNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQ 399
Cdd:PLN00206  376 SRLGADLLANAITVVTGL--------KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPN 447
                         330       340
                  ....*....|....*....|....
gi 1720362776 400 DVESYIHRSGRTGRAGRTGICVCF 423
Cdd:PLN00206  448 TIKEYIHQIGRASRMGEKGTAIVF 471
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
294-424 1.35e-46

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: 161.14  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 294 VEHLAIQCHWSQRPAVIGdVLQVYSGSEGRAIIFCETKKNVTEMAMN-PHIKQNAQCLHGDIAQSQREITLKGFREGSFK 372
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELlEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720362776 373 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICVCFY 424
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 ...
94-277 1.55e-46

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


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 165.53  E-value: 1.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS---RSPKVLVLAPTRELANQVAKDfkdiTRKL 170
Cdd:cd18052    68 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFsevQEPQALIVAPTRELANQIFLE----ARKF 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 S-------VACfYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhES 243
Cdd:cd18052   144 SygtcirpVVV-YGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLV-SE 221
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720362776 244 YKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRY 277
Cdd:cd18052   222 PGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
DEXDc smart00487
DEAD-like helicases superfamily;
84-274 1.99e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 160.35  E-value: 1.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776   84 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 162
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  163 FKDITRK--LSVACFYGGTSYQSQINQIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 239
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720362776  240 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 274
Cdd:smart00487 154 LKLLPK-----NVQLLLLSATPPEEIENLLELFLN 183
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
81-280 3.68e-45

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


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 159.46  E-value: 3.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  81 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVA 160
Cdd:cd17966     2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN-AQPPLERGDGPIVLVLAPTRELAQQIQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 161 KDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVED 238
Cdd:cd17966    81 QEANKFGGssRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720362776 239 IIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSrYEQV 280
Cdd:cd17966   161 IV-------DQIRPdrQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
94-278 4.77e-45

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: 159.39  E-value: 4.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 171
Cdd:cd17940    24 PIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID------PKKDVIQALILVPTRELALQTSQVCKELGKhmGVK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 251
Cdd:cd17940    98 VMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPK-----E 172
                         170       180
                  ....*....|....*....|....*..
gi 1720362776 252 PQTLLFSATCPQWVYKVAKKYMKSRYE 278
Cdd:cd17940   173 RQILLFSATFPLTVKNFMDRHMHNPYE 199
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
94-275 5.51e-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: 159.79  E-value: 5.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQR--NQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 170
Cdd:cd17945    15 PIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDGPYALILAPTRELAQQIEEETQKFAKPLg 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 -SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIH----ESYK 245
Cdd:cd17945    95 iRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDampvSNKK 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720362776 246 TDSEDNP-----------QTLLFSATCPQWVYKVAKKYMKS 275
Cdd:cd17945   175 PDTEEAEklaasgkhryrQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
95-273 1.32e-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: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  95 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSV-- 172
Cdd:cd17939    23 IQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV------RETQALVLAPTRELAQQIQKVVKALGDYMGVkv 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 173 ACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedNP 252
Cdd:cd17939    97 HACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPP-----ET 171
                         170       180
                  ....*....|....*....|.
gi 1720362776 253 QTLLFSATCPQWVYKVAKKYM 273
Cdd:cd17939   172 QVVLFSATMPHEVLEVTKKFM 192
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
83-260 6.88e-44

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: 155.88  E-value: 6.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  83 LLKG---RGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqeTIKKSRSPKVLVLAPTRELANQV 159
Cdd:cd17947     1 LLRAlssLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY---RPKKKAATRVLVLVPTRELAMQC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AK------DFKDITRKLSVacfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGF 232
Cdd:cd17947    78 FSvlqqlaQFTDITFALAV----GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                         170       180
                  ....*....|....*....|....*...
gi 1720362776 233 AEQVEDIIHESYKTDsednpQTLLFSAT 260
Cdd:cd17947   154 ADELKEILRLCPRTR-----QTMLFSAT 176
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
94-274 5.50e-43

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: 153.51  E-value: 5.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LS 171
Cdd:cd17957    15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP----RKKKGLRALILAPTRELASQIYRELLKLSKGtgLR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTS-YQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIihesYKTDSED 250
Cdd:cd17957    91 IVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI----LAACTNP 166
                         170       180
                  ....*....|....*....|....
gi 1720362776 251 NPQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd17957   167 NLQRSLFSATIPSEVEELARSVMK 190
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
76-278 8.15e-43

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: 154.07  E-value: 8.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  76 ISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTREL 155
Cdd:cd17953    19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-DQRPVKPGEGPIGLIMAPTREL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 156 ANQVAKDFKDITRKLS--VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHL--QSGRL-DLSKLRHVVLDEVDQMLDL 230
Cdd:cd17953    98 ALQIYVECKKFSKALGlrVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMFDM 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720362776 231 GFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSRYE 278
Cdd:cd17953   178 GFEPQIMKIV-NNIRPDR----QTVLFSATFPRKVEALARKVLHKPIE 220
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
95-270 1.34e-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: 150.43  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  95 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRK---LS 171
Cdd:cd17949    17 IQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLLKPfhwIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGFAEQVEDII-------HES 243
Cdd:cd17949    97 PGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKILellddkrSKA 176
                         170       180
                  ....*....|....*....|....*...
gi 1720362776 244 YKTDSEDNP-QTLLFSATCPQWVYKVAK 270
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 ...
80-270 1.29e-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: 147.05  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikKSRSPKVLVLAPTRELANQV 159
Cdd:cd17941     1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWT--PEDGLGALIISPTRELAMQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AKDFKDITRK--LSVACFYGGTSYQSQINQIrNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQMLDLGFAEQV 236
Cdd:cd17941    79 FEVLRKVGKYhsFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETL 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720362776 237 EDIIHESYKTDsednpQTLLFSATCPQWVYKVAK 270
Cdd:cd17941   158 DAIVENLPKSR-----QTLLFSATQTKSVKDLAR 186
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
71-274 2.22e-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: 143.74  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLA 150
Cdd:cd18046     1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS------LKATQALVLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAK------DFKDITrklSVACFyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:cd18046    75 PTRELAQQIQKvvmalgDYMGIK---CHACI-GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720362776 225 DQMLDLGFAEQvediIHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd18046   151 DEMLSRGFKDQ----IYDIFQKLPPDT-QVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
94-274 2.85e-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: 143.37  E-value: 2.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIP-LIERLQrnQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRK-L 170
Cdd:cd17958    15 PIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDL--QPIPREQRnGPGVLVLTPTRELALQIEAECSKYSYKgL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhesykTDSED 250
Cdd:cd17958    93 KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKIL-----LDIRP 167
                         170       180
                  ....*....|....*....|....
gi 1720362776 251 NPQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd17958   168 DRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
94-260 3.33e-39

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: 143.49  E-value: 3.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDIT----RK 169
Cdd:cd17961    19 LIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVLEQLTaycrKD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 170 LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtds 248
Cdd:cd17961    99 VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLPK--- 175
                         170
                  ....*....|..
gi 1720362776 249 edNPQTLLFSAT 260
Cdd:cd17961   176 --NYQTFLMSAT 185
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
94-270 3.81e-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: 3.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 171
Cdd:cd17952    15 PIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-DQRELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKayNLR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 172 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHEsyktdSEDN 251
Cdd:cd17952    94 VVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH-----VRPD 168
                         170
                  ....*....|....*....
gi 1720362776 252 PQTLLFSATCPQWVYKVAK 270
Cdd:cd17952   169 RQTLLFSATFKKKIEQLAR 187
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
71-260 6.03e-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: 136.97  E-value: 6.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikkSRSPK---VL 147
Cdd:cd17955     1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---------SEDPYgifAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 148 VLAPTRELANQVAKDFKDITRKLSVAC--FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSG---RLDLSKLRHVVLD 222
Cdd:cd17955    72 VLTPTRELAYQIAEQFRALGAPLGLRCcvIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLD 151
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720362776 223 EVDQMLDLGFAEQVEDIIHESYKTdsednPQTLLFSAT 260
Cdd:cd17955   152 EADRLLTGSFEDDLATILSALPPK-----RQTLLFSAT 184
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
71-282 7.03e-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: 137.83  E-value: 7.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLA 150
Cdd:cd18049    26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLERGDGPICLVLA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:cd18049   105 PTRELAQQVQQVAAEYGRacRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720362776 229 DLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSrYEQVDL 282
Cdd:cd18049   185 DMGFEPQIRKIV-DQIRPDR----QTLMWSATWPKEVRQLAEDFLKD-YIHINI 232
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
503-597 2.00e-36

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: 131.51  E-value: 2.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 503 GASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHD 582
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 1720362776 583 SD-WILSVPAKLPEIE 597
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
80-260 2.56e-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: 135.18  E-value: 2.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 159
Cdd:cd17942     1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK--FKPRNGTGVIIISPTRELALQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 160 AKDFKDITRKLSVAC--FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSK-LRHVVLDEVDQMLDLGFAEQV 236
Cdd:cd17942    79 YGVAKELLKYHSQTFgiVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEM 158
                         170       180
                  ....*....|....*....|....
gi 1720362776 237 EDIIHESYKTDsednpQTLLFSAT 260
Cdd:cd17942   159 RQIIKLLPKRR-----QTMLFSAT 177
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
94-282 7.44e-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: 136.29  E-value: 7.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQV---AKDFKDITRkL 170
Cdd:cd18050    87 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLERGDGPICLVLAPTRELAQQVqqvADDYGKSSR-L 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhESYKTDSed 250
Cdd:cd18050   165 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV-DQIRPDR-- 241
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720362776 251 npQTLLFSATCPQWVYKVAKKYMKSrYEQVDL 282
Cdd:cd18050   242 --QTLMWSATWPKEVRQLAEDFLRD-YVQINI 270
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
71-270 8.92e-36

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: 133.60  E-value: 8.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIkksrspKVLVLA 150
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF------FALVLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDI--TRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQM 227
Cdd:cd17954    76 PTRELAQQISEQFEALgsSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720362776 228 LDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQwvyKVAK 270
Cdd:cd17954   156 LNMDFEPEIDKILKVIPR-----ERTTYLFSATMTT---KVAK 190
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
80-270 9.10e-36

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: 133.47  E-value: 9.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  80 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKsrsPKV--LVLAPTRELAN 157
Cdd:cd17960     1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKK---GQVgaLIISPTRELAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 158 Q---VAKDF-KDITRKLSVACFYGGTSYQSQINQI-RNGIDILVGTPGRIKDHLQS--GRLDLSKLRHVVLDEVDQMLDL 230
Cdd:cd17960    78 QiyeVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720362776 231 GFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAK 270
Cdd:cd17960   158 GFEADLNRILSKLPK-----QRRTGLFSATQTDAVEELIK 192
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
94-260 1.57e-35

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: 133.90  E-value: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGP-VYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQET---IKKSRSPKVLVLAPTRELANQVAKDFKDITR- 168
Cdd:cd17946    15 PIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvGGKQKPLRALILTPTRELAVQVKDHLKAIAKy 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 169 -KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHV---VLDEVDQMLDLG-FAEqVEDIIHES 243
Cdd:cd17946    95 tNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEKGhFAE-LEKILELL 173
                         170
                  ....*....|....*....
gi 1720362776 244 YKTDSEDNP--QTLLFSAT 260
Cdd:cd17946   174 NKDRAGKKRkrQTFVFSAT 192
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
84-275 5.02e-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: 131.23  E-value: 5.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  84 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDF 163
Cdd:cd17943     5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLER------RHPQVLILAPTREIAVQIHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 164 KDITRK---LSVACFYGGTSYQSQINQIrNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 240
Cdd:cd17943    79 KKIGKKlegLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720362776 241 HESYKtdsedNPQTLLFSATCPQWVYKVAKKYMKS 275
Cdd:cd17943   158 SSLPK-----NKQVIAFSATYPKNLDNLLARYMRK 187
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
84-274 6.73e-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: 6.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  84 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERlqrnqeTIKKSRSPKVLVLAPTRELANQVAKDF 163
Cdd:cd17962     5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR------CLTEHRNPSALILTPTRELAVQIEDQA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 164 KDITRKL---SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 240
Cdd:cd17962    79 KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720362776 241 HesyktDSEDNPQTLLFSATCPQWVYKVAKKYMK 274
Cdd:cd17962   159 E-----NISHDHQTILVSATIPRGIEQLAGQLLQ 187
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
81-270 1.30e-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: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  81 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIerLQRNQETIK----KSRSPKVLVLAPTRELA 156
Cdd:cd17951     2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI--MFALEQEKKlpfiKGEGPYGLIVCPSRELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 157 NQVAKDFKDITRKLS--------VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:cd17951    80 RQTHEVIEYYCKALQeggypqlrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720362776 229 DLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAK 270
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 ...
71-278 1.59e-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: 127.46  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKksrspkVLVLA 150
Cdd:cd17950     4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS------VLVIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITRKL---SVACFYGGTSYQSQINQIRNGI-DILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQ 226
Cdd:cd17950    78 HTRELAFQISNEYERFSKYMpnvKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 227 ML-DLGFAEQVEDIihesYKTDSEDNpQTLLFSATCPQWVYKVAKKYMKSRYE 278
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 ...
107-274 1.22e-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: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 107 KDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYggtSYQSQIN 186
Cdd:cd17963    34 ENLIAQSQSGTGKTAAFVLAMLSRVDPT------LKSPQALCLAPTRELARQIGEVVEKMGKFTGVKVAL---AVPGNDV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 187 QIRNGID--ILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLFSATCPQ 263
Cdd:cd17963   105 PRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRI-----KRMLPRNCQILLFSATFPD 179
                         170
                  ....*....|.
gi 1720362776 264 WVYKVAKKYMK 274
Cdd:cd17963   180 SVRKFAEKIAP 190
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
71-273 2.82e-32

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: 123.73  E-value: 2.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  71 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLierLQRNQETIkksRSPKVLVLA 150
Cdd:cd18045     1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISV---LQCLDIQV---RETQALILS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 151 PTRELANQVAKDFKDITRKLSVACF--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 228
Cdd:cd18045    75 PTRELAVQIQKVLLALGDYMNVQCHacIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720362776 229 DLGFAEQVEDIihesYKTdSEDNPQTLLFSATCPQWVYKVAKKYM 273
Cdd:cd18045   155 NKGFKEQIYDV----YRY-LPPATQVVLVSATLPQDILEMTNKFM 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
305-415 3.01e-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: 3.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 305 QRPAVIGDVLQVYSGseGRAIIFCETKKNVTEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGL 384
Cdd:pfam00271   1 EKLEALLELLKKERG--GKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720362776 385 DIPEVDLVIQSSPPQDVESYIHRSGRTGRAG 415
Cdd:pfam00271  79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
GUCT cd12929
RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes ...
518-590 3.26e-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: 118.97  E-value: 3.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 518 GFVTMTLESPEEIQDVSCAWKELNRKLSSNaVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWILSVP 590
Cdd:cd12929     1 GWVTYKLEGPRLIQSLSRLVALLKRQLLSN-VSEVGKVAELEGNGGFYFDVRPEARERLQAEPEVAGLRLEVA 72
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
94-273 3.94e-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: 124.77  E-value: 3.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  94 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRN-------QETIKKSRS---PKVLVLAPTRELANQV---A 160
Cdd:cd18051    46 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpSESGYYGRRkqyPLALVLAPTRELASQIydeA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 161 KDFKdiTRKLSVAC-FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 239
Cdd:cd18051   126 RKFA--YRSRVRPCvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRI 203
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720362776 240 IHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYM 273
Cdd:cd18051   204 VEQDTMPPTGER-QTLMFSATFPKEIQMLARDFL 236
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
84-262 4.17e-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: 124.40  E-value: 4.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  84 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS-RSPKVLVLAPTRELANQVAKD 162
Cdd:cd17948     5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfNAPRGLVITPSRELAEQIGSV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 163 FKDITRKLS--VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI- 239
Cdd:cd17948    85 AQSLTEGLGlkVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFl 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1720362776 240 ----IHESYKTDSEDNP---QTLLFSATCP 262
Cdd:cd17948   165 rrfpLASRRSENTDGLDpgtQLVLVSATMP 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
81-260 3.43e-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: 121.59  E-value: 3.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  81 IKLLKGRGVTYLFPIQVKT---------FGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetiKKSRSPKVLVLAP 151
Cdd:cd17956     2 LKNLQNNGITSAFPVQAAVipwllpsskSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSK-----RVVPRLRALIVVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 152 TRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNG--------IDILVGTPGRIKDHLQSGR-LDLSKLRHVV 220
Cdd:cd17956    77 TKELVQQVYKVFESLCKgtGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720362776 221 LDEVDQMLDLGF---AEQVEDIIHESYKTD------------SEDNPQTLLFSAT 260
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 ...
106-275 1.61e-30

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: 118.96  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 106 GKDLIAQARTGTGKTFSFAIPLIERLQrnqetikksrspkVLVLAPTRELANQVAKDFKDITR-----KLSVACFYGGTS 180
Cdd:cd17938    36 GGDVLMAAETGSGKTGAFCLPVLQIVV-------------ALILEPSRELAEQTYNCIENFKKyldnpKLRVALLIGGVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 181 YQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYK-TDSEDNPQTLLFSA 259
Cdd:cd17938   103 AREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPKiTSDGKRLQVIVCSA 182
                         170
                  ....*....|....*..
gi 1720362776 260 TCPQW-VYKVAKKYMKS 275
Cdd:cd17938   183 TLHSFeVKKLADKIMHF 199
HELICc smart00490
helicase superfamily c-terminal domain;
346-415 2.76e-25

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 99.59  E-value: 2.76e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  346 NAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAG 415
Cdd:smart00490  13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
106-260 2.54e-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: 99.40  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 106 GKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQSQ 184
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLL--------LKKGKKVLVLVPTKALALQTAERLRELfGPGIRVAVLVGGSSAEER 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362776 185 INQIRNGIDILVGTPGRI-KDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsEDNPQTLLFSAT 260
Cdd:cd00046    73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG---LKNAQVILLSAT 146
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
109-277 5.75e-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: 95.52  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 109 LIAqARTGTGKTFSFAIPLIERLQRNQ-----------ETIKKSRSPKVLVLAPTRELANQVAKDFKDI--TRKLSVACF 175
Cdd:cd17965    65 LLA-AETGSGKTLAYLAPLLDYLKRQEqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLshTVKLGIKTF 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 176 YG--GTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDsednpQ 253
Cdd:cd17965   144 SSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLK-----H 218
                         170       180
                  ....*....|....*....|....
gi 1720362776 254 TLLFSATCPqwvyKVAKKYMKSRY 277
Cdd:cd17965   219 LILCSATIP----KEFDKTLRKLF 238
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
63-421 8.67e-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: 94.13  E-value: 8.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  63 TREQKEGAFSNF--SISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikk 140
Cdd:COG1205    26 TIPAREARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED------ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 141 sRSPKVLVLAPTRELAN-QVAKdFKDITRKL----SVACFYGGTSyQSQINQIRNGIDILVGTP-----GRIKDHLQSGR 210
Cdd:COG1205   100 -PGATALYLYPTKALARdQLRR-LRELAEALglgvRVATYDGDTP-PEERRWIREHPDIVLTNPdmlhyGLLPHHTRWAR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 211 LdLSKLRHVVLDE-----------VDQMLD--LGFAEQvediihesYKTDsednPQTLLFSATcpqwvykVAkkymksry 277
Cdd:COG1205   177 F-FRNLRYVVIDEahtyrgvfgshVANVLRrlRRICRH--------YGSD----PQFILASAT-------IG-------- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 278 EQVDLVGKMTQKAATTVE---------HLAIqchWsqRPAVIGDVLQVYSGSEG------------RAIIFCETKKNV-- 334
Cdd:COG1205   229 NPAEHAERLTGRPVTVVDedgsprgerTFVL---W--NPPLVDDGIRRSALAEAarlladlvreglRTLVFTRSRRGAel 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 335 -----TEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSG 409
Cdd:COG1205   304 laryaRRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAG 383
                         410
                  ....*....|..
gi 1720362776 410 RTGRAGRTGICV 421
Cdd:COG1205   384 RAGRRGQDSLVV 395
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
78-422 4.60e-17

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 84.56  E-value: 4.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  78 EETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikksrsPKVLVLAPTRELA 156
Cdd:COG1204     9 EKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG---------GKALYIVPLRALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 157 NQVAKDFKDITRKL--SVACFYGGtsYQSQINQIRNGiDILVGTPGRIkDHLQSGRLD-LSKLRHVVLDEVdQMLDlgfA 233
Cdd:COG1204    80 SEKYREFKRDFEELgiKVGVSTGD--YDSDDEWLGRY-DILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-HLID---D 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 234 EQ----VEDIIheSYKTDSEDNPQTLLFSATCP------QWvykVAKKYMKSRYEQVDL-VGKMTQKAAttvehlaiqcH 302
Cdd:COG1204   152 ESrgptLEVLL--ARLRRLNPEAQIVALSATIGnaeeiaEW---LDAELVKSDWRPVPLnEGVLYDGVL----------R 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 303 WSQRPAVIGDVLQVY----SGSEGRAIIFCETKKNVTEMA------MNPHIKQN-------------------------A 347
Cdd:COG1204   217 FDDGSRRSKDPTLALaldlLEEGGQVLVFVSSRRDAESLAkkladeLKRRLTPEereeleelaeellevseethtneklA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 348 QCL-------HGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPeVDLVIqssppqdVESYiHRSGRT--------- 411
Cdd:COG1204   297 DCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVI-------IRDT-KRGGMVpipvlefkq 367
                         410       420
                  ....*....|....*....|
gi 1720362776 412 --GRAGRTG-------ICVC 422
Cdd:COG1204   368 maGRAGRPGydpygeaILVA 387
GUCT_RH7_like cd12937
RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar ...
510-594 9.46e-17

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: 75.68  E-value: 9.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 510 RSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWI-LS 588
Cdd:cd12937     1 RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSAWVDKRGVtLE 80

                  ....*.
gi 1720362776 589 VPAKLP 594
Cdd:cd12937    81 VATELP 86
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
105-410 3.17e-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: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 105 EGKDLIAQARTGTGKTFsFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKditRKLSVACFYGGtsyqsq 184
Cdd:COG1061    99 GGGRGLVVAPTGTGKTV-LALALAAELLRGK---------RVLVLVPRRELLEQWAEELR---RFLGDPLAGGG------ 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 185 inQIRNGIDILVGTPGRIKDHLQSGRLDlSKLRHVVLDEVdqmldlgfaeqvediiH----ESYKT--DSEDNPQTLLFS 258
Cdd:COG1061   160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEA----------------HhagaPSYRRilEAFPAAYRLGLT 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 259 ATcP-----QWVYkvAKKYMKSRYE--------------------QVDLVGKMTQKAATTVEHLAIQCHWSQR-PAVIGD 312
Cdd:COG1061   221 AT-PfrsdgREIL--LFLFDGIVYEyslkeaiedgylappeyygiRVDLTDERAEYDALSERLREALAADAERkDKILRE 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 313 VLQVYsGSEGRAIIFCETKKNVTEMA-MNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDL 391
Cdd:COG1061   298 LLREH-PDDRKTLVFCSSVDHAEALAeLLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
                         330
                  ....*....|....*....
gi 1720362776 392 VIQSSPPQDVESYIHRSGR 410
Cdd:COG1061   377 AILLRPTGSPREFIQRLGR 395
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
107-271 1.35e-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: 73.52  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 107 KDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKdfkdITRKLSVACFYGGTSYQSQIN 186
Cdd:cd18048    58 QNLIAQSQSGTGKTAAFVLAMLSRVDALK------LYPQCLCLSPTFELALQTGK----VVEEMGKFCVGIQVIYAIRGN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 187 QIRNGID----ILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLFSAT 260
Cdd:cd18048   128 RPGKGTDieaqIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMINVqGHSDHSVRV-----KRSMPKECQMLLFSAT 202
                         170
                  ....*....|.
gi 1720362776 261 CPQWVYKVAKK 271
Cdd:cd18048   203 FEDSVWAFAER 213
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
321-415 1.06e-13

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 74.38  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 321 EGRAIIFCE---TKKNVTEMAMNPHIK------QNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDL 391
Cdd:COG1111   353 DSRIIVFTQyrdTAEMIVEFLSEPGIKagrfvgQASKEGDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDL 432
                          90       100
                  ....*....|....*....|....*..
gi 1720362776 392 VIQSSPpqdVES---YIHRSGRTGRAG 415
Cdd:COG1111   433 VIFYEP---VPSeirSIQRKGRTGRKR 456
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
321-424 1.18e-13

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: 68.39  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 321 EGRAIIFCETKKNVTEMAMnpHIKQN---AQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSP 397
Cdd:cd18794    30 GGSGIIYCLSRKECEQVAA--RLQSKgisAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSL 107
                          90       100
                  ....*....|....*....|....*..
gi 1720362776 398 PQDVESYIHRSGRTGRAGRTGICVCFY 424
Cdd:cd18794   108 PKSMESYYQESGRAGRDGLPSECILFY 134
PRK13766 PRK13766
Hef nuclease; Provisional
323-421 5.39e-13

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 72.21  E-value: 5.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 323 RAIIFCE---TKKNVTEMAMNPHIK------QNAQclHGDIAQSQRE--ITLKGFREGSFKVLVATNVAARGLDIPEVDL 391
Cdd:PRK13766  367 RIIVFTQyrdTAEKIVDLLEKEGIKavrfvgQASK--DGDKGMSQKEqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720362776 392 VIQSSP-PQDVESyIHRSGRTGRaGRTGICV 421
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 ...
91-263 2.23e-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: 66.13  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  91 YLFPIQVKTFGPVY-EGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrsPKVLVLAPTRELANQVAKDFKDITRK 169
Cdd:cd17921     1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSG--------GKAVYIAPTRALVNQKEADLRERFGP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 170 L--SVACFYGGTSyqSQINQIRNGiDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVdQMLDLG-FAEQVEDIIheSYK 245
Cdd:cd17921    73 LgkNVGLLTGDPS--VNKLLLAEA-DILVATPEKLDLLLrNGGERLIQDVRLVVVDEA-HLIGDGeRGVVLELLL--SRL 146
                         170
                  ....*....|....*...
gi 1720362776 246 TDSEDNPQTLLFSATCPQ 263
Cdd:cd17921   147 LRINKNARFVGLSATLPN 164
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
319-418 3.16e-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: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 319 GSEGRAIIFCETKKNVTEMA-----MNPHIK-------QNAQCLHGdIAQSQREITLKGFREGSFKVLVATNVAARGLDI 386
Cdd:cd18801    28 GSDTRVIIFSEFRDSAEEIVnflskIRPGIRatrfigqASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDI 106
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720362776 387 PEVDLVI----QSSPPQdvesYIHRSGRTGRaGRTG 418
Cdd:cd18801   107 GEVDLIIcydaSPSPIR----MIQRMGRTGR-KRQG 137
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
312-414 3.70e-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: 64.15  E-value: 3.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 312 DVLQVYSGSEG--RAIIFCETKknVTEMAMNPHIKQNAQCLHG------------------DIAQSQREITLKGFREGSF 371
Cdd:cd18802    14 EILREYFPKTPdfRGIIFVERR--ATAVVLSRLLKEHPSTLAFircgfligrgnssqrkrsLMTQRKQKETLDKFRDGEL 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720362776 372 KVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRtGRA 414
Cdd:cd18802    92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
351-413 1.71e-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: 1.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 351 HGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGR 413
Cdd:cd18796    75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
370-424 3.22e-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: 56.56  E-value: 3.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362776 370 SFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAG-RTGICVCFY 424
Cdd:cd18785    22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
96-223 5.06e-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: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  96 QVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrspKVLVLAPTRELANQVAKDFKDITR----KLS 171
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-------RALYLYPTKALAQDQLRSLRELLEqlglGIR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362776 172 VACFYGGTSYQSQINQIRNGIDILVGTP-----GRIKDHLQSGRLdLSKLRHVVLDE 223
Cdd:cd17923    78 VATYDGDTPREERRAIIRNPPRILLTNPdmlhyALLPHHDRWARF-LRNLRYVVLDE 133
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
322-416 5.31e-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: 5.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 322 GRAIIFCETKKNVTEMAmnphIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQ-SSPPQD 400
Cdd:cd18789    50 DKIIVFTDNVEALYRYA----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQiSGHGGS 125
                          90
                  ....*....|....*.
gi 1720362776 401 VESYIHRSGRTGRAGR 416
Cdd:cd18789   126 RRQEAQRLGRILRPKK 141
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
325-434 3.06e-09

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 59.77  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 325 IIFCETKKNVTEMAmnPHIKQN---AQCLHGDIAQSQREITLKGFREGSFKVLVATNvaARGL--DIPEVDLVIQSSPPQ 399
Cdd:COG0514   234 IVYCLSRKKVEELA--EWLREAgirAAAYHAGLDAEEREANQDRFLRDEVDVIVATI--AFGMgiDKPDVRFVIHYDLPK 309
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720362776 400 DVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRY 434
Cdd:COG0514   310 SIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRF 344
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
107-224 5.01e-09

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: 56.51  E-value: 5.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 107 KDLIAQARTGTGKTFsFAIPLIERLQRnqETIKKSRSPKVLV-LAPTRELANQVAKDFKDITrKLSVACFYGGTSYQSQI 185
Cdd:cd18034    17 RNTIVVLPTGSGKTL-IAVMLIKEMGE--LNRKEKNPKKRAVfLVPTVPLVAQQAEAIRSHT-DLKVGEYSGEMGVDKWT 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720362776 186 NQIRNG----IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:cd18034    93 KERWKEelekYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
ResIII pfam04851
Type III restriction enzyme, res subunit;
115-224 1.46e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 115 TGTGKTF-SFAIplIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC-FYGGTSYqsqiNQIRNGI 192
Cdd:pfam04851  32 TGSGKTLtAAKL--IARL------FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGeIISGDKK----DESVDDN 99
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720362776 193 DILVGTPGRIKDHLQSGRLDLSKLRHVVL--DEV 224
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLPDFFDVIiiDEA 133
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
113-432 2.87e-08

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 57.24  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  113 ARTGTGKTFSFAIPLIERLQRNQ----ETIKKSRSPKVLVLAPTRELANQVAKDFK--------------DITRKLSVAC 174
Cdd:PRK09751     3 APTGSGKTLAAFLYALDRLFREGgedtREAHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderrrrgETEVNLRVGI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  175 FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQS-GRLDLSKLRHVVLDEVDQM--------LDLGFaEQVEDIIHESyk 245
Cdd:PRK09751    83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLTSrARETLRGVETVIIDEVHAVagskrgahLALSL-ERLDALLHTS-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  246 tdsednPQTLLFSATCpQWVYKVAK-----------KYMKSRYEQVDLV---GKMTQKAATTVEHlAIQCH-------WS 304
Cdd:PRK09751   160 ------AQRIGLSATV-RSASDVAAflggdrpvtvvNPPAMRHPQIRIVvpvANMDDVSSVASGT-GEDSHagregsiWP 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  305 QRPAVIGDvlQVYSGsegRAIIFCETKKNVTE-------------MAMNPHIKQN----------------------AQC 349
Cdd:PRK09751   232 YIETGILD--EVLRH---RSTIVFTNSRGLAEkltarlnelyaarLQRSPSIAVDaahfestsgatsnrvqssdvfiARS 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  350 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTG-RAGrtGICVCFYQPRE 428
Cdd:PRK09751   307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGhQVG--GVSKGLFFPRT 384

                   ....
gi 1720362776  429 RGQL 432
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 ...
96-223 3.46e-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: 54.36  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  96 QVKTFGPVYEGKDLIAQARTGTGKTFsFAIPLIERLQRNqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LSVA 173
Cdd:cd17927     7 QLELAQPALKGKNTIICLPTGSGKTF-VAVLICEHHLKK---FPAGRKGKVVFLANKVPLVEQQKEVFRKHFERpgYKVT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720362776 174 CFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 223
Cdd:cd17927    83 GLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDE 133
PRK00254 PRK00254
ski2-like helicase; Provisional
76-410 3.63e-08

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 56.75  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  76 ISEETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetikksRSPKVLVLAPTRE 154
Cdd:PRK00254    8 VDERIKRVLKERGIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR--------EGGKAVYLVPLKA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 155 LANQVAKDFKDITR-KLSVACFYGgtSYQSQiNQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFA 233
Cdd:PRK00254   80 LAEEKYREFKDWEKlGLRVAMTTG--DYDST-DEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 234 EQVEDIIhesykTDSEDNPQTLLFSATC------PQWvykVAKKYMKSRYEQVDLVGKMTQKAATTVEHLAIQCHWSQRP 307
Cdd:PRK00254  157 ATLEMIL-----THMLGRAQILGLSATVgnaeelAEW---LNAELVVSDWRPVKLRKGVFYQGFLFWEDGKIERFPNSWE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 308 AVIGDVLQVYSGsegrAIIFCETKKNVTEMAM---------------------------NPHIKQNAQCLHGDIA----- 355
Cdd:PRK00254  229 SLVYDAVKKGKG----ALVFVNTRRSAEKEALelakkikrfltkpelralkeladsleeNPTNEKLKKALRGGVAfhhag 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362776 356 --QSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSS-----------PPQDVESYIHRSGR 410
Cdd:PRK00254  305 lgRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTkrysnfgwediPVLEIQQMMGRAGR 372
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
107-271 6.82e-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: 53.57  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 107 KDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRklsvacFYGGTS--YQSQ 184
Cdd:cd18047    41 QNLIAQSQSGTGKTAAFVLAMLSQVE------PANKYPQCLCLSPTYELALQTGKVIEQMGK------FYPELKlaYAVR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 185 INQIRNGI----DILVGTPGRIKDH-LQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIIHESYKtdsedNPQTLLFS 258
Cdd:cd18047   109 GNKLERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPR-----NCQMLLFS 183
                         170
                  ....*....|...
gi 1720362776 259 ATCPQWVYKVAKK 271
Cdd:cd18047   184 ATFEDSVWKFAQK 196
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
63-229 3.73e-07

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 53.36  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  63 TREQKEGAFSNFSISEETIKLLKGRGvTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikks 141
Cdd:COG1202   182 TDEVDTVPVDDLDLPPELKDLLEGRG-EELLPVQSLAVeNGLLEGKDQLVVSATATGKTLIGELAGIKNALEGKG----- 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 142 rspKVLVLAPTRELANQVAKDFKDITRK-LSVACFYGgtsyQSQI-----NQIRNGiDILVGTPGRIkDH-LQSGRlDLS 214
Cdd:COG1202   256 ---KMLFLVPLVALANQKYEDFKDRYGDgLDVSIRVG----ASRIrddgtRFDPNA-DIIVGTYEGI-DHaLRTGR-DLG 325
                         170
                  ....*....|....*
gi 1720362776 215 KLRHVVLDEVdQMLD 229
Cdd:COG1202   326 DIGTVVIDEV-HMLE 339
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
115-224 8.48e-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: 48.84  E-value: 8.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 115 TGTGKTFsFAIPLIERLqrnqetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGtsyqsqINQIRNGIDI 194
Cdd:cd17926    27 TGSGKTL-TALALIAYL----------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG------KKKDFDDANV 89
                          90       100       110
                  ....*....|....*....|....*....|
gi 1720362776 195 LVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:cd17926    90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
92-224 1.22e-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: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  92 LFPIQVKTFGPVYEGKDLIAQARTGTGKTFSfAIPLIER-LQRNQETIKKSRspkVLVLAPTRELANQVA-KDFKDITRK 169
Cdd:cd18036     3 LRNYQLELVLPALRGKNTIICAPTGSGKTRV-AVYICRHhLEKRRSAGEKGR---VVVLVNKVPLVEQQLeKFFKYFRKG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362776 170 LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSG----RLDLSKLRHVVLDEV 224
Cdd:cd18036    79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDEC 137
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
106-229 1.59e-06

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: 48.73  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 106 GKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrSPKVLVLAPTRELANQVAKDFK----DITRKLSVACFYGGTSY 181
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-----GVQVLYISPLKALINDQERRLEepldEIDLEIPVAVRHGDTSQ 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720362776 182 QSQINQIRNGIDILVGTPGRIKDHLQSGRLD--LSKLRHVVLDEVDQMLD 229
Cdd:cd17922    76 SEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALLG 125
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
105-223 2.36e-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: 48.28  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 105 EGKDLIAqARTGTGKTFSFAIPLIERLQRnqetiKKSrspKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQS 183
Cdd:cd18035    16 NGNTLIV-LPTGLGKTIIAILVAADRLTK-----KGG---KVLILAPSRPLVEQHAENLKRVlNIPDKITSLTGEVKPEE 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720362776 184 QINQIRNGiDILVGTPGRIKDHLQSGRLDLSKLRHVVLDE 223
Cdd:cd18035    87 RAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDE 125
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
109-165 2.51e-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: 51.00  E-value: 2.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362776 109 LIAQArTGTGKTFSfAIPLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKD 165
Cdd:COG4096   182 LLVMA-TGTGKTRT-AIALIYRL------LKAGRAKRILFLADRNALVDQAKNAFKP 230
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
325-433 3.04e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 50.48  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 325 IIFCETKKNVTEMA---MNPHIKQNAqcLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDV 401
Cdd:PRK11057  240 IIYCNSRAKVEDTAarlQSRGISAAA--YHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNI 317
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720362776 402 ESYIHRSGRTGRAGRTGICVCFYQPRERGQLR 433
Cdd:PRK11057  318 ESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
316-393 3.11e-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: 46.40  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 316 VYSGSEGRAIIFCETKKNVTEMA-----MNPhikqNAQCLHGDIAQSQRE---ITLKGFREGSFKVLVATNVAARGLDIP 387
Cdd:cd18799     1 PYKYVEIKTLIFCVSIEHAEFMAeafneAGI----DAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIP 76

                  ....*.
gi 1720362776 388 EVDLVI 393
Cdd:cd18799    77 EVDNVV 82
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
323-416 3.43e-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: 47.63  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 323 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 398
Cdd:cd18790    29 RVLVTTLTKRmaeDLTEYLQELGVK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 104
                          90       100
                  ....*....|....*....|...
gi 1720362776 399 qDVESYIhRSGRT-----GRAGR 416
Cdd:cd18790   105 -DKEGFL-RSETSliqtiGRAAR 125
GUCT_Hera cd12938
RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase ...
509-579 5.96e-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: 44.60  E-value: 5.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 509 PRSLITSDKGFVTMTLESPEEIQ--DVSCAWKELNRKLSSNavshVTRMCLLKGNMGVCFDVPTSESERLQAE 579
Cdd:cd12938     1 PRSLLTGEEGWTTLQLTGSRLLPpgSVRRAVGLLSRAAADG----VGKIRILADAGGAVFDLPEEIAKELLAK 69
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
92-432 8.69e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 48.95  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  92 LFPIQVKTFGPVYEGKD-LIAqARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANqvakdfkDITRKL 170
Cdd:COG1201    25 PTPPQREAWPAIAAGEStLLI-APTGSGKTLAAFLPALDELARRPRPGELPDGLRVLYISPLKALAN-------DIERNL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 171 SVACFYGGTSYQSQINQIRNGI------------------DILVGTPGRIkdHL----QSGRLDLSKLRHVVLDEV---- 224
Cdd:COG1201    97 RAPLEEIGEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTPESL--ALlltsPDARELLRGVRTVIVDEIhala 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 225 -----DQ-MLDLgfaEQVEDIihesyktdSEDNPQTLLFSATC--PQwvyKVAkkymksRYeqvdLVGKMTQKAATTVE- 295
Cdd:COG1201   175 gskrgVHlALSL---ERLRAL--------APRPLQRIGLSATVgpLE---EVA------RF----LVGYEDPRPVTIVDa 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 296 ------HLAIQChwsqrPAVIGDVLQVYSGSEGRA---------------IIFCETKKnVTEM------AMNPHIKQNAQ 348
Cdd:COG1201   231 gagkkpDLEVLV-----PVEDLIERFPWAGHLWPHlyprvldlieahrttLVFTNTRS-QAERlfqrlnELNPEDALPIA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 349 CLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQ-SSPPQdVESYIHRSGRTG-RAGRT--GICVcfy 424
Cdd:COG1201   305 AHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQvGSPKS-VARLLQRIGRAGhRVGEVskGRLV--- 380

                  ....*...
gi 1720362776 425 qPRERGQL 432
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 ...
323-416 1.00e-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: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 323 RAIIFCETKKNVTEM-----AMNPHIKQNAQCLH----GDIAQSQREITlKGFREGSFKVLVATNVAARGLDIPEVDLVI 393
Cdd:cd18797    37 KTIVFCRSRKLAELLlrylkARLVEEGPLASKVAsyraGYLAEDRREIE-AELFNGELLGVVATNALELGIDIGGLDAVV 115
                          90       100
                  ....*....|....*....|...
gi 1720362776 394 QSSPPQDVESYIHRSGRTGRAGR 416
Cdd:cd18797   116 LAGYPGSLASLWQQAGRAGRRGK 138
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
325-424 1.41e-05

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 48.35  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  325 IIFCETK---KNVTEMAMnpHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDV 401
Cdd:PLN03137   684 IIYCLSRmdcEKVAERLQ--EFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
                           90       100
                   ....*....|....*....|...
gi 1720362776  402 ESYIHRSGRTGRAGRTGICVCFY 424
Cdd:PLN03137   762 EGYHQECGRAGRDGQRSSCVLYY 784
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
350-433 2.55e-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: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 350 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICVCFYQPR- 427
Cdd:cd18810    57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQlRGRVGRSKERAYAYFLYPDQk 136

                  ....*....
gi 1720362776 428 ---ERGQLR 433
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 ...
350-433 2.56e-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: 44.95  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 350 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICVCFYQPR- 427
Cdd:cd18792    66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQlRGRVGRGKHQSYCYLLYPDPk 145

                  ....*....
gi 1720362776 428 ---ERGQLR 433
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 ...
109-224 4.02e-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: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 109 LIAQArTGTGKTFSFAIpLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSvACFYGGTSYQSQinqi 188
Cdd:cd18032    24 LLVMA-TGTGKTYTAAF-LIKRL------LEANRKKRILFLAHREELLEQAERSFKEVLPDGS-FGNLKGGKKKPD---- 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720362776 189 rnGIDILVGT----PGRIKDHLQS-GRLDLsklrhVVLDEV 224
Cdd:cd18032    91 --DARVVFATvqtlNKRKRLEKFPpDYFDL-----IIIDEA 124
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
323-416 4.54e-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: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 323 RAIIFCETKK---NVTEMAMNPHIKqnAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLV-IQSSpp 398
Cdd:TIGR00631 444 RVLVTTLTKKmaeDLTDYLKELGIK--VRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaILDA-- 519
                          90       100
                  ....*....|....*....|...
gi 1720362776 399 qDVESYIhRSGRT-----GRAGR 416
Cdd:TIGR00631 520 -DKEGFL-RSERSliqtiGRAAR 540
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
108-416 6.63e-05

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 45.52  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 108 DLIAQARTGTGKT---FSFAiplierlqrnQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYG----GTS 180
Cdd:TIGR01587   1 LLVIEAPTGYGKTeaaLLWA----------LHSIKSQKADRVIIALPTRATINAMYRRAKELFGSELVGLHHSssfsRIK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 181 YQSQINQI-----RNGIDILVGTPGRIK----DHLQSGRLDLSKLRH----------VVLDEVDQMLD--LGFAEQVEDI 239
Cdd:TIGR01587  71 EMGDSEEFehlfpLYIHSNDKLFLDPITvctiDQVLKSVFGEFGHYEftlasianslLIFDEVHFYDEytLALILAVLEV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 240 IhesyktdSEDNPQTLLFSATCPqwvykvakKYMKSRYEQVDLVGKM----TQKAATTVEHLAIQC--HWSQRPAVIGDV 313
Cdd:TIGR01587 151 L-------KDNDVPILLMSATLP--------KFLKEYAEKIGYVEFNepldLKEERRFENHRFILIesDKVGEISSLERL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 314 LQVYSgSEGRAIIFCETKKNVTEMAMNPHIKQNAQC---LHGDIAQSQRE----ITLKGFREGSFK-VLVATNVAARGLD 385
Cdd:TIGR01587 216 LEFIK-KGGSIAIIVNTVDRAQEFYQQLKEKAPEEEiilYHSRFTEKDRAkkeaELLREMKKSNEKfVIVATQVIEASLD 294
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720362776 386 IpEVDLVIQSSPPQDveSYIHRSGRTGRAGR 416
Cdd:TIGR01587 295 I-SADVMITELAPID--SLIQRLGRLHRYGR 322
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
105-170 1.65e-04

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 44.92  E-value: 1.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362776 105 EGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrspKVLVLAPTRELANQ-VAKDFKDITRKL 170
Cdd:COG1199    32 EGRHLLIEAGTGTGKTLAYLVPALLAARETGK--------KVVISTATKALQEQlVEKDLPLLRKAL 90
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
363-438 1.79e-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: 42.68  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 363 LKGFREGSFKVLVAT----NVAARGLDIPE-VDLVIQSSPPqdVESYIHRSGRTGR--AGR--TGICVCFYQPRE----- 428
Cdd:cd18798    65 LEKFEEGEIDVLIGVasyyGVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPElfeal 142
                          90
                  ....*....|..
gi 1720362776 429 --RGQLRYVEQK 438
Cdd:cd18798   143 kkRLKLILDEFI 154
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
136-222 2.96e-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: 42.93  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 136 ETIKKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGG-TSYQSQINQIR-NGIDILVGTPGRIKDHLQSGRLD 212
Cdd:pfam14617 117 QRPKSNGSPHTLVLTIAALRAADVLRPLKKLqTKGFKVAKLFAKhIKLEEHITYCKaSRIGIGVGTPGRIADLLENESLS 196
                          90
                  ....*....|
gi 1720362776 213 LSKLRHVVLD 222
Cdd:pfam14617 197 VDNLKYIILD 206
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
108-260 3.06e-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: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 108 DLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSyqsqiNQ 187
Cdd:cd17918    38 DRLLSGDVGSGKTLVALGAALLAYKNGK---------QVAILVPTEILAHQHYEEARKFLPFINVELVTGGTK-----AQ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 188 IRNGIDILVGTpgrikdhlqsgrldlsklrHVVLDEVDQMLDLGFAeqvedIIHESYKTDSED--------NPQTLLFSA 259
Cdd:cd17918   104 ILSGISLLVGT-------------------HALLHLDVKFKNLDLV-----IVDEQHRFGVAQrealynlgATHFLEATA 159

                  .
gi 1720362776 260 T 260
Cdd:cd17918   160 T 160
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
350-426 3.87e-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: 41.56  E-value: 3.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362776 350 LHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHR-SGRTGRAGRTGICVCFYQP 426
Cdd:cd18811    67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQlRGRVGRGDHQSYCLLVYKD 144
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
324-419 5.50e-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: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 324 AIIFCETKKNVTEMAMN-----PHikqnaqclHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPeVDLVIqsspp 398
Cdd:cd18795    46 VLVFCSSRKECEKTAKDlagiaFH--------HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVI----- 111
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720362776 399 qdVESYIHRSGRT-------------GRAGRTGI 419
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 ...
102-223 1.15e-03

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: 40.57  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 102 PVYEGKDLIAQARTGTGKTF-SFAIplierLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL--SVACFYGG 178
Cdd:cd18073    13 PAMKGKNTIICAPTGCGKTFvSLLI-----CEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHgyRVTGISGA 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720362776 179 TSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 223
Cdd:cd18073    88 TAENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
91-224 1.22e-03

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: 40.40  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  91 YLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRK 169
Cdd:cd18028     1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---------KALYLVPLRALASEKYEEFKKLEEI 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362776 170 -LSVACFYGgtSYQSQINQIRNgIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 224
Cdd:cd18028    72 gLKVGISTG--DYDEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEI 124
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
350-392 1.52e-03

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 41.57  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720362776 350 LHGDIAQSQR-EItLKGFREGSFKVLVATNVAARGLDIPEVDLV 392
Cdd:PRK05298  476 LHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
350-392 2.02e-03

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 41.15  E-value: 2.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720362776 350 LHGDIAQSQR-EItLKGFREGSFKVLVATNVAARGLDIPEVDLV 392
Cdd:COG0556   473 LHSDIDTLERvEI-IRDLRLGEFDVLVGINLLREGLDLPEVSLV 515
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
95-224 3.13e-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: 39.65  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776  95 IQVKTFGPVYEG-KDLIAQARTGTGKT--FSFAIplierLQRNQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRKL 170
Cdd:cd18023     5 IQSEVFPDLLYSdKNFVVSAPTGSGKTvlFELAI-----LRLLKERNPLPWgNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720362776 171 SVAC--FYGGTSYQSqINQIRNgIDILVGTPG-------RIKDHlqsGRLdLSKLRHVVLDEV 224
Cdd:cd18023    80 GLSCaeLTGDTEMDD-TFEIQD-ADIILTTPEkwdsmtrRWRDN---GNL-VQLVALVLIDEV 136
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
373-418 4.31e-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: 35.99  E-value: 4.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720362776 373 VLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTG 418
Cdd:cd09300     8 VLIAVN*ALTGFDAPELNTIIVDKNLRSYRGLNQAFGRANRIYTFG 53
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
115-165 5.45e-03

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 40.03  E-value: 5.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720362776 115 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 165
Cdd:PRK05298   41 TGSGKTFTMA-NVIARLQR-----------PTLVLAHNKTLAAQLYSEFKE 79
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
349-424 6.45e-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: 37.90  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362776 349 CLHGDIAQS-QREI---TLKGFRegsfKVLVATNVAARGLDIPEVDLVIqssppqD-----VESYIHRSG---------- 409
Cdd:cd18791    79 PLHSSLPPEeQQRVfepPPPGVR----KVVLATNIAETSITIPGVVYVI------DsglvkEKVYDPRTGlsslvtvwis 148
                          90       100
                  ....*....|....*....|...
gi 1720362776 410 ------RTGRAGRT--GICVCFY 424
Cdd:cd18791   149 kasaeqRAGRAGRTrpGKCYRLY 171
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
115-165 6.52e-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: 6.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720362776 115 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 165
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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