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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729 220 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 299
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80

                          90
                  ....*....|...
gi 1907078729 300 WHDS-DWILSVPA 311
Cdd:cd12936    81 WHDSrRWQLSVAT 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729 220 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 299
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80

                          90
                  ....*....|...
gi 1907078729 300 WHDS-DWILSVPA 311
Cdd:cd12936    81 WHDSrRWQLSVAT 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729   1 MLDLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQR 80
Cdd:COG0513   157 MLDMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729  81 PAVIGDVLQVYSgsEGRAIIFCETKKNVTEMA----------------MNP----------------------------H 116
Cdd:COG0513   229 LELLRRLLRDED--PERAIVFCNTKRGADRLAeklqkrgisaaalhgdLSQgqreraldafrngkirvlvatdvaargiD 306

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907078729 117 IK-----------QDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 178
Cdd:COG0513   307 IDdvshvinydlpEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379

ATP-dependent RNA helicase DbpA; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729   1 MLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHWSQ 79
Cdd:PRK11776  159 MLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSPDE 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729  80 RPAVIGDVLQVY---SgsegrAIIFCETKKNVTEMA-------------------------------------------- 112
Cdd:PRK11776  229 RLPALQRLLLHHqpeS-----CVVFCNTKKECQEVAdalnaqgfsalalhgdleqrdrdqvlvrfanrscsvlvatdvaa 303

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907078729 113 -----------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 170
Cdd:PRK11776  304 rgldikaleavINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729 220 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 299
Cdd:cd12936     1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80

                          90
                  ....*....|...
gi 1907078729 300 WHDS-DWILSVPA 311
Cdd:cd12936    81 WHDSrRWQLSVAT 93

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907078729 238 GFVTMTLESPEEIQDVSCAWKELNRKLSSNaVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWILSVP 310
Cdd:cd12929     1 GWVTYKLEGPRLIQSLSRLVALLKRQLLSN-VSEVGKVAELEGNGGFYFDVRPEARERLQAEPEVAGLRLEVA 72

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907078729   1 MLDLGFAEQVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 55
Cdd:cd17944   148 MLDMGFAEQVEEILSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729 230 RSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWI-LS 308
Cdd:cd12937     1 RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSAWVDKRGVtLE 80

                  ....*.
gi 1907078729 309 VPAKLP 314
Cdd:cd12937    81 VATELP 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907078729   1 MLDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 48
Cdd:cd00268   148 MLDMGFEEDVEKILSALPK-----DRQTLLFSATLPEEVKELAKKFLK 190

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729  68 VEHLAIQCHWSQRPAVIGDVLqVYSGSEGRAIIFCETKKNVTEMAMN--------------------------------- 114
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLL-LEKLKPGKAIIFVNTKKRVDRLAELleelgikvaalhgdlsqeereralkkfrsgkvr 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907078729 115 --------------PHIK--------QDVESYIHRSGRTGRAGRTGICVCFY 144
Cdd:cd18787    80 vlvatdvaargldiPGVDhvinydlpRDAEDYVHRIGRTGRAGRKGTAITFV 131

ATP-dependent RNA helicase SrmB; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729   1 MLDLGFAEQVEDIIHESY--KtdsednpQTLLFSATCP-QWVYKVAKKYMK---------SRYEQvdlvGKMTQ--KAAT 66
Cdd:PRK11192  159 MLDMGFAQDIETIAAETRwrK-------QTLLFSATLEgDAVQDFAERLLNdpveveaepSRRER----KKIHQwyYRAD 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729  67 TVEH-LAIQCHWSQRPAVigdvlqvysgseGRAIIFCETKKNVTEMA--------------------------------- 112
Cdd:PRK11192  228 DLEHkTALLCHLLKQPEV------------TRSIVFVRTRERVHELAgwlrkaginccylegemvqakrneaikrltdgr 295

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907078729 113 MNPHIKQDVES----------------------YIHRSGRTGRAGRTGICVCFYQPRERGQL----RYVEQK 158
Cdd:PRK11192  296 VNVLVATDVAArgididdvshvinfdmprsadtYLHRIGRTGRAGRKGTAISLVEAHDHLLLgkieRYIEEP 367

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907078729   1 MLDLGFAEQVEDIIhESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRY 51
Cdd:cd18052   206 MLDMGFGPEIRKLV-SEPGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255

ATP-dependent RNA helicase RhlB; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729   1 MLDLGFAEQVEDIIHEsykTDSEDNPQTLLFSATCPQWVYKVAKKYMksrYEQVDLVGKMTQKAATTVEH---------- 70
Cdd:PRK01297  249 MLDMGFIPQVRQIIRQ---TPRKEERQTLLFSATFTDDVMNLAKQWT---TDPAIVEIEPENVASDTVEQhvyavagsdk 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078729  71 ------LAIQCHWsQRPAVIGD----VLQVY-------------SGS----------EGraiiFCETKKNV---TEMA-- 112
Cdd:PRK01297  323 ykllynLVTQNPW-ERVMVFANrkdeVRRIEerlvkdginaaqlSGDvpqhkriktlEG----FREGKIRVlvaTDVAgr 397

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907078729 113 ----------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAG 160
Cdd:PRK01297  398 gihidgishvINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLG 455

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907078729   1 MLDLGFAEQVEDIIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSrYEQV 54
Cdd:cd17966   149 MLDMGFEPQIRKIV-------DQIRPdrQTLMWSATWPKEVRRLAEDFLKD-YIQV 196

ATP-dependent RNA helicase RhlB; Provisional

                          10        20
                  ....*....|....*....|....
gi 1907078729 120 DVESYIHRSGRTGRAGRTGICVCF 143
Cdd:PRK04837  335 DCEDYVHRIGRTGRAGASGHSISL 358

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907078729   1 MLDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMKSRYE 52
Cdd:cd17940   153 LLSQDFQPIIEKILNFLPK-----ERQILLFSATFPLTVKNFMDRHMHNPYE 199

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907078729   1 MLDLGFAEQVEDIIHesyktDSEDNPQTLLFSATCPQWVYKVAKKYMK 48
Cdd:cd17962   145 MLKMGFQQQVLDILE-----NISHDHQTILVSATIPRGIEQLAGQLLQ 187

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907078729   1 MLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAK 44
Cdd:cd17941   148 ILDMGFKETLDAIVENLPKSR-----QTLLFSATQTKSVKDLAR 186

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907078729   1 MLDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYM 47
Cdd:cd17939   151 MLSRGFKDQIYDIFQFLPP-----ETQVVLFSATMPHEVLEVTKKFM 192

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907078729   1 MLDLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAK 44
Cdd:cd17951   158 MIDMGFEEDIRTIF-SYFKGQR----QTLLFSATMPKKIQNFAK 196