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Conserved domains on  [gi|568969017|ref|XP_006514408|]
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ATP-dependent RNA helicase DDX50 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
145-346 1.57e-142

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: 413.86  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd17944    1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:cd17944   81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568969017 305 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 346
Cdd:cd17944  161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
GUCT_RHII_Gualpha_beta cd12936
RNA-binding GUCT domain found in vertebrate RNA helicase II/Gualpha (RH-II/Gualpha), RNA ...
511-602 8.05e-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: 165.70  E-value: 8.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 511 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 590
Cdd:cd12936    1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                         90
                 ....*....|...
gi 568969017 591 WHDS-DWILSVPA 602
Cdd:cd12936   81 WHDSrRWQLSVAT 93
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
359-435 1.31e-09

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd18787:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 131  Bit Score: 56.75  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 359 VEHLAIQCHWSQRPAVIGdVLQVYSGSEGRAIIFCETKKNVTEMAMN--------------------------------- 405
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELleelgikvaalhgdlsqeereralkkfrsgkvr 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568969017 406 --------------PHIK--------QDVESYIHRSGRTGRAGRTGICVCFY 435
Cdd:cd18787   80 vlvatdvaargldiPGVDhvinydlpRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
145-346 1.57e-142

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: 413.86  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd17944    1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:cd17944   81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568969017 305 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 346
Cdd:cd17944  161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
136-469 4.31e-109

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 336.35  E-value: 4.31e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 215
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 293
Cdd:COG0513   79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 294 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 373
Cdd:COG0513  159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 374 VIGDVLQVYsgSEGRAIIFCETKKNVTEMA----------------MNP----------------------------HIK 409
Cdd:COG0513  231 LLRRLLRDE--DPERAIVFCNTKRGADRLAeklqkrgisaaalhgdLSQgqreraldafrngkirvlvatdvaargiDID 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 410 -----------QDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 469
Cdd:COG0513  309 dvshvinydlpEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
135-461 1.92e-63

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 217.75  E-value: 1.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 135 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 214
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 215 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:PRK11776  79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 290 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 368
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 369 SQRPAVIGDVLQVY---SgsegrAIIFCETKKNVTEMA------------------------------------------ 403
Cdd:PRK11776 227 DERLPALQRLLLHHqpeS-----CVVFCNTKKECQEVAdalnaqgfsalalhgdleqrdrdqvlvrfanrscsvlvatdv 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 404 -------------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 461
Cdd:PRK11776 302 aargldikaleavINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
159-333 3.01e-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: 177.82  E-value: 3.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 236
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  237 VACFYGGTSYQSQINQIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 316
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 568969017  317 PQTLLFSATCPQWVYKV 333
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 ...
511-602 8.05e-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: 165.70  E-value: 8.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 511 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 590
Cdd:cd12936    1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                         90
                 ....*....|...
gi 568969017 591 WHDS-DWILSVPA 602
Cdd:cd12936   81 WHDSrRWQLSVAT 93
DEXDc smart00487
DEAD-like helicases superfamily;
149-339 1.27e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 161.12  E-value: 1.27e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017   149 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 227
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017   228 FKDITRK--LSVACFYGGTSYQSQINQIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568969017   305 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 339
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 ...
514-608 2.89e-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: 131.12  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  514 GASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHD 593
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 568969017  594 SD-WILSVPAKLPEIE 608
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
359-435 1.31e-09

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: 56.75  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 359 VEHLAIQCHWSQRPAVIGdVLQVYSGSEGRAIIFCETKKNVTEMAMN--------------------------------- 405
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELleelgikvaalhgdlsqeereralkkfrsgkvr 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568969017 406 --------------PHIK--------QDVESYIHRSGRTGRAGRTGICVCFY 435
Cdd:cd18787   80 vlvatdvaargldiPGVDhvinydlpRDAEDYVHRIGRTGRAGRKGTAITFV 131
 
Name Accession Description Interval E-value
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
145-346 1.57e-142

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: 413.86  E-value: 1.57e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd17944    1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:cd17944   81 TKDFKDITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568969017 305 IHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 346
Cdd:cd17944  161 LSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYEQVD 202
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
136-469 4.31e-109

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 336.35  E-value: 4.31e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikKSRSPKVLVLA 215
Cdd:COG0513    4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPS-----RPRAPQALILA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 293
Cdd:COG0513   79 PTRELALQVAEELRKLAKylGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 294 DLGFAEQVEDIIHesyKTDSEDnpQTLLFSATCPQWVYKVAKKYMKSrYEQVDLVGKmtQKAATTVEHLAIQCHWSQRPA 373
Cdd:COG0513  159 DMGFIEDIERILK---LLPKER--QTLLFSATMPPEIRKLAKRYLKN-PVRIEVAPE--NATAETIEQRYYLVDKRDKLE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 374 VIGDVLQVYsgSEGRAIIFCETKKNVTEMA----------------MNP----------------------------HIK 409
Cdd:COG0513  231 LLRRLLRDE--DPERAIVFCNTKRGADRLAeklqkrgisaaalhgdLSQgqreraldafrngkirvlvatdvaargiDID 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 410 -----------QDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSK 469
Cdd:COG0513  309 dvshvinydlpEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKR 379
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
145-339 1.72e-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: 1.72e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd00268    1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVE 302
Cdd:cd00268   79 AEVARKLGKgtGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568969017 303 DIIHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 339
Cdd:cd00268  159 KILSALPK-----DRQTLLFSATLPEEVKELAKKFLK 190
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
135-461 1.92e-63

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 217.75  E-value: 1.92e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 135 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVL 214
Cdd:PRK11776   5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD------VKRFRVQALVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 215 APTRELANQVAKDFKDITR-----KLSVACfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:PRK11776  79 CPTRELADQVAKEIRRLARfipniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 290 DQMLDLGFAEQVEDIIHESYKTDsednpQTLLFSATCPQWVYKVAKKYMKSRYE-QVDlvgkmTQKAATTVEHLAIQCHW 368
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARR-----QTLLFSATYPEGIAAISQRFQRDPVEvKVE-----STHDLPAIEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 369 SQRPAVIGDVLQVY---SgsegrAIIFCETKKNVTEMA------------------------------------------ 403
Cdd:PRK11776 227 DERLPALQRLLLHHqpeS-----CVVFCNTKKECQEVAdalnaqgfsalalhgdleqrdrdqvlvrfanrscsvlvatdv 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 404 -------------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 461
Cdd:PRK11776 302 aargldikaleavINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPS 372
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
141-346 9.47e-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: 199.73  E-value: 9.47e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 141 ISEETIKLLKGRGVTYLFPIQVKTFGPVYE-GKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSpKVLVLAPTRE 219
Cdd:cd17964    1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGV-SALIISPTRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 220 LANQVAKDFKDIT---RKLSVACFYGGTSYQSQINQI-RNGIDILVGTPGRIKDHL--QSGRLDLSKLRHVVLDEVDQML 293
Cdd:cd17964   80 LALQIAAEAKKLLqglRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLenPGVAKAFTDLDYLVLDEADRLL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568969017 294 DLGFAEQVEDIIhESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD 346
Cdd:cd17964  160 DMGFRPDLEQIL-RHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFID 211
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
133-461 1.50e-55

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 200.07  E-value: 1.50e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 133 EGAFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVL 212
Cdd:PRK11634   5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD------PELKAPQIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 213 VLAPTRELANQVAK---DFKDITRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:PRK11634  79 VLAPTRELAVQVAEamtDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 290 DQMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQvdlvgkMTQKAATTVEHLAiQCHWS 369
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQ-----IPEGHQTALFSATMPEAIRRITRRFMKEPQEV------RIQSSVTTRPDIS-QSYWT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 370 QRPAVIGDVLQVYSGSE--GRAIIFCETKKNVTEMA-------------------------------------------- 403
Cdd:PRK11634 227 VWGMRKNEALVRFLEAEdfDAAIIFVRTKNATLEVAealerngynsaalngdmnqalreqtlerlkdgrldiliatdvaa 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568969017 404 -----------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAGITFKRVGVPS 461
Cdd:PRK11634 307 rgldverislvVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPN 375
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
159-339 1.05e-52

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


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 181.15  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRS----PKVLVLAPTRELANQVakdfKDITRK 234
Cdd:cd17967   25 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkayPSALILAPTRELAIQI----YEEARK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 235 LS------VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHES 308
Cdd:cd17967  101 FSyrsgvrSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVEHP 180
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568969017 309 YKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 339
Cdd:cd17967  181 DMPPKGER-QTLMFSATFPREIQRLAADFLK 210
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
159-333 3.01e-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: 177.82  E-value: 3.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrSPKVLVLAPTRELANQVAKDFKDIT--RKLS 236
Cdd:pfam00270   2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN------GPQALVLAPTRELAEQIYEELKKLGkgLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  237 VACFYGGTSYQSQINQIRnGIDILVGTPGRIKDHLQSGRLdLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 316
Cdd:pfam00270  76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-----K 148
                         170
                  ....*....|....*..
gi 568969017  317 PQTLLFSATCPQWVYKV 333
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 ...
511-602 8.05e-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: 165.70  E-value: 8.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 511 HISGASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAE 590
Cdd:cd12936    1 HISGATSKEQRSLLNSDKGFVTMALRCSEEIPNRSYAWKELKEKLGVDADAHISRMCLLKGRMGVCFDVPTAEVESIQAE 80
                         90
                 ....*....|...
gi 568969017 591 WHDS-DWILSVPA 602
Cdd:cd12936   81 WHDSrRWQLSVAT 93
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
134-327 2.70e-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: 2.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 134 GAFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKV-- 211
Cdd:cd17959    1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVga 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 212 --LVLAPTRELANQVAKDFKDITRK--LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLD 287
Cdd:cd17959   73 raLILSPTRELALQTLKVTKELGKFtdLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568969017 288 EVDQMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP 327
Cdd:cd17959  153 EADRLFEMGFAEQLHEILSR-----LPENRQTLLFSATLP 187
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
159-342 1.74e-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: 1.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS---RSPKVLVLAPTRELANQVAKDfkdiTRKL 235
Cdd:cd18052   68 PVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFsevQEPQALIVAPTRELANQIFLE----ARKF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 236 S-------VACfYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhES 308
Cdd:cd18052  144 SygtcirpVVV-YGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLV-SE 221
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568969017 309 YKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRY 342
Cdd:cd18052  222 PGMPSKEDRQTLMFSATFPEEIQRLAAEFLKEDY 255
DEXDc smart00487
DEAD-like helicases superfamily;
149-339 1.27e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 161.12  E-value: 1.27e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017   149 LKGRGVTYLFPIQVKTFGPVYEG-KDLIAQARTGTGKTFSFAIPLIERLqrnqetiKKSRSPKVLVLAPTRELANQVAKD 227
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017   228 FKDITRK--LSVACFYGGTSYQSQINQIRNG-IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:smart00487  74 LKKLGPSlgLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568969017   305 IHESYKtdsedNPQTLLFSATCPQWVYKVAKKYMK 339
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 ...
146-345 3.04e-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: 159.84  E-value: 3.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 146 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVA 225
Cdd:cd17966    2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN-AQPPLERGDGPIVLVLAPTRELAQQIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 226 KDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVED 303
Cdd:cd17966   81 QEANKFGGssRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568969017 304 IIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSrYEQV 345
Cdd:cd17966  161 IV-------DQIRPdrQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
159-340 5.11e-45

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 160.18  E-value: 5.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQR--NQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 235
Cdd:cd17945   15 PIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDGPYALILAPTRELAQQIEEETQKFAKPLg 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 236 -SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIH----ESYK 310
Cdd:cd17945   95 iRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDampvSNKK 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568969017 311 TDSEDNP-----------QTLLFSATCPQWVYKVAKKYMKS 340
Cdd:cd17945  175 PDTEEAEklaasgkhryrQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
159-343 5.29e-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: 5.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 236
Cdd:cd17940   24 PIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID------PKKDVIQALILVPTRELALQTSQVCKELGKhmGVK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 237 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedN 316
Cdd:cd17940   98 VMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPK-----E 172
                        170       180
                 ....*....|....*....|....*..
gi 568969017 317 PQTLLFSATCPQWVYKVAKKYMKSRYE 343
Cdd:cd17940  173 RQILLFSATFPLTVKNFMDRHMHNPYE 199
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
160-338 5.47e-45

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: 159.41  E-value: 5.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 160 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSV-- 237
Cdd:cd17939   23 IQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV------RETQALVLAPTRELAQQIQKVVKALGDYMGVkv 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 238 ACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsedNP 317
Cdd:cd17939   97 HACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPP-----ET 171
                        170       180
                 ....*....|....*....|.
gi 568969017 318 QTLLFSATCPQWVYKVAKKYM 338
Cdd:cd17939  172 QVVLFSATMPHEVLEVTKKFM 192
PTZ00110 PTZ00110
helicase; Provisional
146-437 9.52e-45

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 168.41  E-value: 9.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 146 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqRNQETIKKSRSPKVLVLAPTRELANQV- 224
Cdd:PTZ00110 142 LKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHI-NAQPLLRYGDGPIVLVLAPTRELAEQIr 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 --AKDFKDITrKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVE 302
Cdd:PTZ00110 221 eqCNKFGASS-KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 303 DIIhesyktdSEDNP--QTLLFSATCPQWVYKVAKKYMKSRYEQVDlVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVLQ 380
Cdd:PTZ00110 300 KIV-------SQIRPdrQTLMWSATWPKEVQSLARDLCKEEPVHVN-VGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQ 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 381 VYSGSEGRAIIFCETKKNVTEM----------AMNPH-----------------------IKQDV--------------- 412
Cdd:PTZ00110 372 RIMRDGDKILIFVETKKGADFLtkelrldgwpALCIHgdkkqeertwvlnefktgkspimIATDVasrgldvkdvkyvin 451
                        330       340       350
                 ....*....|....*....|....*....|..
gi 568969017 413 -------ESYIHRSGRTGRAGRTGICVCFYQP 437
Cdd:PTZ00110 452 fdfpnqiEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
58-451 1.27e-44

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 166.63  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  58 APKPKKAKMREKLNGDTKEGLRFSDEFSPSHKSRRKDLPNGDVDEYEKRSKRVSSSENshkssdkaeETLTREQKEGA-- 135
Cdd:PRK01297  18 APAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKL---------EDFVVEPQEGKtr 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrnQETIKKSR---SPKVL 212
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLL--QTPPPKERymgEPRAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 213 VLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIR-NGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKytGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 290 DQMLDLGFAEQVEDIIHEsykTDSEDNPQTLLFSATCPQWVYKVAKKYMksrYEQVDLVGKMTQKAATTVEHLAIQCHWS 369
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQ---TPRKEERQTLLFSATFTDDVMNLAKQWT---TDPAIVEIEPENVASDTVEQHVYAVAGS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 370 QRPAVIGDVlqVYSGSEGRAIIFCETKKNV-------------------------------------------TEMA--- 403
Cdd:PRK01297 321 DKYKLLYNL--VTQNPWERVMVFANRKDEVrrieerlvkdginaaqlsgdvpqhkriktlegfregkirvlvaTDVAgrg 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568969017 404 ---------MNPHIKQDVESYIHRSGRTGRAGRTGICVCFYQPRERGQLRYVEQKAG 451
Cdd:PRK01297 399 ihidgishvINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLG 455
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
148-325 7.58e-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: 7.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 148 LLKG---RGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqeTIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd17947    1 LLRAlssLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY---RPKKKAATRVLVLVPTRELAMQC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AK------DFKDITRKLSVacfyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGF 297
Cdd:cd17947   78 FSvlqqlaQFTDITFALAV----GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGF 153
                        170       180
                 ....*....|....*....|....*...
gi 568969017 298 AEQVEDIIHESYKTDsednpQTLLFSAT 325
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 ...
159-339 5.20e-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: 153.90  E-value: 5.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LS 236
Cdd:cd17957   15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP----RKKKGLRALILAPTRELASQIYRELLKLSKGtgLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 237 VACFYGGTS-YQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIihesYKTDSED 315
Cdd:cd17957   91 IVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI----LAACTNP 166
                        170       180
                 ....*....|....*....|....
gi 568969017 316 NPQTLLFSATCPQWVYKVAKKYMK 339
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) ...
141-343 7.94e-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: 7.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 141 ISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTREL 220
Cdd:cd17953   19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK-DQRPVKPGEGPIGLIMAPTREL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 221 ANQVAKDFKDITRKLS--VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHL--QSGRL-DLSKLRHVVLDEVDQMLDL 295
Cdd:cd17953   98 ALQIYVECKKFSKALGlrVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMFDM 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568969017 296 GFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSRYE 343
Cdd:cd17953  178 GFEPQIMKIV-NNIRPDR----QTVLFSATFPRKVEALARKVLHKPIE 220
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
130-434 1.09e-42

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 159.75  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 130 EQKegaFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL-QRNQETIKKSRS 208
Cdd:PRK04837   7 EQK---FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlSHPAPEDRKVNQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 209 PKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVL 286
Cdd:PRK04837  84 PRALIMAPTRELAVQIHADAEPLAQatGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 287 DEVDQMLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKS-RYEQVDlvgkMTQKAATTV-EHL-- 362
Cdd:PRK04837 164 DEADRMFDLGF---IKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVE----PEQKTGHRIkEELfy 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 363 ------------AIQCHWSQRpAVI--------------------------GDVLQvysgsEGRAIIFCE-TKKNV---- 399
Cdd:PRK04837 237 psneekmrllqtLIEEEWPDR-AIIfantkhrceeiwghlaadghrvglltGDVAQ-----KKRLRILEEfTRGDLdilv 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 568969017 400 -TEMAMNP-HIKQ-----------DVESYIHRSGRTGRAGRTGICVCF 434
Cdd:PRK04837 311 aTDVAARGlHIPAvthvfnydlpdDCEDYVHRIGRTGRAGASGHSISL 358
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
160-335 1.68e-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: 150.04  E-value: 1.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 160 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRK---LS 236
Cdd:cd17949   17 IQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLLKPfhwIV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 237 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQMLDLGFAEQVEDII-------HES 308
Cdd:cd17949   97 PGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKILellddkrSKA 176
                        170       180
                 ....*....|....*....|....*...
gi 568969017 309 YKTDSEDNP-QTLLFSATCPQWVYKVAK 335
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 ...
145-335 1.40e-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: 1.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikKSRSPKVLVLAPTRELANQV 224
Cdd:cd17941    1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWT--PEDGLGALIISPTRELAMQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITRK--LSVACFYGGTSYQSQINQIrNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQMLDLGFAEQV 301
Cdd:cd17941   79 FEVLRKVGKYhsFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETL 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568969017 302 EDIIHESYKTDsednpQTLLFSATCPQWVYKVAK 335
Cdd:cd17941  158 DAIVENLPKSR-----QTLLFSATQTKSVKDLAR 186
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
136-449 1.09e-39

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 151.63  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQ---RnqetiKKSRSPKVL 212
Cdd:PRK11192   3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfpR-----RKSGPPRIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 213 VLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVD 290
Cdd:PRK11192  78 ILTPTRELAMQVADQARELAKhtHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 291 QMLDLGFAEQVEDIIHEsyktdSEDNPQTLLFSATCP-QWVYKVAKKYMK---------SRYEQvdlvGKMTQ--KAATT 358
Cdd:PRK11192 158 RMLDMGFAQDIETIAAE-----TRWRKQTLLFSATLEgDAVQDFAERLLNdpveveaepSRRER----KKIHQwyYRADD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 359 VEH-LAIQCHWSQRPAVigdvlqvysgseGRAIIFCETKKNVTEMA---------------------------------M 404
Cdd:PRK11192 229 LEHkTALLCHLLKQPEV------------TRSIVFVRTRERVHELAgwlrkaginccylegemvqakrneaikrltdgrV 296
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 405 NPHIKQDVES----------------------YIHRSGRTGRAGRTGICVCFYQPRERGQL----RYVEQK 449
Cdd:PRK11192 297 NVLVATDVAArgididdvshvinfdmprsadtYLHRIGRTGRAGRKGTAISLVEAHDHLLLgkieRYIEEP 367
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
136-339 1.14e-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: 144.51  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLA 215
Cdd:cd18046    1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS------LKATQALVLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAK------DFKDITrklSVACFyGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:cd18046   75 PTRELAQQIQKvvmalgDYMGIK---CHACI-GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568969017 290 DQMLDLGFAEQvediIHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYMK 339
Cdd:cd18046  151 DEMLSRGFKDQ----IYDIFQKLPPDT-QVVLLSATMPNDVLEVTTKFMR 195
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
159-325 2.39e-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: 143.88  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDIT----RK 234
Cdd:cd17961   19 LIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVLEQLTaycrKD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 235 LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtds 313
Cdd:cd17961   99 VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSYLPK--- 175
                        170
                 ....*....|..
gi 568969017 314 edNPQTLLFSAT 325
Cdd:cd17961  176 --NYQTFLMSAT 185
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
159-339 2.84e-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: 2.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIP-LIERLQrnQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRK-L 235
Cdd:cd17958   15 PIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDL--QPIPREQRnGPGVLVLTPTRELALQIEAECSKYSYKgL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 236 SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhesykTDSED 315
Cdd:cd17958   93 KSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKIL-----LDIRP 167
                        170       180
                 ....*....|....*....|....
gi 568969017 316 NPQTLLFSATCPQWVYKVAKKYMK 339
Cdd:cd17958  168 DRQTIMTSATWPDGVRRLAQSYLK 191
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
159-335 4.11e-38

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 140.24  E-value: 4.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITR--KLS 236
Cdd:cd17952   15 PIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-DQRELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKayNLR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 237 VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHEsyktdSEDN 316
Cdd:cd17952   94 VVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGH-----VRPD 168
                        170
                 ....*....|....*....
gi 568969017 317 PQTLLFSATCPQWVYKVAK 335
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 ...
136-325 6.42e-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: 6.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLqrnqetikkSRSPK---VL 212
Cdd:cd17955    1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL---------SEDPYgifAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 213 VLAPTRELANQVAKDFKDITRKLSVAC--FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSG---RLDLSKLRHVVLD 287
Cdd:cd17955   72 VLTPTRELAYQIAEQFRALGAPLGLRCcvIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLD 151
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568969017 288 EVDQMLDLGFAEQVEDIIHESYKTdsednPQTLLFSAT 325
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, ...
136-347 7.49e-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: 7.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLA 215
Cdd:cd18049   26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLERGDGPICLVLA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 293
Cdd:cd18049  105 PTRELAQQVQQVAAEYGRacRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568969017 294 DLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAKKYMKSrYEQVDL 347
Cdd:cd18049  185 DMGFEPQIRKIV-DQIRPDR----QTLMWSATWPKEVRQLAEDFLKD-YIHINI 232
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
135-460 8.57e-37

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 143.80  E-value: 8.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 135 AFSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVL 214
Cdd:PRK10590   2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 215 APTRELANQVAKDFKDITRKLSVACF--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQM 292
Cdd:PRK10590  82 TPTRELAAQIGENVRDYSKYLNIRSLvvFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 293 LDLGFaeqvediIHESYKTDSEDNP--QTLLFSAT------------------------------CPQWVYKVAKK---- 336
Cdd:PRK10590 162 LDMGF-------IHDIRRVLAKLPAkrQNLLFSATfsddikalaekllhnpleievarrntaseqVTQHVHFVDKKrkre 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 337 ---YM--KSRYEQVdLVGKMTQKAATtveHLAIQCHWS--QRPAVIGDVLQvysGSEGRAII-FCETKKNV---TEMAMN 405
Cdd:PRK10590 235 llsQMigKGNWQQV-LVFTRTKHGAN---HLAEQLNKDgiRSAAIHGNKSQ---GARTRALAdFKSGDIRVlvaTDIAAR 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568969017 406 -------PHI-----KQDVESYIHRSGRTGRAGRTG-----ICVcfyqpRERGQLRYVEQKAGITFKRVGVP 460
Cdd:PRK10590 308 gldieelPHVvnyelPNVPEDYVHRIGRTGRAAATGealslVCV-----DEHKLLRDIEKLLKKEIPRIAIP 374
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
145-325 2.72e-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: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetIKKSRSPKVLVLAPTRELANQV 224
Cdd:cd17942    1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK--FKPRNGTGVIIISPTRELALQI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 225 AKDFKDITRKLSVAC--FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSK-LRHVVLDEVDQMLDLGFAEQV 301
Cdd:cd17942   79 YGVAKELLKYHSQTFgiVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEEEM 158
                        170       180
                 ....*....|....*....|....
gi 568969017 302 EDIIHESYKTDsednpQTLLFSAT 325
Cdd:cd17942  159 RQIIKLLPKRR-----QTMLFSAT 177
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
136-449 2.74e-36

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 144.32  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIER-LQRNQETIKKSRSPKVLVL 214
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRlLSRPALADRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 215 APTRELANQVAKDFKDITRKLSV--ACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVDQ 291
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADLGLrfALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEADR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 292 MLDLGFaeqVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKsryEQVDLVGKMTQKAATTVEHlaiQCHWSQR 371
Cdd:PRK04537 171 MFDLGF---IKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMN---EPEKLVVETETITAARVRQ---RIYFPAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 372 PAVIGDVLQVYSGSEG-RAIIFCETKKNVTEMAMN---------------PHIKQ------------------------- 410
Cdd:PRK04537 242 EEKQTLLLGLLSRSEGaRTMVFVNTKAFVERVARTlerhgyrvgvlsgdvPQKKResllnrfqkgqleilvatdvaargl 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568969017 411 ---------------DVESYIHRSGRTGRAGRTGICVCFYQPRERGQL----RYVEQK 449
Cdd:PRK04537 322 hidgvkyvynydlpfDAEDYVHRIGRTARLGEEGDAISFACERYAMSLpdieAYIEQK 379
GUCT pfam08152
GUCT (NUC152) domain; This is the C terminal domain found in the RNA helicase II / Gu protein ...
514-608 2.89e-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: 131.12  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  514 GASSFEPRSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHD 593
Cdd:pfam08152   1 GYTEIKQRSLLSSEEGFVTLLLTSSREIRTPGYAWSILRRNLSEEIADKVKGMRLTKDKMGAVFDVPSELVEEFLAGWED 80
                          90
                  ....*....|....*.
gi 568969017  594 SD-WILSVPAKLPEIE 608
Cdd:pfam08152  81 SRgVTLEVATELPELQ 96
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
145-335 5.49e-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: 134.24  E-value: 5.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 145 TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKsrsPKV--LVLAPTRELAN 222
Cdd:cd17960    1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKK---GQVgaLIISPTRELAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 223 Q---VAKDF-KDITRKLSVACFYGGTSYQSQINQI-RNGIDILVGTPGRIKDHLQS--GRLDLSKLRHVVLDEVDQMLDL 295
Cdd:cd17960   78 QiyeVLQSFlEHHLPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568969017 296 GFAEQVEDIIHESYKtdsedNPQTLLFSATCPQWVYKVAK 335
Cdd:cd17960  158 GFEADLNRILSKLPK-----QRRTGLFSATQTDAVEELIK 192
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
136-335 9.44e-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: 9.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIkksrspKVLVLA 215
Cdd:cd17954    2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF------FALVLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDI--TRKLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGR-LDLSKLRHVVLDEVDQM 292
Cdd:cd17954   76 PTRELAQQISEQFEALgsSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568969017 293 LDLGFAEQVEDIIHESYKtdsedNPQTLLFSATCPQwvyKVAK 335
Cdd:cd17954  156 LNMDFEPEIDKILKVIPR-----ERTTYLFSATMTT---KVAK 190
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
159-347 1.95e-35

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: 135.14  E-value: 1.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQrNQETIKKSRSPKVLVLAPTRELANQV---AKDFKDITRkL 235
Cdd:cd18050   87 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLERGDGPICLVLAPTRELAQQVqqvADDYGKSSR-L 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 236 SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIhESYKTDSed 315
Cdd:cd18050  165 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV-DQIRPDR-- 241
                        170       180       190
                 ....*....|....*....|....*....|..
gi 568969017 316 npQTLLFSATCPQWVYKVAKKYMKSrYEQVDL 347
Cdd:cd18050  242 --QTLMWSATWPKEVRQLAEDFLRD-YVQINI 270
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
159-325 2.11e-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: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGP-VYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQET---IKKSRSPKVLVLAPTRELANQVAKDFKDITR- 233
Cdd:cd17946   15 PIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvGGKQKPLRALILTPTRELAVQVKDHLKAIAKy 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 234 -KLSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHV---VLDEVDQMLDLG-FAEqVEDIIHES 308
Cdd:cd17946   95 tNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLEKGhFAE-LEKILELL 173
                        170
                 ....*....|....*....
gi 568969017 309 YKTDSEDNP--QTLLFSAT 325
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, ...
149-340 2.96e-35

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


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 132.00  E-value: 2.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 149 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKDF 228
Cdd:cd17943    5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLER------RHPQVLILAPTREIAVQIHDVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 229 KDITRK---LSVACFYGGTSYQSQINQIrNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 305
Cdd:cd17943   79 KKIGKKlegLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568969017 306 HESYKtdsedNPQTLLFSATCPQWVYKVAKKYMKS 340
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 ...
149-339 3.70e-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: 131.90  E-value: 3.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 149 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERlqrnqeTIKKSRSPKVLVLAPTRELANQVAKDF 228
Cdd:cd17962    5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIR------CLTEHRNPSALILTPTRELAVQIEDQA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 229 KDITRKL---SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDII 305
Cdd:cd17962   79 KELMKGLppmKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568969017 306 HesyktDSEDNPQTLLFSATCPQWVYKVAKKYMK 339
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 ...
146-335 1.15e-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: 130.92  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 146 IKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIerLQRNQETIK----KSRSPKVLVLAPTRELA 221
Cdd:cd17951    2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI--MFALEQEKKlpfiKGEGPYGLIVCPSRELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 222 NQVAKDFKDITRKLS--------VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 293
Cdd:cd17951   80 RQTHEVIEYYCKALQeggypqlrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568969017 294 DLGFAEQVEDIIhESYKTDSednpQTLLFSATCPQWVYKVAK 335
Cdd:cd17951  160 DMGFEEDIRTIF-SYFKGQR----QTLLFSATMPKKIQNFAK 196
PTZ00424 PTZ00424
helicase 45; Provisional
160-448 1.89e-34

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 135.72  E-value: 1.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 160 IQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC 239
Cdd:PTZ00424  54 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD------LNACQALILAPTRELAQQIQKVVLALGDYLKVRC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 240 F--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQvediIHESYKTDSEDnP 317
Cdd:PTZ00424 128 HacVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQ----IYDVFKKLPPD-V 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 318 QTLLFSATCPQWVYKVAKKYMKS------RYEQVDLVG---------KMTQKAAT--------TVEHLAIQCHWSQRPAV 374
Cdd:PTZ00424 203 QVALFSATMPNEILELTTKFMRDpkrilvKKDELTLEGirqfyvaveKEEWKFDTlcdlyetlTITQAIIYCNTRRKVDY 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 375 IGDVLQ-----VYS-----GSEGRAIIFCETKKNVTE------------------MAMNPHIKQDVESYIHRSGRTGRAG 426
Cdd:PTZ00424 283 LTKKMHerdftVSCmhgdmDQKDRDLIMREFRSGSTRvlittdllargidvqqvsLVINYDLPASPENYIHRIGRSGRFG 362
                        330       340
                 ....*....|....*....|..
gi 568969017 427 RTGICVCFYQPRERGQLRYVEQ 448
Cdd:PTZ00424 363 RKGVAINFVTPDDIEQLKEIER 384
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
136-343 1.62e-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: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKksrspkVLVLA 215
Cdd:cd17950    4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS------VLVIC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDITRKL---SVACFYGGTSYQSQINQIRNGI-DILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQ 291
Cdd:cd17950   78 HTRELAFQISNEYERFSKYMpnvKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568969017 292 ML-DLGFAEQVEDIihesYKTDSEDNpQTLLFSATCPQWVYKVAKKYMKSRYE 343
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 ...
172-339 1.26e-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: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 172 KDLIAQARTGTGKTFSFAIPLIERLQRNqetikkSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYggtSYQSQIN 251
Cdd:cd17963   34 ENLIAQSQSGTGKTAAFVLAMLSRVDPT------LKSPQALCLAPTRELARQIGEVVEKMGKFTGVKVAL---AVPGNDV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 252 QIRNGID--ILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLFSATCPQ 328
Cdd:cd17963  105 PRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRI-----KRMLPRNCQILLFSATFPD 179
                        170
                 ....*....|.
gi 568969017 329 WVYKVAKKYMK 339
Cdd:cd17963  180 SVRKFAEKIAP 190
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
159-340 1.54e-32

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 132.22  E-value: 1.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIER--LQRNQEtIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL- 235
Cdd:PLN00206 146 PIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGH-PSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLp 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 236 -SVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHesyktdSE 314
Cdd:PLN00206 225 fKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ------AL 298
                        170       180
                 ....*....|....*....|....*.
gi 568969017 315 DNPQTLLFSATCPQWVYKVAKKYMKS 340
Cdd:PLN00206 299 SQPQVLLFSATVSPEVEKFASSLAKD 324
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
136-338 1.99e-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: 124.12  E-value: 1.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 136 FSNFSISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLierLQRNQETIkksRSPKVLVLA 215
Cdd:cd18045    1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISV---LQCLDIQV---RETQALILS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 216 PTRELANQVAKDFKDITRKLSVACF--YGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQML 293
Cdd:cd18045   75 PTRELAVQIQKVLLALGDYMNVQCHacIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568969017 294 DLGFAEQVEDIihesYKTdSEDNPQTLLFSATCPQWVYKVAKKYM 338
Cdd:cd18045  155 NKGFKEQIYDV----YRY-LPPATQVVLVSATLPQDILEMTNKFM 194
GUCT cd12929
RNA-binding GUCT domain found in the RNA helicase II/Gu protein family; This family includes ...
529-601 3.36e-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: 3.36e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969017 529 GFVTMTLESPEEIQDVSCAWKELNRKLSSNaVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWILSVP 601
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 ...
159-338 4.20e-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: 4.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 159 PIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRN-------QETIKKSRS---PKVLVLAPTRELANQV---A 225
Cdd:cd18051   46 PVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpSESGYYGRRkqyPLALVLAPTRELASQIydeA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 226 KDFKdiTRKLSVAC-FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI 304
Cdd:cd18051  126 RKFA--YRSRVRPCvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRI 203
                        170       180       190
                 ....*....|....*....|....*....|....
gi 568969017 305 IHESYKTDSEDNpQTLLFSATCPQWVYKVAKKYM 338
Cdd:cd18051  204 VEQDTMPPTGER-QTLMFSATFPKEIQMLARDFL 236
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
149-327 4.35e-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: 4.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 149 LKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKS-RSPKVLVLAPTRELANQVAKD 227
Cdd:cd17948    5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfNAPRGLVITPSRELAEQIGSV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 228 FKDITRKLS--VACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDI- 304
Cdd:cd17948   85 AQSLTEGLGlkVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFl 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 568969017 305 ----IHESYKTDSEDNP---QTLLFSATCP 327
Cdd:cd17948  165 rrfpLASRRSENTDGLDpgtQLVLVSATMP 194
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
146-325 2.05e-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: 122.36  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 146 IKLLKGRGVTYLFPIQVKT---------FGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetiKKSRSPKVLVLAP 216
Cdd:cd17956    2 LKNLQNNGITSAFPVQAAVipwllpsskSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSK-----RVVPRLRALIVVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 217 TRELANQVAKDFKDITR--KLSVACFYGGTSY---QSQINQIRNG-----IDILVGTPGRIKDHLQSGR-LDLSKLRHVV 285
Cdd:cd17956   77 TKELVQQVYKVFESLCKgtGLKVVSLSGQKSFkkeQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLV 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568969017 286 LDEVDQMLDLGF---AEQVEDIIHESYKTD------------SEDNPQTLLFSAT 325
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 ...
171-340 1.67e-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: 1.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 171 GKDLIAQARTGTGKTFSFAIPLIERLQrnqetikksrspkVLVLAPTRELANQVAKDFKDITR-----KLSVACFYGGTS 245
Cdd:cd17938   36 GGDVLMAAETGSGKTGAFCLPVLQIVV-------------ALILEPSRELAEQTYNCIENFKKyldnpKLRVALLIGGVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 246 YQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYK-TDSEDNPQTLLFSA 324
Cdd:cd17938  103 AREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPKiTSDGKRLQVIVCSA 182
                        170
                 ....*....|....*..
gi 568969017 325 TCPQW-VYKVAKKYMKS 340
Cdd:cd17938  183 TLHSFeVKKLADKIMHF 199
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
171-325 2.60e-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: 2.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 171 GKDLIAQARTGTGKTFSFAIPLIERLqrnqetikKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQSQ 249
Cdd:cd00046    1 GENVLITAPTGSGKTLAALLAALLLL--------LKKGKKVLVLVPTKALALQTAERLRELfGPGIRVAVLVGGSSAEER 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568969017 250 INQIRNGIDILVGTPGRI-KDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKtdsEDNPQTLLFSAT 325
Cdd:cd00046   73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAG---LKNAQVILLSAT 146
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
174-342 9.65e-22

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


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 95.14  E-value: 9.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 174 LIAqARTGTGKTFSFAIPLIERLQRNQ-----------ETIKKSRSPKVLVLAPTRELANQVAKDFKDI--TRKLSVACF 240
Cdd:cd17965   65 LLA-AETGSGKTLAYLAPLLDYLKRQEqepfeeaeeeyESAKDTGRPRSVILVPTHELVEQVYSVLKKLshTVKLGIKTF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 241 YG--GTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDsednpQ 318
Cdd:cd17965  144 SSgfGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLK-----H 218
                        170       180
                 ....*....|....*....|....
gi 568969017 319 TLLFSATCPqwvyKVAKKYMKSRY 342
Cdd:cd17965  219 LILCSATIP----KEFDKTLRKLF 238
GUCT_RH7_like cd12937
RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar ...
521-605 1.16e-16

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: 75.30  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 521 RSLITSDKGFVTMTLESPEEIQDVSCAWKELNRKLSSNAVSHVTRMCLLKGNMGVCFDVPTSESERLQAEWHDSDWI-LS 599
Cdd:cd12937    1 RSLLTSHEGYTTLLLKSNTPIRSPGYVWNALRRYLPEDIVESIKGMTLTADGKGAVFDVPSELIEEFLSAWVDKRGVtLE 80

                 ....*.
gi 568969017 600 VPAKLP 605
Cdd:cd12937   81 VATELP 86
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
128-289 3.12e-15

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: 79.49  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 128 TREQKEGAFSNF--SISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikk 205
Cdd:COG1205   26 TIPAREARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED------ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 206 sRSPKVLVLAPTRELAN-QVAKdFKDITRKL----SVACFYGGTSyQSQINQIRNGIDILVGTP-----GRIKDHLQSGR 275
Cdd:COG1205  100 -PGATALYLYPTKALARdQLRR-LRELAEALglgvRVATYDGDTP-PEERRWIREHPDIVLTNPdmlhyGLLPHHTRWAR 176
                        170
                 ....*....|....
gi 568969017 276 LdLSKLRHVVLDEV 289
Cdd:COG1205  177 F-FRNLRYVVIDEA 189
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
172-336 1.37e-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: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 172 KDLIAQARTGTGKTFSFAIPLIERLQRNQetikksRSPKVLVLAPTRELANQVAKdfkdITRKLSVACFYGGTSYQSQIN 251
Cdd:cd18048   58 QNLIAQSQSGTGKTAAFVLAMLSRVDALK------LYPQCLCLSPTFELALQTGK----VVEEMGKFCVGIQVIYAIRGN 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 252 QIRNGID----ILVGTPGRIKDHLQSGRL-DLSKLRHVVLDEVDQMLDL-GFAEQVEDIihesyKTDSEDNPQTLLFSAT 325
Cdd:cd18048  128 RPGKGTDieaqIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMINVqGHSDHSVRV-----KRSMPKECQMLLFSAT 202
                        170
                 ....*....|.
gi 568969017 326 CPQWVYKVAKK 336
Cdd:cd18048  203 FEDSVWAFAER 213
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
156-328 1.61e-12

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 66.52  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 156 YLFPIQVKTFGPVY-EGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrsPKVLVLAPTRELANQVAKDFKDITRK 234
Cdd:cd17921    1 LLNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSG--------GKAVYIAPTRALVNQKEADLRERFGP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 235 L--SVACFYGGTSyqSQINQIRNGiDILVGTPGRIKDHL-QSGRLDLSKLRHVVLDEVdQMLDLG-FAEQVEDIIheSYK 310
Cdd:cd17921   73 LgkNVGLLTGDPS--VNKLLLAEA-DILVATPEKLDLLLrNGGERLIQDVRLVVVDEA-HLIGDGeRGVVLELLL--SRL 146
                        170
                 ....*....|....*...
gi 568969017 311 TDSEDNPQTLLFSATCPQ 328
Cdd:cd17921  147 LRINKNARFVGLSATLPN 164
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
143-403 1.86e-10

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 63.76  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 143 EETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNqetikksrsPKVLVLAPTRELA 221
Cdd:COG1204    9 EKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNG---------GKALYIVPLRALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 222 NQVAKDFKDITRKL--SVACFYGGtsYQSQINQIRNGiDILVGTPGRIkDHLQSGRLD-LSKLRHVVLDEVdQMLDlgfA 298
Cdd:COG1204   80 SEKYREFKRDFEELgiKVGVSTGD--YDSDDEWLGRY-DILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-HLID---D 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 299 EQ----VEDIIheSYKTDSEDNPQTLLFSATCP------QWvykVAKKYMKSRYEQVDL-VGKMTQKAAttvehlaiqcH 367
Cdd:COG1204  152 ESrgptLEVLL--ARLRRLNPEAQIVALSATIGnaeeiaEW---LDAELVKSDWRPVPLnEGVLYDGVL----------R 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568969017 368 WSQRPAVIGDVLQVY----SGSEGRAIIFCETKKNVTEMA 403
Cdd:COG1204  217 FDDGSRRSKDPTLALaldlLEEGGQVLVFVSSRRDAESLA 256
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
161-288 5.16e-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: 5.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 161 QVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrspKVLVLAPTRELANQVAKDFKDITR----KLS 236
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS-------RALYLYPTKALAQDQLRSLRELLEqlglGIR 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568969017 237 VACFYGGTSYQSQINQIRNGIDILVGTP-----GRIKDHLQSGRLdLSKLRHVVLDE 288
Cdd:cd17923   78 VATYDGDTPREERRAIIRNPPRILLTNPdmlhyALLPHHDRWARF-LRNLRYVVLDE 133
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
359-435 1.31e-09

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: 56.75  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 359 VEHLAIQCHWSQRPAVIGdVLQVYSGSEGRAIIFCETKKNVTEMAMN--------------------------------- 405
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLL-LLLLEKLKPGKAIIFVNTKKRVDRLAELleelgikvaalhgdlsqeereralkkfrsgkvr 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568969017 406 --------------PHIK--------QDVESYIHRSGRTGRAGRTGICVCFY 435
Cdd:cd18787   80 vlvatdvaargldiPGVDhvinydlpRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
172-289 5.06e-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: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 172 KDLIAQARTGTGKTFsFAIPLIERLQRnqETIKKSRSPKVLV-LAPTRELANQVAKDFKDITrKLSVACFYGGTSYQSQI 250
Cdd:cd18034   17 RNTIVVLPTGSGKTL-IAVMLIKEMGE--LNRKEKNPKKRAVfLVPTVPLVAQQAEAIRSHT-DLKVGEYSGEMGVDKWT 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568969017 251 NQIRNG----IDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:cd18034   93 KERWKEelekYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
ResIII pfam04851
Type III restriction enzyme, res subunit;
180-289 1.42e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  180 TGTGKTF-SFAIplIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVAC-FYGGTSYqsqiNQIRNGI 257
Cdd:pfam04851  32 TGSGKTLtAAKL--IARL------FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGeIISGDKK----DESVDDN 99
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568969017  258 DILVGTPGRIKDHLQSGRLDLSKLRHVVL--DEV 289
Cdd:pfam04851 100 KIVVTTIQSLYKALELASLELLPDFFDVIiiDEA 133
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
161-288 3.10e-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: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 161 QVKTFGPVYEGKDLIAQARTGTGKTFsFAIPLIERLQRNqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRK--LSVA 238
Cdd:cd17927    7 QLELAQPALKGKNTIICLPTGSGKTF-VAVLICEHHLKK---FPAGRKGKVVFLANKVPLVEQQKEVFRKHFERpgYKVT 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568969017 239 CFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 288
Cdd:cd17927   83 GLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDE 133
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
172-336 7.57e-08

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 53.19  E-value: 7.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 172 KDLIAQARTGTGKTFSFAIPLIERLQrnqetiKKSRSPKVLVLAPTRELANQVAKDFKDITRklsvacFYGGTS--YQSQ 249
Cdd:cd18047   41 QNLIAQSQSGTGKTAAFVLAMLSQVE------PANKYPQCLCLSPTYELALQTGKVIEQMGK------FYPELKlaYAVR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 250 INQIRNGI----DILVGTPGRIKDH-LQSGRLDLSKLRHVVLDEVDQMLDL-GFAEQVEDIIHESYKtdsedNPQTLLFS 323
Cdd:cd18047  109 GNKLERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPR-----NCQMLLFS 183
                        170
                 ....*....|...
gi 568969017 324 ATCPQWVYKVAKK 336
Cdd:cd18047  184 ATFEDSVWKFAQK 196
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
128-294 5.85e-07

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 52.97  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 128 TREQKEGAFSNFSISEETIKLLKGRGvTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikks 206
Cdd:COG1202  182 TDEVDTVPVDDLDLPPELKDLLEGRG-EELLPVQSLAVeNGLLEGKDQLVVSATATGKTLIGELAGIKNALEGKG----- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 207 rspKVLVLAPTRELANQVAKDFKDITRK-LSVACFYGgtsyQSQI-----NQIRNGiDILVGTPGRIkDH-LQSGRlDLS 279
Cdd:COG1202  256 ---KMLFLVPLVALANQKYEDFKDRYGDgLDVSIRVG----ASRIrddgtRFDPNA-DIIVGTYEGI-DHaLRTGR-DLG 325
                        170
                 ....*....|....*
gi 568969017 280 KLRHVVLDEVdQMLD 294
Cdd:COG1202  326 DIGTVVIDEV-HMLE 339
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
180-289 8.64e-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: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 180 TGTGKTFsFAIPLIERLqrnqetikksRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGtsyqsqINQIRNGIDI 259
Cdd:cd17926   27 TGSGKTL-TALALIAYL----------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG------KKKDFDDANV 89
                         90       100       110
                 ....*....|....*....|....*....|
gi 568969017 260 LVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:cd17926   90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
170-289 8.84e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.95  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 170 EGKDLIAQARTGTGKTFsFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKditRKLSVACFYGGtsyqsq 249
Cdd:COG1061   99 GGGRGLVVAPTGTGKTV-LALALAAELLRGK---------RVLVLVPRRELLEQWAEELR---RFLGDPLAGGG------ 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568969017 250 inQIRNGIDILVGTPGRIKDHLQSGRLDlSKLRHVVLDEV 289
Cdd:COG1061  160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEA 196
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
157-289 1.18e-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: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 157 LFPIQVKTFGPVYEGKDLIAQARTGTGKTFSfAIPLIER-LQRNQETIKKSRspkVLVLAPTRELANQVA-KDFKDITRK 234
Cdd:cd18036    3 LRNYQLELVLPALRGKNTIICAPTGSGKTRV-AVYICRHhLEKRRSAGEKGR---VVVLVNKVPLVEQQLeKFFKYFRKG 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568969017 235 LSVACFYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQSG----RLDLSKLRHVVLDEV 289
Cdd:cd18036   79 YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGreeeRVYLSDFSLLIFDEC 137
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
171-294 1.62e-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: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 171 GKDLIAQARTGTGKTFSFAIPLIERLQRNQETikksrSPKVLVLAPTRELANQVAKDFK----DITRKLSVACFYGGTSY 246
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK-----GVQVLYISPLKALINDQERRLEepldEIDLEIPVAVRHGDTSQ 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568969017 247 QSQINQIRNGIDILVGTPGRIKDHLQSGRLD--LSKLRHVVLDEVDQMLD 294
Cdd:cd17922   76 SEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALLG 125
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
170-288 2.50e-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: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 170 EGKDLIAqARTGTGKTFSFAIPLIERLQRnqetiKKSrspKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGGTSYQS 248
Cdd:cd18035   16 NGNTLIV-LPTGLGKTIIAILVAADRLTK-----KGG---KVLILAPSRPLVEQHAENLKRVlNIPDKITSLTGEVKPEE 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568969017 249 QINQIRNGiDILVGTPGRIKDHLQSGRLDLSKLRHVVLDE 288
Cdd:cd18035   87 RAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDE 125
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
174-230 2.73e-06

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 50.61  E-value: 2.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568969017 174 LIAQArTGTGKTFSfAIPLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKD 230
Cdd:COG4096  182 LLVMA-TGTGKTRT-AIALIYRL------LKAGRAKRILFLADRNALVDQAKNAFKP 230
GUCT_Hera cd12938
RNA-binding GUCT-like domain found in Thermus thermophilus heat resistant RNA-dependent ATPase ...
520-590 6.06e-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: 6.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969017 520 PRSLITSDKGFVTMTLESPEEIQ--DVSCAWKELNRKLSSNavshVTRMCLLKGNMGVCFDVPTSESERLQAE 590
Cdd:cd12938    1 PRSLLTGEEGWTTLQLTGSRLLPpgSVRRAVGLLSRAAADG----VGKIRILADAGGAVFDLPEEIAKELLAK 69
PRK13766 PRK13766
Hef nuclease; Provisional
180-288 6.25e-06

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 49.49  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 180 TGTGKTfsfAIPLI---ERLQRNQEtikksrspKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIR 254
Cdd:PRK13766  38 TGLGKT---AIALLviaERLHKKGG--------KVLILAPTKPLVEQHAEFFRKFLNipEEKIVVFTGEVSPEKRAELWE 106
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568969017 255 NGiDILVGTPGRIKDHLQSGRLDLSKLRHVVLDE 288
Cdd:PRK13766 107 KA-KVIVATPQVIENDLIAGRISLEDVSLLIFDE 139
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
180-288 6.61e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 49.34  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 180 TGTGKTFSFAIPLIERLQRnqetikksRSPKVLVLAPTRELANQVAKDFKDITR--KLSVACFYGGTSYQSQINQIRNGi 257
Cdd:COG1111   26 TGLGKTAVALLVIAERLHK--------KGGKVLFLAPTKPLVEQHAEFFKEALNipEDEIVVFTGEVSPEKRKELWEKA- 96
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568969017 258 DILVGTPGRIKDHLQSGRLDLSKLRHVVLDE 288
Cdd:COG1111   97 RIIVATPQVIENDLIAGRIDLDDVSLLIFDE 127
PRK00254 PRK00254
ski2-like helicase; Provisional
141-289 1.49e-05

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 48.27  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 141 ISEETIKLLKGRGVTYLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRnqetikksRSPKVLVLAPTRE 219
Cdd:PRK00254   8 VDERIKRVLKERGIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR--------EGGKAVYLVPLKA 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568969017 220 LANQVAKDFKDITR-KLSVACFYGgtSYQSQiNQIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:PRK00254  80 LAEEKYREFKDWEKlGLRVAMTTG--DYDST-DEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEI 147
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
174-289 3.45e-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: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 174 LIAQArTGTGKTFSfAIPLIERLqrnqetIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSvACFYGGTSYQSQinqi 253
Cdd:cd18032   24 LLVMA-TGTGKTYT-AAFLIKRL------LEANRKKRILFLAHREELLEQAERSFKEVLPDGS-FGNLKGGKKKPD---- 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568969017 254 rnGIDILVGT----PGRIKDHLQS-GRLDLsklrhVVLDEV 289
Cdd:cd18032   91 --DARVVFATvqtlNKRKRLEKFPpDYFDL-----IIIDEA 124
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
170-235 1.66e-04

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 44.92  E-value: 1.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568969017 170 EGKDLIAQARTGTGKTFSFAIPLIERLQRNQEtikksrspKVLVLAPTRELANQ-VAKDFKDITRKL 235
Cdd:COG1199   32 EGRHLLIEAGTGTGKTLAYLVPALLAARETGK--------KVVISTATKALQEQlVEKDLPLLRKAL 90
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
173-325 2.63e-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: 42.40  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 173 DLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSyqsqiNQ 252
Cdd:cd17918   38 DRLLSGDVGSGKTLVALGAALLAYKNGK---------QVAILVPTEILAHQHYEEARKFLPFINVELVTGGTK-----AQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 253 IRNGIDILVGTpgrikdhlqsgrldlsklrHVVLDEVDQMLDLGFAeqvedIIHESYKTDSED--------NPQTLLFSA 324
Cdd:cd17918  104 ILSGISLLVGT-------------------HALLHLDVKFKNLDLV-----IVDEQHRFGVAQrealynlgATHFLEATA 159

                 .
gi 568969017 325 T 325
Cdd:cd17918  160 T 160
CMS1 pfam14617
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ...
201-287 5.48e-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: 42.16  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  201 ETIKKSRSPKVLVLAPTRELANQVAKDFKDI-TRKLSVACFYGG-TSYQSQINQIR-NGIDILVGTPGRIKDHLQSGRLD 277
Cdd:pfam14617 117 QRPKSNGSPHTLVLTIAALRAADVLRPLKKLqTKGFKVAKLFAKhIKLEEHITYCKaSRIGIGVGTPGRIADLLENESLS 196
                          90
                  ....*....|
gi 568969017  278 LSKLRHVVLD 287
Cdd:pfam14617 197 VDNLKYIILD 206
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
167-288 1.18e-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: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 167 PVYEGKDLIAQARTGTGKTF-SFAIplierLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKL--SVACFYGG 243
Cdd:cd18073   13 PAMKGKNTIICAPTGCGKTFvSLLI-----CEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHgyRVTGISGA 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568969017 244 TSYQSQINQIRNGIDILVGTPGRIKDHLQSGRL-DLSKLRHVVLDE 288
Cdd:cd18073   88 TAENVPVEQIIENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
156-289 1.24e-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: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 156 YLFPIQVKTF-GPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQetikksrspKVLVLAPTRELANQVAKDFKDITRK 234
Cdd:cd18028    1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---------KALYLVPLRALASEKYEEFKKLEEI 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568969017 235 -LSVACFYGgtSYQSQINQIRNgIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEV 289
Cdd:cd18028   72 gLKVGISTG--DYDEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEI 124
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
178-289 1.62e-03

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 41.83  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017  178 ARTGTGKTFSFAIPLIERLQRNQ----ETIKKSRSPKVLVLAPTRELANQVAKDFK--------------DITRKLSVAC 239
Cdd:PRK09751    3 APTGSGKTLAAFLYALDRLFREGgedtREAHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderrrrgETEVNLRVGI 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568969017  240 FYGGTSYQSQINQIRNGIDILVGTPGRIKDHLQS-GRLDLSKLRHVVLDEV 289
Cdd:PRK09751   83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLTSrARETLRGVETVIIDEV 133
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
160-289 3.43e-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: 39.26  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568969017 160 IQVKTFGPVYEG-KDLIAQARTGTGKT--FSFAIplierLQRNQETIKKSR-SPKVLVLAPTRELANQVAKDFKDITRKL 235
Cdd:cd18023    5 IQSEVFPDLLYSdKNFVVSAPTGSGKTvlFELAI-----LRLLKERNPLPWgNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568969017 236 SVAC--FYGGTSYQSqINQIRNgIDILVGTPG-------RIKDHlqsGRLdLSKLRHVVLDEV 289
Cdd:cd18023   80 GLSCaeLTGDTEMDD-TFEIQD-ADIILTTPEkwdsmtrRWRDN---GNL-VQLVALVLIDEV 136
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
180-230 6.33e-03

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 39.65  E-value: 6.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568969017 180 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 230
Cdd:PRK05298  41 TGSGKTFTMA-NVIARLQR-----------PTLVLAHNKTLAAQLYSEFKE 79
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
180-230 6.84e-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: 6.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568969017 180 TGTGKTFSFAiPLIERLQRnqetikksrspKVLVLAPTRELANQVAKDFKD 230
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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