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Conserved domains on  [gi|1622946382|ref|XP_028705494|]
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3'-5' RNA helicase YTHDC2 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 31-206 2.51e-120

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 370.31  E-value: 2.51e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17987     81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160

                          170
                   ....*....|....*.
gi 1622946382  191 VNLFLRYFGSCPVIYI 206
Cdd:cd17987    161 VNLFIRYFGSCPVIYI 176
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
26-786 3.86e-83

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 290.83  E-value: 3.86e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   26 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRE 104
Cdd:COG1643      5 TYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGG---RIGMLEPRRLAARAAAERMAEELGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  105 RIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKhptlklil 184
Cdd:COG1643     82 PVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQR-DPELEGVDTVIFDEFHERSLNADLLLALLLDLQPA-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  185 ssaaldvnlfLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKykkekqqeekqqttltewysaqentfkpes 264
Cdd:COG1643    153 ----------LR----------------------PD------------LK------------------------------ 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  265 qrqrtvpnvtdeydllddggdavfsqltekdvnclepwlikemdaclsdiwlhkdidafaqvfhLILTenvsvdyrhset 344
Cdd:COG1643    159 ----------------------------------------------------------------LLVM------------ 162

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  345 SATalmvaagrgfasqveqlismganvhskasngwmaLD---WAKHFGQTEIVdllesysaslefgnldESS----LVQT 417
Cdd:COG1643    163 SAT----------------------------------LDaerFARLLGDAPVI----------------ESSgrtyPVEV 192

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  418 NGSDLSAEDRELLKAyhhsfddekVdLDLIMHLLYNichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVF 497
Cdd:COG1643    193 RYRPLPADERDLEDA---------V-ADAVREALAE-----EPGDILVFLPGEREIRRTAEAL---RGRLPPDT---EIL 251

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  498 MLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 577
Cdd:COG1643    252 PLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGR 331

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  578 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLapvNCP-IADFLMkaPEPPPALIVRNAVQMLKTIDA 656
Cdd:COG1643    332 AGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAW---GLGdPEDLPF--LDPPPARAIADARALLQELGA 406

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  657 MDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptqasqkraamlcrkRFTAGafSDHM 736
Cdd:COG1643    407 LDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-----------------RGAAG--SDLL 467

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622946382  737 ALLRAFQAWQKARsdgwerafceKNFLSQATMEIIIGMRTQLLGQLRASG 786
Cdd:COG1643    468 ARLNLWRRLREQQ----------REFLSYLRLREWRDLARQLRRLLGEGA 507
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
 1127-1256 3.58e-64

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


:

Pssm-ID: 410979  Cd Length: 133  Bit Score: 213.58  E-value: 3.58e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382 1127 RYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKS---QDWGSAGL 1203
Cdd:cd21134      1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSpswPWWSQDKL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622946382 1204 GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLW 1256
Cdd:cd21134     81 GGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 809-904 3.51e-12

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 63.04  E-value: 3.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  809 VKAALVAGMYPNLVHVDRENLVLTGPKEK-KVRFHPASVLSQPqyKKIPPAngqaaaikalptdWLIYDEMTRAHRIAnI 887
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNqRVFIHPSSVLFNE--KTFPPE-------------WVVYQELVETTKVY-I 64

                           90
                   ....*....|....*..
gi 1622946382  888 RCCSAVTPVTILVFCGP 904
Cdd:pfam07717   65 RTVTAISPEWLLLFAPH 81
 
Name Accession Description Interval E-value
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 31-206 2.51e-120

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 370.31  E-value: 2.51e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17987     81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160

                          170
                   ....*....|....*.
gi 1622946382  191 VNLFLRYFGSCPVIYI 206
Cdd:cd17987    161 VNLFIRYFGSCPVIYI 176
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
26-786 3.86e-83

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 290.83  E-value: 3.86e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   26 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRE 104
Cdd:COG1643      5 TYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGG---RIGMLEPRRLAARAAAERMAEELGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  105 RIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKhptlklil 184
Cdd:COG1643     82 PVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQR-DPELEGVDTVIFDEFHERSLNADLLLALLLDLQPA-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  185 ssaaldvnlfLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKykkekqqeekqqttltewysaqentfkpes 264
Cdd:COG1643    153 ----------LR----------------------PD------------LK------------------------------ 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  265 qrqrtvpnvtdeydllddggdavfsqltekdvnclepwlikemdaclsdiwlhkdidafaqvfhLILTenvsvdyrhset 344
Cdd:COG1643    159 ----------------------------------------------------------------LLVM------------ 162

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  345 SATalmvaagrgfasqveqlismganvhskasngwmaLD---WAKHFGQTEIVdllesysaslefgnldESS----LVQT 417
Cdd:COG1643    163 SAT----------------------------------LDaerFARLLGDAPVI----------------ESSgrtyPVEV 192

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  418 NGSDLSAEDRELLKAyhhsfddekVdLDLIMHLLYNichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVF 497
Cdd:COG1643    193 RYRPLPADERDLEDA---------V-ADAVREALAE-----EPGDILVFLPGEREIRRTAEAL---RGRLPPDT---EIL 251

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  498 MLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 577
Cdd:COG1643    252 PLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGR 331

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  578 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLapvNCP-IADFLMkaPEPPPALIVRNAVQMLKTIDA 656
Cdd:COG1643    332 AGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAW---GLGdPEDLPF--LDPPPARAIADARALLQELGA 406

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  657 MDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptqasqkraamlcrkRFTAGafSDHM 736
Cdd:COG1643    407 LDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-----------------RGAAG--SDLL 467

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622946382  737 ALLRAFQAWQKARsdgwerafceKNFLSQATMEIIIGMRTQLLGQLRASG 786
Cdd:COG1643    468 ARLNLWRRLREQQ----------REFLSYLRLREWRDLARQLRRLLGEGA 507
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 435-590 1.90e-72

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


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 238.59  E-value: 1.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  435 HSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRDRILfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKN 514
Cdd:cd18791     18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLR--EELLSPDLGKLLVLPLHSSLPPEEQQRVFEP 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946382  515 PPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLF 590
Cdd:cd18791     96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 26-856 6.21e-66

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 244.97  E-value: 6.21e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   26 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRER 105
Cdd:PRK11131    68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELETE 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  106 IGQTIGYQIRLESRVSPKTLLTFCTNGVLL------RTLMAGDStlstvthVIVDEVHERDRFSDFLLTKLRDLLQKHPT 179
Cdd:PRK11131   146 LGGCVGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLMQYDT-------IIIDEAHERSLNIDFILGYLKELLPRRPD 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  180 LKLILSSAALDVNLFLRYFGSCPVIYIQGR--PFEVkemfledilrttgytnkemlkykkekqqeekqqttltewysaqe 257
Cdd:PRK11131   219 LKVIITSATIDPERFSRHFNNAPIIEVSGRtyPVEV-------------------------------------------- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  258 ntfkpesqRQRtvPNVTDEYDLLDDGGDAVFsqltekdvnclepwlikemDAclsdiwlhkdidafaqvfhliltenvsV 337
Cdd:PRK11131   255 --------RYR--PIVEEADDTERDQLQAIF-------------------DA---------------------------V 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  338 DYRHSEtsatalmvaaGRGfasqvEQLISMGanvhskasngwmaldwakhfGQTEIVDLLESysaslefgnLDESSLVQT 417
Cdd:PRK11131   279 DELGRE----------GPG-----DILIFMS--------------------GEREIRDTADA---------LNKLNLRHT 314

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  418 ngsdlsaedrellkayhhsfddekvdldlimhllynichscdagavliflpgydEIVGLRDRIlfddkrfadsthryqvf 497
Cdd:PRK11131   315 ------------------------------------------------------EILPLYARL----------------- 323

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  498 mlhSNmqtSDQKKVLKnpPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 577
Cdd:PRK11131   324 ---SN---SEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  578 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNcpIADFlmkaP--EPPPALIVRNAVQMLKTID 655
Cdd:PRK11131   396 CGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGD--IAAF----PfvEAPDKRNIQDGVRLLEELG 469

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  656 AMDTWED-----LTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPT---QASQKRaamlcRKRF 727
Cdd:PRK11131   470 AITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkqQASDEK-----HRRF 544

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  728 tAGAFSDHMALLRAF---QAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFvrargggdirDVNTNSE 804
Cdd:PRK11131   545 -ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGI----------PVNSEPA 613

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946382  805 NWAVVKAALVAGMypnLVHV---DRENLVLTGPkeKKVRFH--PASVLsqpqYKKIP 856
Cdd:PRK11131   614 EYREIHTALLTGL---LSHIgmkDAEKQEYTGA--RNARFSifPGSGL----FKKPP 661
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
 1127-1256 3.58e-64

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


Pssm-ID: 410979  Cd Length: 133  Bit Score: 213.58  E-value: 3.58e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382 1127 RYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKS---QDWGSAGL 1203
Cdd:cd21134      1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSpswPWWSQDKL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622946382 1204 GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLW 1256
Cdd:cd21134     81 GGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
YTH pfam04146
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ...
 1126-1257 4.66e-60

YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.


Pssm-ID: 461195  Cd Length: 135  Bit Score: 201.96  E-value: 4.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382 1126 VRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQ-DWGSAGL- 1203
Cdd:pfam04146    1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFiFWEADSDk 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622946382 1204 -GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWE 1257
Cdd:pfam04146   81 wGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLFD 135
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 647-738 1.71e-27

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 107.71  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  647 AVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKR 726
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80

                           90       100
                   ....*....|....*....|....
gi 1622946382  727 FTA------------GAFSDHMAL 738
Cdd:pfam04408   81 RRAadekarakfarlDLEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
37-210 7.23e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 7.23e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382    37 QEEIVKIIKEN-KVVLIVGETGSGKTTQIPQFLLdDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGY--- 112
Cdd:smart00487   13 QKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL-EALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   113 ---QIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDR--FSDFLLTKLRDLlqkHPTLKLILSSA 187
Cdd:smart00487   92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLL---PKNVQLLLLSA 168

                           170       180
                    ....*....|....*....|....*
gi 1622946382   188 ALDVNL--FLRYFGSCPVIYIQGRP 210
Cdd:smart00487  169 TPPEEIenLLELFLNDPVFIDVGFT 193
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 654-739 5.41e-18

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 79.62  E-value: 5.41e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   654 IDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptQASQKRAAMLCRKRFtAGAFS 733
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR----PKEKREDADAARRRF-ADPES 76


                    ....*.
gi 1622946382   734 DHMALL 739
Cdd:smart00847   77 DHLTLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 809-904 3.51e-12

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 63.04  E-value: 3.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  809 VKAALVAGMYPNLVHVDRENLVLTGPKEK-KVRFHPASVLSQPqyKKIPPAngqaaaikalptdWLIYDEMTRAHRIAnI 887
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNqRVFIHPSSVLFNE--KTFPPE-------------WVVYQELVETTKVY-I 64

                           90
                   ....*....|....*..
gi 1622946382  888 RCCSAVTPVTILVFCGP 904
Cdd:pfam07717   65 RTVTAISPEWLLLFAPH 81
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 3-217 2.79e-08

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 58.07  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382    3 KTSGRLNNGIPQIPVKrgesefdsFRQSLPvfEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFL-----LDDCFKN-G 76
Cdd:PHA02653   145 DTIGILGNPEPFSKIP--------LASLQP--DVQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnyLFGGFDNlD 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   77 IPCRIFCTQPRRLAAiavaERVAAERRERIG--QTIGYQIRLESRVSPK---------------TLLTFCTNGVLLRTLM 139
Cdd:PHA02653   215 KIDPNFIERPIVLSL----PRVALVRLHSITllKSLGFDEIDGSPISLKygsipdelintnpkpYGLVFSTHKLTLNKLF 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  140 AGDStlstvthVIVDEVHERDRFSDFLLTKLRdllqKHPTL--KLILSSAAL--DVNLFLRYFGSCPVIYIQGRP-FEVK 214
Cdd:PHA02653   291 DYGT-------VIIDEVHEHDQIGDIIIAVAR----KHIDKirSLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPIS 359


                   ...
gi 1622946382  215 EMF 217
Cdd:PHA02653   360 EVY 362
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 37-193 8.54e-08

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: 53.02  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   37 QEEIVKIIKENKVVLIVGETGSGKTT--QIPqfLLDDCFKNGIPCRIFCTQPRR-LAA--IAVAERVAAERRERI----- 106
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTReLAEqiYEELKKLGKGLGLKVasllg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  107 GQTIGYQIRLESRVSpktlLTFCTNGVLLrTLMAGDSTLSTVTHVIVDEVHE--RDRFSDFLLTKLRDLLQKHPTLKLil 184
Cdd:pfam00270   82 GDSRKEQLEKLKGPD----ILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRLPKKRQILLL-- 154


                   ....*....
gi 1622946382  185 sSAALDVNL 193
Cdd:pfam00270  155 -SATLPRNL 162
 
Name Accession Description Interval E-value
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 31-206 2.51e-120

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 370.31  E-value: 2.51e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17987     81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160

                          170
                   ....*....|....*.
gi 1622946382  191 VNLFLRYFGSCPVIYI 206
Cdd:cd17987    161 VNLFIRYFGSCPVIYI 176
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 47-206 1.86e-87

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 280.11  E-value: 1.86e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   47 NKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLL 126
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  127 TFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFLRYFGSCPVIYI 206
Cdd:cd17917     81 KFCTDGILLRELL-SDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
26-786 3.86e-83

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 290.83  E-value: 3.86e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   26 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRE 104
Cdd:COG1643      5 TYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGG---RIGMLEPRRLAARAAAERMAEELGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  105 RIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKhptlklil 184
Cdd:COG1643     82 PVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQR-DPELEGVDTVIFDEFHERSLNADLLLALLLDLQPA-------- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  185 ssaaldvnlfLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKykkekqqeekqqttltewysaqentfkpes 264
Cdd:COG1643    153 ----------LR----------------------PD------------LK------------------------------ 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  265 qrqrtvpnvtdeydllddggdavfsqltekdvnclepwlikemdaclsdiwlhkdidafaqvfhLILTenvsvdyrhset 344
Cdd:COG1643    159 ----------------------------------------------------------------LLVM------------ 162

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  345 SATalmvaagrgfasqveqlismganvhskasngwmaLD---WAKHFGQTEIVdllesysaslefgnldESS----LVQT 417
Cdd:COG1643    163 SAT----------------------------------LDaerFARLLGDAPVI----------------ESSgrtyPVEV 192

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  418 NGSDLSAEDRELLKAyhhsfddekVdLDLIMHLLYNichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVF 497
Cdd:COG1643    193 RYRPLPADERDLEDA---------V-ADAVREALAE-----EPGDILVFLPGEREIRRTAEAL---RGRLPPDT---EIL 251

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  498 MLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 577
Cdd:COG1643    252 PLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGR 331

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  578 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLapvNCP-IADFLMkaPEPPPALIVRNAVQMLKTIDA 656
Cdd:COG1643    332 AGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAW---GLGdPEDLPF--LDPPPARAIADARALLQELGA 406

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  657 MDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptqasqkraamlcrkRFTAGafSDHM 736
Cdd:COG1643    407 LDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR-----------------RGAAG--SDLL 467

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622946382  737 ALLRAFQAWQKARsdgwerafceKNFLSQATMEIIIGMRTQLLGQLRASG 786
Cdd:COG1643    468 ARLNLWRRLREQQ----------REFLSYLRLREWRDLARQLRRLLGEGA 507
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 435-590 1.90e-72

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


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 238.59  E-value: 1.90e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  435 HSFDDEKVDLDLIMHLLYNICHSCDAGAVLIFLPGYDEIVGLRDRILfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKN 514
Cdd:cd18791     18 SSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLR--EELLSPDLGKLLVLPLHSSLPPEEQQRVFEP 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946382  515 PPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLF 590
Cdd:cd18791     96 PPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 31-206 8.77e-70

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to 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: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 231.27  E-value: 8.77e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIP--CRIFCTQPRRLAAIAVAERVAAERRERIGQ 108
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLpvANIICTQPRRISAISVAERVAQERAERVGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  109 TIGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAA 188
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSAT 159

                          170
                   ....*....|....*...
gi 1622946382  189 LDVNLFLRYFGSCPVIYI 206
Cdd:cd17985    160 LNAELFSDYFNSCPVIHI 177
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 26-856 6.21e-66

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 244.97  E-value: 6.21e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   26 SFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRER 105
Cdd:PRK11131    68 TYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELETE 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  106 IGQTIGYQIRLESRVSPKTLLTFCTNGVLL------RTLMAGDStlstvthVIVDEVHERDRFSDFLLTKLRDLLQKHPT 179
Cdd:PRK11131   146 LGGCVGYKVRFNDQVSDNTMVKLMTDGILLaeiqqdRLLMQYDT-------IIIDEAHERSLNIDFILGYLKELLPRRPD 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  180 LKLILSSAALDVNLFLRYFGSCPVIYIQGR--PFEVkemfledilrttgytnkemlkykkekqqeekqqttltewysaqe 257
Cdd:PRK11131   219 LKVIITSATIDPERFSRHFNNAPIIEVSGRtyPVEV-------------------------------------------- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  258 ntfkpesqRQRtvPNVTDEYDLLDDGGDAVFsqltekdvnclepwlikemDAclsdiwlhkdidafaqvfhliltenvsV 337
Cdd:PRK11131   255 --------RYR--PIVEEADDTERDQLQAIF-------------------DA---------------------------V 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  338 DYRHSEtsatalmvaaGRGfasqvEQLISMGanvhskasngwmaldwakhfGQTEIVDLLESysaslefgnLDESSLVQT 417
Cdd:PRK11131   279 DELGRE----------GPG-----DILIFMS--------------------GEREIRDTADA---------LNKLNLRHT 314

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  418 ngsdlsaedrellkayhhsfddekvdldlimhllynichscdagavliflpgydEIVGLRDRIlfddkrfadsthryqvf 497
Cdd:PRK11131   315 ------------------------------------------------------EILPLYARL----------------- 323

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  498 mlhSNmqtSDQKKVLKnpPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGR 577
Cdd:PRK11131   324 ---SN---SEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  578 AGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNcpIADFlmkaP--EPPPALIVRNAVQMLKTID 655
Cdd:PRK11131   396 CGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGD--IAAF----PfvEAPDKRNIQDGVRLLEELG 469

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  656 AMDTWED-----LTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPT---QASQKRaamlcRKRF 727
Cdd:PRK11131   470 AITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkqQASDEK-----HRRF 544

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  728 tAGAFSDHMALLRAF---QAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFvrargggdirDVNTNSE 804
Cdd:PRK11131   545 -ADKESDFLAFVNLWnylQEQQKALSSNQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGI----------PVNSEPA 613

                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622946382  805 NWAVVKAALVAGMypnLVHV---DRENLVLTGPkeKKVRFH--PASVLsqpqYKKIP 856
Cdd:PRK11131   614 EYREIHTALLTGL---LSHIgmkDAEKQEYTGA--RNARFSifPGSGL----FKKPP 661
YTH cd21134
YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; ...
 1127-1256 3.58e-64

YTH (YT521-B homology) domains are RNA-binding domains that belong to the PUA superfamily; Individual members of the YTH family have been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. In general, eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or in other forms of silencing. The YTH domain is a novel RNA-binding domain that has been shown to bind to short, degenerate, single-stranded RNA motifs that loosely follow a consensus sequence. It belongs to the larger PUA superfamily.


Pssm-ID: 410979  Cd Length: 133  Bit Score: 213.58  E-value: 3.58e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382 1127 RYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKS---QDWGSAGL 1203
Cdd:cd21134      1 RFFIIKSNNEENIHLSIKYGVWATQPHNEKKLNQAFRESGNVYLIFSVNGSGHFQGYARMTSPPDPNRSpswPWWSQDKL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622946382 1204 GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLW 1256
Cdd:cd21134     81 GGPFKVEWLRVKDLPFSKLRHLKNPLNENKPVTISRDGQEIEPEVGEQLLKLF 133
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 23-204 2.24e-62

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to 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: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 212.39  E-value: 2.24e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   23 EFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKN--GIPCRIFCTQPRRLAAIAVAERVAA 100
Cdd:cd17972     51 QILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNdrAAECNIVVTQPRRISAVSVAERVAF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  101 ERRERIGQTIGYQIRLESRV-SPKTLLTFCTNGVLLRTLMAGdstLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT 179
Cdd:cd17972    131 ERGEEVGKSCGYSVRFESVLpRPHASILFCTVGVLLRKLEAG---IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPD 207

                          170       180
                   ....*....|....*....|....*
gi 1622946382  180 LKLILSSAALDVNLFLRYFGSCPVI 204
Cdd:cd17972    208 LRVILMSATIDTSMFCEYFFNCPVI 232
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 31-206 3.22e-61

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to 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: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 207.00  E-value: 3.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGI--PCRIFCTQPRRLAAIAVAERVAAERRE--RI 106
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKgsSCRIVCTQPRRISAISVAERVAAERAEscGL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  107 GQTIGYQIRLESRVSPK-TLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILS 185
Cdd:cd17981     81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQS-DPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159

                          170       180
                   ....*....|....*....|.
gi 1622946382  186 SAALDVNLFLRYFGSCPVIYI 206
Cdd:cd17981    160 SATLNAEKFSDYFNNCPMIHI 180
YTH pfam04146
YT521-B-like domain; A protein of the YTH family has been shown to selectively remove ...
 1126-1257 4.66e-60

YT521-B-like domain; A protein of the YTH family has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells. It has been speculated that in higher eukaryotic YTH-family members may be involved in similar mechanisms to suppress gene regulation during gametogenesis or general silencing. The rat protein YT521-B is a tyrosine-phosphorylated nuclear protein, that interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. The YTH domain has been identified as part of the PUA superfamily.


Pssm-ID: 461195  Cd Length: 135  Bit Score: 201.96  E-value: 4.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382 1126 VRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQ-DWGSAGL- 1203
Cdd:pfam04146    1 ARFFIIKSLNEENIHLSIKYGIWATQPHNNKRLNEAFKESKNVYLIFSVNKSGHFQGYARMTSPVDFDPSFiFWEADSDk 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622946382 1204 -GGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWE 1257
Cdd:pfam04146   81 wGGPFKVEWLSVKDLPFSRLRHLRNPLNENKPVKISRDGQEIEPEVGRQLLKLFD 135
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 31-206 2.11e-57

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 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: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 196.29  E-value: 2.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNG---IPCRIFCTQPRRLAAIAVAERVAAERRERIG 107
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGgtaQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  108 -----QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKL 182
Cdd:cd17975     81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQE-DGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHL 159

                          170       180
                   ....*....|....*....|....
gi 1622946382  183 ILSSAALDVNLFLRYFGSCPVIYI 206
Cdd:cd17975    160 ILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 31-206 6.31e-56

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to 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: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 191.93  E-value: 6.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF--KNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQ 108
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVlrGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  109 TIGYQIRLESRVSPKT-LLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 187
Cdd:cd17976     81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQ-SNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSA 159

                          170
                   ....*....|....*....
gi 1622946382  188 ALDVNLFLRYFGSCPVIYI 206
Cdd:cd17976    160 TGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 31-206 1.91e-54

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to 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: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 187.56  E-value: 1.91e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGIpcrIFCTQPRRLAAIAVAERVAAERRERIGQT 109
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFaRGGM---IGITQPRRVAAVSVAKRVAEEMGVELGQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  110 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRD-----LLQKHPTLKLIL 184
Cdd:cd17978     78 VGYSVRFDDVTSEETRIKYMTDGMLLREAI-GDPLLSKYSVIILDEAHERTVHTDVLFGLVKSaqrrrKEQKLSPLKVII 156

                          170       180
                   ....*....|....*....|..
gi 1622946382  185 SSAALDVNLFLRYFGSCPVIYI 206
Cdd:cd17978    157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 28-206 5.10e-54

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to 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: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 186.85  E-value: 5.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   28 RQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIG 107
Cdd:cd17973     10 RRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDVKLG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  108 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 187
Cdd:cd17973     90 EEVGYSIRFEDCSSAKTILKYMTDGMLLREAMS-DPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIVMSA 168

                          170
                   ....*....|....*....
gi 1622946382  188 ALDVNLFLRYFGSCPVIYI 206
Cdd:cd17973    169 TLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 31-204 2.76e-53

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to 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: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 183.80  E-value: 2.76e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNgipcrIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH-----IACTQPRRIACISLAKRVAFESLNQYGSKV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17979     76 AYQIRFERTRTLATKLLFLTEGLLLRQ-IQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATIN 154

                          170
                   ....*....|....
gi 1622946382  191 VNLFLRYFGSCPVI 204
Cdd:cd17979    155 IELFSGYFEGAPVV 168
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 31-206 1.18e-51

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to 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: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 179.58  E-value: 1.18e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGIpcrIFCTQPRRLAAIAVAERVAAERRERIGQT 109
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYtDYGM---IGCTQPRRVAAMSVAKRVSEEMGVELGEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  110 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAAL 189
Cdd:cd17983     78 VGYAIRFEDCTSENTVIKYMTDGILLRESL-RDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156

                          170
                   ....*....|....*..
gi 1622946382  190 DVNLFLRYFGSCPVIYI 206
Cdd:cd17983    157 DADKFADFFGNVPIFTI 173
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 31-200 1.50e-51

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to 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: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 179.23  E-value: 1.50e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT-LKLILSSAAL 189
Cdd:cd17988     81 GYQVGLERPASEETRLIYCTTGVLLQKLIN-NKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATI 159

                          170
                   ....*....|.
gi 1622946382  190 DVNLFLRYFGS 200
Cdd:cd17988    160 SCKEFADYFTT 170
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 28-206 5.14e-50

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to 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: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 174.98  E-value: 5.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   28 RQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNgiPCRIFCTQPRRLAAIAVAERVAAERRERIG 107
Cdd:cd17971      3 RESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTS--RGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  108 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSA 187
Cdd:cd17971     81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLI-DPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSA 159

                          170
                   ....*....|....*....
gi 1622946382  188 ALDVNLFLRYFGSCPVIYI 206
Cdd:cd17971    160 TLDAVKFSQYFYEAPIFTI 178
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 31-206 1.19e-49

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to 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: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 173.84  E-value: 1.19e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPcRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG-KIGCTQPRRVAAMSVAARVAEEMGVKLGNEV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17974     80 GYSIRFEDCTSEKTVLKYMTDGMLLREFL-TEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMD 158

                          170
                   ....*....|....*.
gi 1622946382  191 VNLFLRYFGSCPVIYI 206
Cdd:cd17974    159 AEKFSAFFDDAPIFRI 174
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 31-204 2.29e-48

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to 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: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 169.94  E-value: 2.29e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDdcFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALD 190
Cdd:cd17989     79 GYKVRFTDQTSDETCVKLMTDGILLAE-TQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATID 157

                          170
                   ....*....|....
gi 1622946382  191 VNLFLRYFGSCPVI 204
Cdd:cd17989    158 AERFSRHFNNAPII 171
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 31-198 8.36e-46

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to 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: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 163.02  E-value: 8.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCrIFCTQPRRLAAIAVAERVAAERRERIGQTI 110
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRV-VGCTQPRRVAAVTVAGRVAEEMGAVLGHEV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  111 GYQIRLESRVSP-KTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAAL 189
Cdd:cd17980     80 GYCIRFDDCTDPqATRIKFLTDGMLVREMML-DPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATL 158


                   ....*....
gi 1622946382  190 DVNLFLRYF 198
Cdd:cd17980    159 DAEKFRDFF 167
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 31-195 8.35e-43

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to 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: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 154.82  E-value: 8.35e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF---KNGIPCRIFCTQPRRLAAIAVAERVAAErRERIG 107
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFgspESDNPGMIGITQPRRVAAVSMAKRVAEE-LNVFG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  108 QTIGYQIRLESRVSPKTLLTFCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLL----------TKLRDLLQKH 177
Cdd:cd17982     80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKE-IQTDFLLRKYSVIIIDEAHERSVNTDILIgmlsrivplrAKLYLQDQTV 158

                          170
                   ....*....|....*...
gi 1622946382  178 PTLKLILSSAALDVNLFL 195
Cdd:cd17982    159 KPLKLVIMSATLRVEDFT 176
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 30-686 1.08e-39

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 159.32  E-value: 1.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   30 SLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIP-QFLLddcfKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQ 108
Cdd:PRK11664     3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQ----HGGINGKIIMLEPRRLAARNVAQRLAEQLGEKPGE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  109 TIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHErdrfsdflltklRDLlqkHPTLKLILssaA 188
Cdd:PRK11664    79 TVGYRMRAESKVGPNTRLEVVTEGILTRMIQR-DPELSGVGLVILDEFHE------------RSL---QADLALAL---L 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  189 LDVNLFLRyfgscpviyiqgrpfevkemflEDilrttgytnkemLKYkkekqqeekqqttltewysaqentfkpesqrqr 268
Cdd:PRK11664   140 LDVQQGLR----------------------DD------------LKL--------------------------------- 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  269 tvpnvtdeydllddggdavfsqltekdvnclepwLIkeMDACLsdiwlhkDIDAFAQvfhlILTEnvsvdyrhsetsaTA 348
Cdd:PRK11664   153 ----------------------------------LI--MSATL-------DNDRLQQ----LLPD-------------AP 172

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  349 LMVAAGRGFAsqVE-QLISMGANVHskasngwmaldwakhfgqteivdllesysaslefgnLDESSLVQTngsdlsaedR 427
Cdd:PRK11664   173 VIVSEGRSFP--VErRYQPLPAHQR------------------------------------FDEAVARAT---------A 205

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  428 ELLKAyhhsfddekvdldlimhllynichscDAGAVLIFLPGYDEIVGLRDRIlfdDKRFADSThryQVFMLHSNMQTSD 507
Cdd:PRK11664   206 ELLRQ--------------------------ESGSLLLFLPGVGEIQRVQEQL---ASRVASDV---LLCPLYGALSLAE 253

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  508 QKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICF 587
Cdd:PRK11664   254 QQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICL 333

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  588 RLFSRLRFQNMLEFQTPELLRMPLQELCLHtklLAPVNCPIADFLMKAPEPPPALIvRNAVQMLKTIDAMDTWEDLTELG 667
Cdd:PRK11664   334 HLYSKEQAERAAAQSEPEILHSDLSGLLLE---LLQWGCHDPAQLSWLDQPPAAAL-AAAKRLLQQLGALDGQGRLTARG 409

                          650
                   ....*....|....*....
gi 1622946382  668 YHLADLPVEPHLGKMVLCA 686
Cdd:PRK11664   410 RKMAALGNDPRLAAMLVAA 428
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 31-206 1.54e-39

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to 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: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 145.00  E-value: 1.54e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCF-KNGipcRIFCTQPRRLAAIAVAERVAAERRERIGQT 109
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFsQHG---MIGVTQPRRVAAISVAQRVAEEMKCTLGSK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  110 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPT-----LKLIL 184
Cdd:cd17984     78 VGYQVRFDDCSSKETAIKYMTDGCLLRHILA-DPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkehLKVVV 156

                          170       180
                   ....*....|....*....|..
gi 1622946382  185 SSAALDVNLFLRYFGSCPVIYI 206
Cdd:cd17984    157 MSATLELAKLSAFFGNCPVFDI 178
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 31-204 2.10e-39

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 144.40  E-value: 2.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLD-DCFKNGipcRIFCTQPRRLAAIAVAERVAAERRERIGQT 109
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAeLWIAGG---KIIVLEPRRVAARAAARRLATLLGEAPGET 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  110 IGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQ-KHPTLKLILSSAA 188
Cdd:cd17990     78 VGYRVRGESRVGRRTRVEVVTEGVLLRRLQR-DPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSAT 156

                          170
                   ....*....|....*.
gi 1622946382  189 LDVNLFLRYFGSCPVI 204
Cdd:cd17990    157 LDGDGLAALLPEAPVV 172
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 31-204 1.96e-29

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to 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: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 115.69  E-value: 1.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   31 LPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQ----FLLDDCFKNGIpcrIFCTQPRRLAAIAVAERVAAERRERI 106
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV---VVCTQVHKQTAVWLALRVADEMDVNI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  107 GQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSS 186
Cdd:cd17977     78 GHEVGYVIPFENCCTNETILRYCTDDMLLREMMS-DPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIIT 156

                          170
                   ....*....|....*...
gi 1622946382  187 AALDVNLFLRYFGSCPVI 204
Cdd:cd17977    157 CPHLSSKLLSYYGNVPLI 174
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 647-738 1.71e-27

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 107.71  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  647 AVQMLKTIDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKR 726
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80

                           90       100
                   ....*....|....*....|....
gi 1622946382  727 FTA------------GAFSDHMAL 738
Cdd:pfam04408   81 RRAadekarakfarlDLEGDHLTL 104
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 49-206 8.58e-24

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to 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: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 99.59  E-value: 8.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   49 VVLIVGETGSGKTTQIPQFLLDDCFKNGIPC-RIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLT 127
Cdd:cd17986     20 IVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPNTILR 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  128 FCTNGVLLRTlMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKL-ILSSAALDVNLfLRYFGSCPVIYI 206
Cdd:cd17986    100 FCWDRLLLQE-MTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVvVVTSPALEPKL-RAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
37-210 7.23e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 7.23e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382    37 QEEIVKIIKEN-KVVLIVGETGSGKTTQIPQFLLdDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGY--- 112
Cdd:smart00487   13 QKEAIEALLSGlRDVILAAPTGSGKTLAALLPAL-EALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLygg 91

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   113 ---QIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDR--FSDFLLTKLRDLlqkHPTLKLILSSA 187
Cdd:smart00487   92 dskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLL---PKNVQLLLLSA 168

                           170       180
                    ....*....|....*....|....*
gi 1622946382   188 ALDVNL--FLRYFGSCPVIYIQGRP 210
Cdd:smart00487  169 TPPEEIenLLELFLNDPVFIDVGFT 193
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 654-739 5.41e-18

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 79.62  E-value: 5.41e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   654 IDAMDTWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFvlptQASQKRAAMLCRKRFtAGAFS 733
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR----PKEKREDADAARRRF-ADPES 76


                    ....*.
gi 1622946382   734 DHMALL 739
Cdd:smart00847   77 DHLTLL 82
HELICc smart00490
helicase superfamily c-terminal domain;
492-580 2.38e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.55  E-value: 2.38e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   492 HRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGkvkeksfdalnfvtmlkmVWISKASA 571
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWSPASY 71


                    ....*....
gi 1622946382   572 IQRKGRAGR 580
Cdd:smart00490   72 IQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 448-580 3.06e-14

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 69.93  E-value: 3.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  448 MHLLYNICHSCDAGAVLIFLPGYDEIvglrdrilfdDKRFADSTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTN 527
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFSQTKKTL----------EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622946382  528 IAETSITVNDVVFVIDsgkvkeksFDAlnfvtmlkmvWISKASAIQRKGRAGR 580
Cdd:pfam00271   73 VAERGLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGR 107
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 47-187 4.69e-14

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: 70.51  E-value: 4.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   47 NKVVLIVGETGSGKTTQIPQFLLDDCFKNGipCRIFCTQPRRLAAIAVAERVAaeRRERIGQTIGYqirLESRVSPKTL- 125
Cdd:cd00046      1 GENVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAERLR--ELFGPGIRVAV---LVGGSSAEERe 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622946382  126 --------LTFCTNGVLLRTLMAGD-STLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKH-PTLKLILSSA 187
Cdd:cd00046     74 knklgdadIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGlKNAQVILLSA 145
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 809-904 3.51e-12

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 63.04  E-value: 3.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  809 VKAALVAGMYPNLVHVDRENLVLTGPKEK-KVRFHPASVLSQPqyKKIPPAngqaaaikalptdWLIYDEMTRAHRIAnI 887
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGKGYTTLSDNqRVFIHPSSVLFNE--KTFPPE-------------WVVYQELVETTKVY-I 64

                           90
                   ....*....|....*..
gi 1622946382  888 RCCSAVTPVTILVFCGP 904
Cdd:pfam07717   65 RTVTAISPEWLLLFAPH 81
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 522-591 1.57e-09

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 62.30  E-value: 1.57e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622946382  522 IILSTNIAETSITVNDVVFVIDSGKVKEKS-FDAlnfvtmlKMVWISKASAIQRKGRAGRCRPGICFRLFS 591
Cdd:PHA02653   449 IIISTPYLESSVTIRNATHVYDTGRVYVPEpFGG-------KEMFISKSMRTQRKGRVGRVSPGTYVYFYD 512
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-402 4.96e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 4.96e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622946382  347 TALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSA 402
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 3-217 2.79e-08

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 58.07  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382    3 KTSGRLNNGIPQIPVKrgesefdsFRQSLPvfEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFL-----LDDCFKN-G 76
Cdd:PHA02653   145 DTIGILGNPEPFSKIP--------LASLQP--DVQLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnyLFGGFDNlD 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   77 IPCRIFCTQPRRLAAiavaERVAAERRERIG--QTIGYQIRLESRVSPK---------------TLLTFCTNGVLLRTLM 139
Cdd:PHA02653   215 KIDPNFIERPIVLSL----PRVALVRLHSITllKSLGFDEIDGSPISLKygsipdelintnpkpYGLVFSTHKLTLNKLF 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  140 AGDStlstvthVIVDEVHERDRFSDFLLTKLRdllqKHPTL--KLILSSAAL--DVNLFLRYFGSCPVIYIQGRP-FEVK 214
Cdd:PHA02653   291 DYGT-------VIIDEVHEHDQIGDIIIAVAR----KHIDKirSLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPIS 359


                   ...
gi 1622946382  215 EMF 217
Cdd:PHA02653   360 EVY 362
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 37-193 8.54e-08

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: 53.02  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   37 QEEIVKIIKENKVVLIVGETGSGKTT--QIPqfLLDDCFKNGIPCRIFCTQPRR-LAA--IAVAERVAAERRERI----- 106
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTReLAEqiYEELKKLGKGLGLKVasllg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  107 GQTIGYQIRLESRVSpktlLTFCTNGVLLrTLMAGDSTLSTVTHVIVDEVHE--RDRFSDFLLTKLRDLLQKHPTLKLil 184
Cdd:pfam00270   82 GDSRKEQLEKLKGPD----ILVGTPGRLL-DLLQERKLLKNLKLLVLDEAHRllDMGFGPDLEEILRRLPKKRQILLL-- 154


                   ....*....
gi 1622946382  185 sSAALDVNL 193
Cdd:pfam00270  155 -SATLPRNL 162
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
324-485 1.83e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  324 AQVFHLILTENVSVDYRhSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSAS 403
Cdd:COG0666    100 LEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  404 L---------------EFGNLDessLVQT---NGSDLSAEDRE----LLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAG 461
Cdd:COG0666    179 VnardndgetplhlaaENGHLE---IVKLlleAGADVNAKDNDgktaLDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

                          170       180
                   ....*....|....*....|....
gi 1622946382  462 AVLIFLPGYDEIVGLRDRILFDDK 485
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
347-448 3.31e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 3.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  347 TALMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSASLEFGNLDESSLVQTNGSDLSAED 426
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                           90       100
                   ....*....|....*....|..
gi 1622946382  427 RELLKAYHHSFDDEKVDLDLIM 448
Cdd:COG0666    268 VKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
303-397 4.79e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 4.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382  303 LIKEMDACLSDIWLHKDIDAFAQVFHLILTENVSVDYRhSETSATALMVAAGRGFASQVEQLISMGANVHSKASNGWMAL 382
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAK-DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124

                           90
                   ....*....|....*
gi 1622946382  383 DWAKHFGQTEIVDLL 397
Cdd:COG0666    125 HLAAYNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
349-417 2.53e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 2.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946382  349 LMVAAGRGFASQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLesysasLEFGNLDESSLVQT 417
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL------LEHADVNLKDNGRT 63
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 519-589 1.75e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.15  E-value: 1.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622946382  519 VRKIILSTNIAETSITVNDVVFVIdSGKVKEKSFD--ALNFVTMLkMVWISKASAIQRKGRAGR--CRPGICFRL 589
Cdd:cd18785      4 VKIIVFTNSIEHAEEIASSLEILV-ATNVLGEGIDvpSLDTVIFF-DPPSSAASYIQRVGRAGRggKDEGEVILF 76
AAA_22 pfam13401
AAA domain;
49-185 1.87e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   49 VVLIVGETGSGKTTQIPQFLlddcfkngipcRIFCTQPRRLAAIAVAERV-AAERRERIGQTIGyqIRLESRVSPKTLLT 127
Cdd:pfam13401    7 ILVLTGESGTGKTTLLRRLL-----------EQLPEVRDSVVFVDLPSGTsPKDLLRALLRALG--LPLSGRLSKEELLA 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622946382  128 FCTNGVLlrtlmagdsTLSTVTHVIVDEVHerdRFSDFLLTKLRDLLQKHPT-LKLILS 185
Cdd:pfam13401   74 ALQQLLL---------ALAVAVVLIIDEAQ---HLSLEALEELRDLLNLSSKlLQLILV 120
AAA_19 pfam13245
AAA domain;
37-156 3.91e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 39.12  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622946382   37 QEEIVKIIKENKVVLIVGETGSGKTTQIpqfllddcfkNGIpCRIFC---TQPRRLAAIAVAERVAAERRERIG---QTI 110
Cdd:pfam13245    1 QREAVRTALPSKVVLLTGGPGTGKTTTI----------RHI-VALLValgGVSFPILLAAPTGRAAKRLSERTGlpaSTI 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1622946382  111 GYqirlesrvspktLLTFctNGVLLRTLMAGDSTLSTVTHVIVDEV 156
Cdd:pfam13245   70 HR------------LLGF--DDLEAGGFLRDEEEPLDGDLLIVDEF 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-397 4.15e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 4.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622946382  326 VFHLILTENVSVDyRHSETSATALMVAAGRGFASQVEQLIS-MGANVhskASNGWMALDWAKHFGQTEIVDLL 397
Cdd:pfam12796   12 LVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEhADVNL---KDNGRTALHYAARSGHLEIVKLL 80
 
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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