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Conserved domains on  [gi|528968445|ref|XP_005212723|]
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putative ATP-dependent RNA helicase DHX57 isoform X1 [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
539-1166 1.57e-123

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: 404.85  E-value: 1.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  539 SLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 618
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDiVLQ--RPTLQVILMS 696
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLD-LQPalRPDLKLLVMS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  697 ATLNAELFSEYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskekLKARRSRTAFEeveedlrls 776
Cdd:COG1643   164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE--------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  777 lhlqdqDSVKDAVpdqqldfkqllaryqgvsksviktmsvmdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEI 856
Cdd:COG1643   206 ------DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREI 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  857 KMLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 936
Cdd:COG1643   234 RRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYD 307

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  937 ASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHFNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNLQ 1014
Cdd:COG1643   308 PRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDPE 381

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1015 SVfaRLIEPPHADSLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFV 1094
Cdd:COG1643   382 DL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRR 459

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528968445 1095 SPwdkkeeanqkklefafANSDYLALLRAykgWQlsmkegmraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1166
Cdd:COG1643   460 GA----------------AGSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
 237-420 1.48e-50

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


:

Pssm-ID: 467661  Cd Length: 115  Bit Score: 173.92  E-value: 1.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  237 EECVEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtskfckfkqkestkniqeaslevckfylkgnckfgskckf 316
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  317 khevppnqivgrvernvddshlnanedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALTFA 396
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91

                         170       180
                  ....*....|....*....|....
gi 528968445  397 ETSEPVVYSLITLLEEESEITKLL 420
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1210-1307 1.64e-23

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: 95.40  E-value: 1.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1210 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSDELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLVYHEKIKTSRV 1289
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62

                           90
                   ....*....|....*...
gi 528968445  1290 FIRDCSMVSVYPLVLFGG 1307
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
 176-213 2.54e-12

UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase.


:

Pssm-ID: 270502  Cd Length: 38  Bit Score: 62.33  E-value: 2.54e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 528968445  176 VSAFAVHRLSRYGFHTEHCQAALRICDGDMGASLERLL 213
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
ZnF_C3H1 smart00356
zinc finger;
298-318 1.09e-06

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 46.08  E-value: 1.09e-06
                            10        20
                    ....*....|....*....|.
gi 528968445    298 EVCKFYLKGNCKFGSKCKFKH 318
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
539-1166 1.57e-123

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 404.85  E-value: 1.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  539 SLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 618
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDiVLQ--RPTLQVILMS 696
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLD-LQPalRPDLKLLVMS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  697 ATLNAELFSEYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskekLKARRSRTAFEeveedlrls 776
Cdd:COG1643   164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE--------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  777 lhlqdqDSVKDAVpdqqldfkqllaryqgvsksviktmsvmdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEI 856
Cdd:COG1643   206 ------DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREI 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  857 KMLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 936
Cdd:COG1643   234 RRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYD 307

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  937 ASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHFNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNLQ 1014
Cdd:COG1643   308 PRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDPE 381

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1015 SVfaRLIEPPHADSLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFV 1094
Cdd:COG1643   382 DL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRR 459

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528968445 1095 SPwdkkeeanqkklefafANSDYLALLRAykgWQlsmkegmraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1166
Cdd:COG1643   460 GA----------------AGSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 540-716 8.94e-114

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: 354.15  E-value: 8.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160

                         170
                  ....*....|....*..
gi 528968445  700 NAELFSEYFNSCPVITI 716
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 538-1171 2.14e-80

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 290.81  E-value: 2.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  538 QSLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERV 617
Cdd:PRK11131   71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  618 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSA 697
Cdd:PRK11131  147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  698 TLNAELFSEYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskeklkarrsRTAFEEveedlrlsl 777
Cdd:PRK11131  227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEE--------- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  778 hlqDQDSVKDavpdqQLdfkqllaryQGVsksviktmsvmdfekvnlelIEALLEWIVDGkhsypPGAILVFLPGLAEIK 857
Cdd:PRK11131  263 ---ADDTERD-----QL---------QAI--------------------FDAVDELGREG-----PGDILIFMSGEREIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  858 MLYEQLQSNSLFNNRrsnrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDA 937
Cdd:PRK11131  301 DTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  938 SKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHFNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQS 1015
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLGD 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1016 VFA-RLIEPPHA----DSLRAskirLRDLGALTPDET-----LTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAA 1085
Cdd:PRK11131  444 IAAfPFVEAPDKrniqDGVRL----LEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITS 519

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1086 SLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLRAYKGWQLSMKEGMRASY-NYCRQNFLSGRVLQEMASLKRQFTE 1164
Cdd:PRK11131  520 ALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLNYLRVREWQDIYTQLRQ 599


                  ....*..
gi 528968445 1165 LLSDIGF 1171
Cdd:PRK11131  600 VVKELGI 606
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 549-1087 4.88e-77

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 273.57  E-value: 4.88e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   549 ILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGppekvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLE 628
Cdd:TIGR01970   10 LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   629 SVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQ-RPTLQVILMSATLNAELFSEY 707
Cdd:TIGR01970   85 NKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   708 FNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskeklKARRSRTAFEEveedlrlslhlQDQDSVKD 787
Cdd:TIGR01970  165 LPDAPVVESEGRSFPVE----------IRY--------------------LPLRGDQRLED-----------AVSRAVEH 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   788 AVPDQqldfkqllaryqgvsksviktmsvmdfekvnlelieallewivdgkhsypPGAILVFLPGLAEIKMLYEQLQSns 867
Cdd:TIGR01970  204 ALASE--------------------------------------------------TGSILVFLPGQAEIRRVQEQLAE-- 231

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   868 lfnnRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDT 947
Cdd:TIGR01970  232 ----RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETV 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   948 FVSQANALQRKGRAGRVASGVCFHLFtSHHFNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsvfaRLIEPPHAD 1027
Cdd:TIGR01970  308 RISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL-----RWLDAPPSV 381

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1028 SLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASL 1087
Cdd:TIGR01970  382 ALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
 237-420 1.48e-50

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


Pssm-ID: 467661  Cd Length: 115  Bit Score: 173.92  E-value: 1.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  237 EECVEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtskfckfkqkestkniqeaslevckfylkgnckfgskckf 316
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  317 khevppnqivgrvernvddshlnanedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALTFA 396
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91

                         170       180
                  ....*....|....*....|....
gi 528968445  397 ETSEPVVYSLITLLEEESEITKLL 420
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
DEXDc smart00487
DEAD-like helicases superfamily;
549-726 7.00e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 7.00e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445    549 ILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVaniICTQPRRISAISVAERVAKE----RAERVGLTVGYQ 624
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYGGDS 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445    625 IR--LESVKSSATRLLYCTTGVLLRRLE-GDTALQGVTHIIVDEVHERTEES--DFLLLVLKDIvlqRPTLQVILMSATL 699
Cdd:smart00487   94 KReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLSATP 170

                           170       180       190
                    ....*....|....*....|....*....|.
gi 528968445    700 --NAELFSEYFNSCPVITIPGRT--FPVDQF 726
Cdd:smart00487  171 peEIENLLELFLNDPVFIDVGFTplEPIEQF 201
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1210-1307 1.64e-23

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: 95.40  E-value: 1.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1210 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSDELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLVYHEKIKTSRV 1289
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62

                           90
                   ....*....|....*...
gi 528968445  1290 FIRDCSMVSVYPLVLFGG 1307
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 1036-1115 1.09e-22

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: 93.84  E-value: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1036 LRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1111
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84


                   ....
gi 528968445  1112 FANS 1115
Cdd:pfam04408   85 DEKA 88
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
 176-213 2.54e-12

UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase.


Pssm-ID: 270502  Cd Length: 38  Bit Score: 62.33  E-value: 2.54e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 528968445  176 VSAFAVHRLSRYGFHTEHCQAALRICDGDMGASLERLL 213
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
ZnF_C3H1 smart00356
zinc finger;
298-318 1.09e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 46.08  E-value: 1.09e-06
                            10        20
                    ....*....|....*....|.
gi 528968445    298 EVCKFYLKGNCKFGSKCKFKH 318
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 317-414 1.54e-06

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 48.09  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   317 KHEVPPNQIVGRVERNVDDSHLNANEDASFLYELEIRFSKDHKYPYQAPLVAFySTNENLPLACRLHISEFLYGKALTFa 396
Cdd:pfam05773   17 EFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN- 94

                           90
                   ....*....|....*...
gi 528968445   397 eTSEPVVYSLITLLEEES 414
Cdd:pfam05773   95 -LGEVMIFELIEWLQENL 111
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
 300-318 2.19e-06

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 45.10  E-value: 2.19e-06
                           10
                   ....*....|....*....
gi 528968445   300 CKFYLKGNCKFGSKCKFKH 318
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
539-1166 1.57e-123

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 404.85  E-value: 1.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  539 SLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 618
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDiVLQ--RPTLQVILMS 696
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLD-LQPalRPDLKLLVMS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  697 ATLNAELFSEYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskekLKARRSRTAFEeveedlrls 776
Cdd:COG1643   164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE--------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  777 lhlqdqDSVKDAVpdqqldfkqllaryqgvsksviktmsvmdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEI 856
Cdd:COG1643   206 ------DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREI 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  857 KMLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYD 936
Cdd:COG1643   234 RRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYD 307

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  937 ASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHFNhQLLKQQLPEIQRVPLEQLclrikILEMFS--THNLQ 1014
Cdd:COG1643   308 PRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASL-----ILELAAwgLGDPE 381

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1015 SVfaRLIEPPHADSLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFV 1094
Cdd:COG1643   382 DL--PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRR 459

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528968445 1095 SPwdkkeeanqkklefafANSDYLALLRAykgWQlsmkegmraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1166
Cdd:COG1643   460 GA----------------AGSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 540-716 8.94e-114

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: 354.15  E-value: 8.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160

                         170
                  ....*....|....*..
gi 528968445  700 NAELFSEYFNSCPVITI 716
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 556-716 1.20e-88

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: 284.35  E-value: 1.20e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  556 HQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEkvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSAT 635
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  636 RLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATLNAELFSEYFNSCPVIT 715
Cdd:cd17917    79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158


                  .
gi 528968445  716 I 716
Cdd:cd17917   159 I 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 538-1171 2.14e-80

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 290.81  E-value: 2.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  538 QSLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERV 617
Cdd:PRK11131   71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETEL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  618 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSA 697
Cdd:PRK11131  147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  698 TLNAELFSEYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskeklkarrsRTAFEEveedlrlsl 777
Cdd:PRK11131  227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-------------------------RPIVEE--------- 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  778 hlqDQDSVKDavpdqQLdfkqllaryQGVsksviktmsvmdfekvnlelIEALLEWIVDGkhsypPGAILVFLPGLAEIK 857
Cdd:PRK11131  263 ---ADDTERD-----QL---------QAI--------------------FDAVDELGREG-----PGDILIFMSGEREIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  858 MLYEQLQSNSLFNNRrsnrcvIHPLHSSLSSEEQQAVFvkPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDA 937
Cdd:PRK11131  301 DTADALNKLNLRHTE------ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  938 SKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHFNHqllKQQL--PEIQRVPLEQLclrikILEMFSThNLQS 1015
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQMTAL-GLGD 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1016 VFA-RLIEPPHA----DSLRAskirLRDLGALTPDET-----LTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAA 1085
Cdd:PRK11131  444 IAAfPFVEAPDKrniqDGVRL----LEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITS 519

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445 1086 SLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLRAYKGWQLSMKEGMRASY-NYCRQNFLSGRVLQEMASLKRQFTE 1164
Cdd:PRK11131  520 ALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLNYLRVREWQDIYTQLRQ 599


                  ....*..
gi 528968445 1165 LLSDIGF 1171
Cdd:PRK11131  600 VVKELGI 606
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 549-1087 4.88e-77

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 273.57  E-value: 4.88e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   549 ILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGppekvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLE 628
Cdd:TIGR01970   10 LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   629 SVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQ-RPTLQVILMSATLNAELFSEY 707
Cdd:TIGR01970   85 NKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   708 FNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspyarsmkqmskeklKARRSRTAFEEveedlrlslhlQDQDSVKD 787
Cdd:TIGR01970  165 LPDAPVVESEGRSFPVE----------IRY--------------------LPLRGDQRLED-----------AVSRAVEH 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   788 AVPDQqldfkqllaryqgvsksviktmsvmdfekvnlelieallewivdgkhsypPGAILVFLPGLAEIKMLYEQLQSns 867
Cdd:TIGR01970  204 ALASE--------------------------------------------------TGSILVFLPGQAEIRRVQEQLAE-- 231

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   868 lfnnRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDT 947
Cdd:TIGR01970  232 ----RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETV 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   948 FVSQANALQRKGRAGRVASGVCFHLFtSHHFNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSTHNLqsvfaRLIEPPHAD 1027
Cdd:TIGR01970  308 RISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL-----RWLDAPPSV 381

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1028 SLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASL 1087
Cdd:TIGR01970  382 ALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 814-973 1.64e-73

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: 242.05  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  814 MSVMDFEKVNLELIEALLEWIVdgkHSYPPGAILVFLPGLAEIKMLYEQLQSNSLFNNrrSNRCVIHPLHSSLSSEEQQA 893
Cdd:cd18791    17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPD--LGKLLVLPLHSSLPPEEQQR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  894 VFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLF 973
Cdd:cd18791    92 VFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 540-716 9.02e-70

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: 231.66  E-value: 9.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 --TVGYQIRLESVKS-SATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMS 696
Cdd:cd17981    81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160

                         170       180
                  ....*....|....*....|
gi 528968445  697 ATLNAELFSEYFNSCPVITI 716
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 540-716 2.34e-69

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: 230.49  E-value: 2.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSL-NGPPekvANIICTQPRRISAISVAERVAKERAERVG 618
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIP---CRIFCTQPRRLAAIAVAERVAAERGEKIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSA 697
Cdd:cd17987    78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157

                         170
                  ....*....|....*....
gi 528968445  698 TLNAELFSEYFNSCPVITI 716
Cdd:cd17987   158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 524-716 2.36e-68

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: 229.72  E-value: 2.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  524 KQASRQFQSVLQERQSLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAI 603
Cdd:cd17972    43 REQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  604 SVAERVAKERAERVGLTVGYQIRLESV-KSSATRLLYCTTGVLLRRLEgdTALQGVTHIIVDEVHERTEESDFLLLVLKD 682
Cdd:cd17972   123 SVAERVAFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLLVVLRD 200

                         170       180       190
                  ....*....|....*....|....*....|....
gi 528968445  683 IVLQRPTLQVILMSATLNAELFSEYFNSCPVITI 716
Cdd:cd17972   201 VVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 540-716 1.69e-66

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: 222.48  E-value: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSL-NGPPEKVANIICTQPRRISAISVAERVAKERAERVG 618
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 -----LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVI 693
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160

                         170       180
                  ....*....|....*....|...
gi 528968445  694 LMSATLNAELFSEYFNSCPVITI 716
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 551-1088 9.96e-64

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 233.66  E-value: 9.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  551 KLLSKHQVLVvSGMTGCGKTTQIP-QFILDDSLNGppekvaNIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLES 629
Cdd:PRK11664   16 ALKTAPQVLL-KAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYRMRAES 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  630 VKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIvlQ---RPTLQVILMSATLNAELFSE 706
Cdd:PRK11664   89 KVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDV--QqglRDDLKLLIMSATLDNDRLQQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  707 YFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgSPyarsmkqmskeklkarrsrtafeeveedlrLSLHLQDQDSVK 786
Cdd:PRK11664  167 LLPDAPVIVSEGRSFPVE----------RRY-----QP------------------------------LPAHQRFDEAVA 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  787 DAVpdqqldfKQLLARyqgvsksviktmsvmdfekvnlelieallewivdgkhsyPPGAILVFLPGLAEIKMLYEQLQsn 866
Cdd:PRK11664  202 RAT-------AELLRQ---------------------------------------ESGSLLLFLPGVGEIQRVQEQLA-- 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  867 slfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLED 946
Cdd:PRK11664  234 ----SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVT 309

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  947 TFVSQANALQRKGRAGRVASGVCFHLFTSHHFNHQLLkQQLPEIQRVPLEQLCLRikiLEMFSTHNLQSVfaRLIEPPHA 1026
Cdd:PRK11664  310 QRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAA-QSEPEILHSDLSGLLLE---LLQWGCHDPAQL--SWLDQPPA 383

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528968445 1027 DSLRASKIRLRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRclDPALTIAASLA 1088
Cdd:PRK11664  384 AALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLA 443
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 540-716 8.89e-62

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: 208.88  E-value: 8.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSAT 698
Cdd:cd17976    81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160

                         170
                  ....*....|....*...
gi 528968445  699 LNAELFSEYFNSCPVITI 716
Cdd:cd17976   161 GDNQRLSRYFGGCPVVRV 178
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 529-716 1.36e-60

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: 205.73  E-value: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  529 QFQSVLQERQSLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVanIICTQPRRISAISVAER 608
Cdd:cd17973     2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  609 VAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRP 688
Cdd:cd17973    80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159

                         170       180
                  ....*....|....*....|....*...
gi 528968445  689 TLQVILMSATLNAELFSEYFNSCPVITI 716
Cdd:cd17973   160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 540-716 2.59e-58

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: 198.44  E-value: 2.59e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppekvaNIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17979    74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153

                         170
                  ....*....|....*..
gi 528968445  700 NAELFSEYFNSCPVITI 716
Cdd:cd17979   154 NIELFSGYFEGAPVVQV 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 540-716 1.22e-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: 188.33  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA----RGGMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQR-----PTLQVIL 694
Cdd:cd17978    77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156

                         170       180
                  ....*....|....*....|..
gi 528968445  695 MSATLNAELFSEYFNSCPVITI 716
Cdd:cd17978   157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 540-710 5.81e-53

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: 183.47  E-value: 5.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgpPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPT-LQVILMSAT 698
Cdd:cd17988    79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSAT 158

                         170
                  ....*....|..
gi 528968445  699 LNAELFSEYFNS 710
Cdd:cd17988   159 ISCKEFADYFTT 170
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 535-717 9.25e-53

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: 183.07  E-value: 9.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  535 QERQSLPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERA 614
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYT----SRGKIGCTQPRRVAAMSVAKRVAEEFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  615 ERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVIL 694
Cdd:cd17971    77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156

                         170       180
                  ....*....|....*....|...
gi 528968445  695 MSATLNAELFSEYFNSCPVITIP 717
Cdd:cd17971   157 TSATLDAVKFSQYFYEAPIFTIP 179
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
 237-420 1.48e-50

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


Pssm-ID: 467661  Cd Length: 115  Bit Score: 173.92  E-value: 1.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  237 EECVEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtskfckfkqkestkniqeaslevckfylkgnckfgskckf 316
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  317 khevppnqivgrvernvddshlnanedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYGKALTFA 396
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91

                         170       180
                  ....*....|....*....|....
gi 528968445  397 ETSEPVVYSLITLLEEESEITKLL 420
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 540-716 1.69e-50

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: 176.15  E-value: 1.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDslnGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17974    78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157

                         170
                  ....*....|....*..
gi 528968445  700 NAELFSEYFNSCPVITI 716
Cdd:cd17974   158 DAEKFSAFFDDAPIFRI 174
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 540-710 5.80e-49

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: 172.27  E-value: 5.80e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDdslNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAE---AGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSAT 698
Cdd:cd17980    78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157

                         170
                  ....*....|..
gi 528968445  699 LNAELFSEYFNS 710
Cdd:cd17980   158 LDAEKFRDFFNQ 169
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 540-716 8.47e-45

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: 159.94  E-value: 8.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYT----DYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17983    77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156

                         170
                  ....*....|....*..
gi 528968445  700 NAELFSEYFNSCPVITI 716
Cdd:cd17983   157 DADKFADFFGNVPIFTI 173
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 540-716 6.19e-44

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: 157.23  E-value: 6.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppekVANIIC-TQPRRISAISVAERVAKERAERVG 618
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRG-----IRGLIGhTQPRRLAARSVAERIAEELKTELG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSAT 698
Cdd:cd17989    76 GAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155

                         170
                  ....*....|....*...
gi 528968445  699 LNAELFSEYFNSCPVITI 716
Cdd:cd17989   156 IDAERFSRHFNNAPIIEV 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 540-714 6.69e-43

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: 154.41  E-value: 6.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPpekvANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIV-LQRPTLQVILMSAT 698
Cdd:cd17990    77 TVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSAT 156

                         170
                  ....*....|....*.
gi 528968445  699 LNAELFSEYFNSCPVI 714
Cdd:cd17990   157 LDGDGLAALLPEAPVV 172
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 540-716 8.86e-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: 142.69  E-value: 8.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS----QHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPT-----LQVIL 694
Cdd:cd17984    77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkehLKVVV 156

                         170       180
                  ....*....|....*....|..
gi 528968445  695 MSATLNAELFSEYFNSCPVITI 716
Cdd:cd17984   157 MSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 540-716 2.27e-38

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: 142.11  E-value: 2.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVANII-CTQPRRISAISVAERVAKERAErVG 618
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIgITQPRRVAAVSMAKRVAEELNV-FG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPT--------- 689
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 528968445  690 -LQVILMSATLNAELFSE----YFNSCPVITI 716
Cdd:cd17982   160 pLKLVIMSATLRVEDFTEnkllFPRPPPVIKV 191
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 540-714 6.69e-34

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: 128.79  E-value: 6.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVAnIICTQPRRISAISVAERVAKERAERVGL 619
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  620 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSATL 699
Cdd:cd17977    80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159

                         170
                  ....*....|....*
gi 528968445  700 NAELFSEYFNSCPVI 714
Cdd:cd17977   160 LSSKLLSYYGNVPLI 174
DEXDc smart00487
DEAD-like helicases superfamily;
549-726 7.00e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.81  E-value: 7.00e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445    549 ILKLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKVaniICTQPRRISAISVAERVAKE----RAERVGLTVGYQ 624
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYGGDS 93

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445    625 IR--LESVKSSATRLLYCTTGVLLRRLE-GDTALQGVTHIIVDEVHERTEES--DFLLLVLKDIvlqRPTLQVILMSATL 699
Cdd:smart00487   94 KReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLSATP 170

                           170       180       190
                    ....*....|....*....|....*....|.
gi 528968445    700 --NAELFSEYFNSCPVITIPGRT--FPVDQF 726
Cdd:smart00487  171 peEIENLLELFLNDPVFIDVGFTplEPIEQF 201
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 540-716 8.38e-25

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: 102.67  E-value: 8.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  540 LPAWEERENIL-KLLSKHQVLVVSGMTGCGKTTQIPQFILDDSLNGPPEKvANIICTQPRRISAISVAERVAKERAERVG 618
Cdd:cd17986     1 LPIWAAKFTFLeQLESPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQK-GQVTVTQPHPLAARSLALRVADEMDLNLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  619 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHERTEESDFLLLVLKDIVLQRPTLQVILMSAT 698
Cdd:cd17986    80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSP 159

                         170
                  ....*....|....*...
gi 528968445  699 LNAELFSEYFNSCPVITI 716
Cdd:cd17986   160 ALEPKLRAFWGNPPVVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 1210-1307 1.64e-23

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: 95.40  E-value: 1.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1210 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSDELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLVYHEKIKTSRV 1289
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62

                           90
                   ....*....|....*...
gi 528968445  1290 FIRDCSMVSVYPLVLFGG 1307
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 1039-1121 3.59e-23

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: 94.64  E-value: 3.59e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   1039 LGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFvsPWDKKEEANQKKLEFAFANSDYL 1118
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79


                    ...
gi 528968445   1119 ALL 1121
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 1036-1115 1.09e-22

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: 93.84  E-value: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  1036 LRDLGALTPDETLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1111
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84


                   ....
gi 528968445  1112 FANS 1115
Cdd:pfam04408   85 DEKA 88
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 825-964 1.49e-13

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: 68.01  E-value: 1.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   825 ELIEALLEWIvdgkHSYPPGAILVFLPGlaeIKMLYEQLqsnsLFNNRRSNrcvIHPLHSSLSSEEQQAVFVKPPMGVTK 904
Cdd:pfam00271    1 EKLEALLELL----KKERGGKVLIFSQT---KKTLEAEL----LLEKEGIK---VARLHGDLSQEEREEILEDFRKGKID 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   905 IIISTNIAETSITIDDVVYVIDsgkmkekrYDASKGMESLedtfvsqanaLQRKGRAGRV 964
Cdd:pfam00271   67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
873-963 4.36e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 65.70  E-value: 4.36e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445    873 RSNRCVIHPLHSSLSSEEQQAVFVKPPMGVTKIIISTNIAETSITIDDVVYVIDsgkmkekrYDASKGMESLedtfvsqa 952
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDLPWSPASY-------- 71

                            90
                    ....*....|.
gi 528968445    953 naLQRKGRAGR 963
Cdd:smart00490   72 --IQRIGRAGR 80
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 549-967 5.93e-13

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 73.47  E-value: 5.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  549 ILKLLSKHQVLVVSGMTGCGKTTQIPQFIL-----------DDSLNGPPEKvANIICTQPR----RISAISVAERVAKER 613
Cdd:PHA02653  172 IFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnLDKIDPNFIE-RPIVLSLPRvalvRLHSITLLKSLGFDE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  614 AERVGLTVGY---QIRLESVKSSATRLLYCTTGVLLrrlegdTALQGVTHIIVDEVHERTEESDFLLLVL-KDIVLQRpt 689
Cdd:PHA02653  251 IDGSPISLKYgsiPDELINTNPKPYGLVFSTHKLTL------NKLFDYGTVIIDEVHEHDQIGDIIIAVArKHIDKIR-- 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  690 lQVILMSATL--NAELFSEYFNSCPVITIPGRT-FPVDQFfledaiavtrYVLQDGSPYARsmkqmskeklkarrsrtaF 766
Cdd:PHA02653  323 -SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV----------YVKNKYNPKNK------------------R 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  767 EEVEEDLRLSLHlqdqdSVKDAVPDQQldfkqllaryqgvsKSVI---KTMSVMDFEKVNLE-LIEALLEWIVDGKhsyp 842
Cdd:PHA02653  374 AYIEEEKKNIVT-----ALKKYTPPKG--------------SSGIvfvASVSQCEEYKKYLEkRLPIYDFYIIHGK---- 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  843 pgailvfLPGLAEIkmlyeqlqSNSLFNNRRsnrcvihplhsslsseeqqavfvkppmgvTKIIISTNIAETSITIDDVV 922
Cdd:PHA02653  431 -------VPNIDEI--------LEKVYSSKN-----------------------------PSIIISTPYLESSVTIRNAT 466

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 528968445  923 YVIDSGKMKEKR-YDAskgmeslEDTFVSQANALQRKGRAGRVASG 967
Cdd:PHA02653  467 HVYDTGRVYVPEpFGG-------KEMFISKSMRTQRKGRVGRVSPG 505
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
 176-213 2.54e-12

UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, also called DEAH box protein 57, is a multi-domain protein with an N-terminal ubiquitin-association (UBA) domain, a Zinc finger domain, a RWD domain, a DEAD-like helicase domain and two C-terminal helicase associated domains. Although the precise biological function of DHX57 remains unclear, it may function as a putative ATP-dependent RNA helicase.


Pssm-ID: 270502  Cd Length: 38  Bit Score: 62.33  E-value: 2.54e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 528968445  176 VSAFAVHRLSRYGFHTEHCQAALRICDGDMGASLERLL 213
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 565-698 2.59e-12

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: 65.89  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  565 TGCGKTTQIPQFILDDSLNGPPeKVAnIICtqPRRISAISVAERVAKERAE--RVGLTVGY---QIRLESVKSSAtRLLY 639
Cdd:cd00046    10 TGSGKTLAALLAALLLLLKKGK-KVL-VLV--PTKALALQTAERLRELFGPgiRVAVLVGGssaEEREKNKLGDA-DIII 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528968445  640 CTTGVLLRRLEGDTAL--QGVTHIIVDEVHERTEESDFLLLV-LKDIVLQRPTLQVILMSAT 698
Cdd:cd00046    85 ATPDMLLNLLLREDRLflKDLKLIIVDEAHALLIDSRGALILdLAVRKAGLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 549-703 1.59e-11

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: 64.19  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   549 ILKLLSKHQVLVVSGmTGCGKTT--QIPqfILDDSLNGPPEKVANIICtqPRRISAISVAERvAKERAERVGLTV----- 621
Cdd:pfam00270    8 IPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVasllg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   622 GYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVTHIIVDEVHeRTEESDF---LLLVLKDIvlqRPTLQVILMSAT 698
Cdd:pfam00270   82 GDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLLSAT 157


                   ....*
gi 528968445   699 LNAEL 703
Cdd:pfam00270  158 LPRNL 162
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 551-717 4.37e-07

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 51.49  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  551 KLLSKHQVLVVSGMTGCGKTTQIPQFILDdSLNGPPEKVaniICTQPRRisAIsVAERVA--KERAERVGLTVGYQIRLE 628
Cdd:cd17921    12 ALYLSGDSVLVSAPTSSGKTLIAELAILR-ALATSGGKA---VYIAPTR--AL-VNQKEAdlRERFGPLGKNVGLLTGDP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  629 SV---KSSATRLLYCTT---GVLLRRLEGDTaLQGVTHIIVDEVH--ERTEESDFLLLVLKDIVLQRPTLQVILMSATL- 699
Cdd:cd17921    85 SVnklLLAEADILVATPeklDLLLRNGGERL-IQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARFVGLSATLp 163

                         170
                  ....*....|....*...
gi 528968445  700 NAELFSEYFNSCPVITIP 717
Cdd:cd17921   164 NAEDLAEWLGVEDLIRFD 181
ZnF_C3H1 smart00356
zinc finger;
298-318 1.09e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 46.08  E-value: 1.09e-06
                            10        20
                    ....*....|....*....|.
gi 528968445    298 EVCKFYLKGNCKFGSKCKFKH 318
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 317-414 1.54e-06

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 48.09  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445   317 KHEVPPNQIVGRVERNVDDSHLNANEDASFLYELEIRFSKDHKYPYQAPLVAFySTNENLPLACRLHISEFLYGKALTFa 396
Cdd:pfam05773   17 EFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN- 94

                           90
                   ....*....|....*...
gi 528968445   397 eTSEPVVYSLITLLEEES 414
Cdd:pfam05773   95 -LGEVMIFELIEWLQENL 111
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
 300-318 2.19e-06

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 45.10  E-value: 2.19e-06
                           10
                   ....*....|....*....
gi 528968445   300 CKFYLKGNCKFGSKCKFKH 318
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
298-318 1.91e-05

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 42.57  E-value: 1.91e-05
                           10        20
                   ....*....|....*....|..
gi 528968445   298 EVCKFYLK-GNCKFGSKCKFKH 318
Cdd:pfam00642    4 ELCRFFLRtGYCKYGDRCKFAH 25
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
 299-318 3.87e-05

CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and one histidine to coordinate the zinc ion. This domain is found in a wide variety of proteins such as E3 ligases.


Pssm-ID: 465626  Cd Length: 22  Bit Score: 41.81  E-value: 3.87e-05
                           10        20
                   ....*....|....*....|
gi 528968445   299 VCKFYLKGNCKFGSKCKFKH 318
Cdd:pfam18044    2 LCRYFQKGGCRYGDNCRFSH 21
zf-CCCH_2 pfam14608
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ...
 300-318 7.55e-04

RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented by fingers 5-7 of Nab2. Nab2 ZnF5-7 are zinc-fingers of the type C-x8-C-x5-C-x3-H. Nab2 ZnFs function in the generation of export-competent mRNPs. Mab2 is a conserved polyadenosine-RNA-binding Zn finger protein required for both mRNA export and polyadenylation regulation and becomes attached to the mRNP after splicing and during or immediately after polyadenylation. The three ZnFs, 5-7, have almost identical folds and, most unusually, associate with one another to form a single coherent structural unit. ZnF5-7 bind to eight consecutive adenines, and chemical shift perturbations identify residues on each finger that interact with RNA.


Pssm-ID: 464217  Cd Length: 19  Bit Score: 37.88  E-value: 7.55e-04
                           10
                   ....*....|....*....
gi 528968445   300 CKFYlkGNCKFGSKCKFKH 318
Cdd:pfam14608    2 CRFG--GNCTFGPKCPFSH 18
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
614-706 4.00e-03

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 41.46  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528968445  614 AERVGLTVGYqirlESVKSSAtRLLYCTTGVLLRRL-EGDTALQGVTHIIVDEVH-----ERT---EESdflllvlkdIV 684
Cdd:COG4581    94 AENVGLLTGD----ASVNPDA-PIVVMTTEILRNMLyREGADLEDVGVVVMDEFHyladpDRGwvwEEP---------II 159

                          90       100
                  ....*....|....*....|...
gi 528968445  685 LQRPTLQVILMSATL-NAELFSE 706
Cdd:COG4581   160 HLPARVQLVLLSATVgNAEEFAE 182
 
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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