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Conserved domains on  [gi|397493579|ref|XP_003817681|]
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putative ATP-dependent RNA helicase DHX57 [Pan paniscus]

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];
544-1171 1.77e-126

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: 412.94  E-value: 1.77e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  544 SLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 623
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSA 702
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  703 TLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspymrsmkqiskekLKARRNRTAFEeveedlrlsl 782
Cdd:COG1643   165 TLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE---------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  783 hlqdqDSVKDAVpdqqldfkqllarykgvsksviktmsimdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEIK 862
Cdd:COG1643   206 -----DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREIR 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  863 MLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDA 942
Cdd:COG1643   235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  943 SKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLqsvf 1022
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579 1023 sRLIEPPHTDSLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPw 1102
Cdd:COG1643   384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA- 461
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 397493579 1103 dkkeeanqkklefafANSDYLALLRAykgWQlstkegvraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1171
Cdd:COG1643   462 ---------------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 ...
243-426 7.53e-51

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: 174.69  E-value: 7.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  243 DECMEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtsrfrkskpkestknvqensleickfylkgnckfgskcrf 322
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  323 khevppnqivgriersvddshlnaiedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYDKALTFA 402
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91
                         170       180
                  ....*....|....*....|....
gi 397493579  403 ETSEPVVYSLITLLEEESEIVKLL 426
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1214-1311 1.07e-22

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: 93.09  E-value: 1.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1214 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1293
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 397493579  1294 FIRDCSMVSVYPLVLFGG 1311
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
182-219 2.57e-17

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: 76.58  E-value: 2.57e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 397493579  182 VSPFAVQKLSRYGFNTERCQAVLRMCDGDVGASLEHLL 219
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
306-324 1.07e-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: 45.87  E-value: 1.07e-06
                           10
                   ....*....|....*....
gi 397493579   306 CKFYLKGNCKFGSKCRFKH 324
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
544-1171 1.77e-126

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 412.94  E-value: 1.77e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  544 SLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 623
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSA 702
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  703 TLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspymrsmkqiskekLKARRNRTAFEeveedlrlsl 782
Cdd:COG1643   165 TLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE---------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  783 hlqdqDSVKDAVpdqqldfkqllarykgvsksviktmsimdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEIK 862
Cdd:COG1643   206 -----DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREIR 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  863 MLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDA 942
Cdd:COG1643   235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  943 SKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLqsvf 1022
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579 1023 sRLIEPPHTDSLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPw 1102
Cdd:COG1643   384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA- 461
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 397493579 1103 dkkeeanqkklefafANSDYLALLRAykgWQlstkegvraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1171
Cdd:COG1643   462 ---------------AGSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
545-721 1.17e-115

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: 359.54  E-value: 1.17e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 397493579  705 NAELFSDYFNSCPVITI 721
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
502-1176 1.19e-80

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 291.58  E-value: 1.19e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  502 KKISKRYDWQAksVHAENGKICKQFRMKQASRQFQS-ILQERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQ 580
Cdd:PRK11131   31 KKIKNPDAQQA--IFQEIAKEIAQAAQRVLLREAARpEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  581 FILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTAL 660
Cdd:PRK11131  109 ICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  661 QGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavT 740
Cdd:PRK11131  185 MQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE----------V 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  741 RYvlqdgspymrsmkqiskeklkarrnRTAFEEveedlrlslhlqDQDSVKDavpdqqldfkQLLArykgvsksviktms 820
Cdd:PRK11131  255 RY-------------------------RPIVEE------------ADDTERD----------QLQA-------------- 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  821 imdfekvnleLIEALLEWIVDGkhsypPGAILVFLPGLAEIKMLYEQLQSNSLFNNRrsnrcvIHPLHSSLSSEEQQAVF 900
Cdd:PRK11131  274 ----------IFDAVDELGREG-----PGDILIFMSGEREIRDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  901 vkPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTS 980
Cdd:PRK11131  333 --QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSE 410
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  981 HHYNHqllKQQL--PEIQRVPLEQLclrikILEMfSAHNLQ--SVFSrLIEPPHT----DSLRAskirLRDLGALTPDE- 1051
Cdd:PRK11131  411 DDFLS---RPEFtdPEILRTNLASV-----ILQM-TALGLGdiAAFP-FVEAPDKrniqDGVRL----LEELGAITTDEq 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579 1052 ----RLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLR 1127
Cdd:PRK11131  477 asayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVN 556
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 397493579 1128 AYKGWQLSTKEGVRASY-NYCRQNFLSGRVLQEMASLKRQFTELLSDIGF 1176
Cdd:PRK11131  557 LWNYLQEQQKALSSNQFrRLCRTDYLNYLRVREWQDIYTQLRQVVKELGI 606
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
554-1092 1.69e-78

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: 277.80  E-value: 1.69e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   554 ILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGppekvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLE 633
Cdd:TIGR01970   10 LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   634 SVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSATLNAELFSDY 712
Cdd:TIGR01970   85 NKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   713 FNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspymrsmkqiskeklKARRNRTAFEEveedlrlslhlQDQDSVKD 792
Cdd:TIGR01970  165 LPDAPVVESEGRSFPVE----------IRY--------------------LPLRGDQRLED-----------AVSRAVEH 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   793 AVPDQqldfkqllarykgvsksviktmsimdfekvnlelieallewivdgkhsypPGAILVFLPGLAEIKMLYEQLQSns 872
Cdd:TIGR01970  204 ALASE--------------------------------------------------TGSILVFLPGQAEIRRVQEQLAE-- 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   873 lfnnRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDT 952
Cdd:TIGR01970  232 ----RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETV 307
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   953 FVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLqsvfsRLIEPPHTD 1032
Cdd:TIGR01970  308 RISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL-----RWLDAPPSV 381
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1033 SLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASL 1092
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 ...
243-426 7.53e-51

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: 174.69  E-value: 7.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  243 DECMEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtsrfrkskpkestknvqensleickfylkgnckfgskcrf 322
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  323 khevppnqivgriersvddshlnaiedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYDKALTFA 402
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91
                         170       180
                  ....*....|....*....|....
gi 397493579  403 ETSEPVVYSLITLLEEESEIVKLL 426
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
DEXDc smart00487
DEAD-like helicases superfamily;
551-731 2.11e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.96  E-value: 2.11e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579    551 RETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVaniICTQPRRISAISVAERVAKE----RAERVGLTV 626
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579    627 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDTALQGVSHIIVDEVHERTEES--DFLLLVLKDIvsqRPGLQVILMS 701
Cdd:smart00487   91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
                           170       180       190
                    ....*....|....*....|....*....|....
gi 397493579    702 ATL--NAELFSDYFNSCPVITIPGRT--FPVDQF 731
Cdd:smart00487  168 ATPpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1041-1120 1.86e-23

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: 96.15  E-value: 1.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1041 LRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1116
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84

                   ....
gi 397493579  1117 FANS 1120
Cdd:pfam04408   85 DEKA 88
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1214-1311 1.07e-22

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: 93.09  E-value: 1.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1214 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1293
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 397493579  1294 FIRDCSMVSVYPLVLFGG 1311
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
182-219 2.57e-17

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: 76.58  E-value: 2.57e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 397493579  182 VSPFAVQKLSRYGFNTERCQAVLRMCDGDVGASLEHLL 219
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
323-420 6.62e-07

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: 49.24  E-value: 6.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   323 KHEVPPNQIVGRIERSVDDSHLNAIEDASFLYELEIRFSKDHKYPYQAPLVAFySTNENLPLACRLHISEFLYDKALTFa 402
Cdd:pfam05773   17 EFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN- 94
                           90
                   ....*....|....*...
gi 397493579   403 eTSEPVVYSLITLLEEES 420
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 ...
306-324 1.07e-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: 45.87  E-value: 1.07e-06
                           10
                   ....*....|....*....
gi 397493579   306 CKFYLKGNCKFGSKCRFKH 324
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
ZnF_C3H1 smart00356
zinc finger;
304-324 1.49e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 45.70  E-value: 1.49e-06
                            10        20
                    ....*....|....*....|.
gi 397493579    304 EICKFYLKGNCKFGSKCRFKH 324
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
544-1171 1.77e-126

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 412.94  E-value: 1.77e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  544 SLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLnGPPEKvanIICTQPRRISAISVAERVAKERAERVG 623
Cdd:COG1643     9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGW-GAGGR---IGMLEPRRLAARAAAERMAEELGEPVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSA 702
Cdd:COG1643    85 ETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  703 TLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspymrsmkqiskekLKARRNRTAFEeveedlrlsl 782
Cdd:COG1643   165 TLDAERFARLLGDAPVIESSGRTYPVE----------VRY-------------------RPLPADERDLE---------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  783 hlqdqDSVKDAVpdqqldfkqllarykgvsksviktmsimdfekvnlelIEALLEwivdgkhsyPPGAILVFLPGLAEIK 862
Cdd:COG1643   206 -----DAVADAV-------------------------------------REALAE---------EPGDILVFLPGEREIR 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  863 MLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDA 942
Cdd:COG1643   235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  943 SKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNhQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLqsvf 1022
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579 1023 sRLIEPPHTDSLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPw 1102
Cdd:COG1643   384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGA- 461
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 397493579 1103 dkkeeanqkklefafANSDYLALLRAykgWQlstkegvraSYNYCRQNFLSGRVLQEMASLKRQFTELL 1171
Cdd:COG1643   462 ---------------AGSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
545-721 1.17e-115

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: 359.54  E-value: 1.17e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 397493579  705 NAELFSDYFNSCPVITI 721
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) ...
561-721 2.27e-89

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: 286.28  E-value: 2.27e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  561 HQVVVISGMTGCGKTTQIPQFILDDSLNGPPEkvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSAT 640
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGK--GRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  641 RLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATLNAELFSDYFNSCPVIT 720
Cdd:cd17917    79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158

                  .
gi 397493579  721 I 721
Cdd:cd17917   159 I 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
502-1176 1.19e-80

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 291.58  E-value: 1.19e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  502 KKISKRYDWQAksVHAENGKICKQFRMKQASRQFQS-ILQERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQ 580
Cdd:PRK11131   31 KKIKNPDAQQA--IFQEIAKEIAQAAQRVLLREAARpEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  581 FILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTAL 660
Cdd:PRK11131  109 ICLELGRG----VKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  661 QGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavT 740
Cdd:PRK11131  185 MQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVE----------V 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  741 RYvlqdgspymrsmkqiskeklkarrnRTAFEEveedlrlslhlqDQDSVKDavpdqqldfkQLLArykgvsksviktms 820
Cdd:PRK11131  255 RY-------------------------RPIVEE------------ADDTERD----------QLQA-------------- 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  821 imdfekvnleLIEALLEWIVDGkhsypPGAILVFLPGLAEIKMLYEQLQSNSLFNNRrsnrcvIHPLHSSLSSEEQQAVF 900
Cdd:PRK11131  274 ----------IFDAVDELGREG-----PGDILIFMSGEREIRDTADALNKLNLRHTE------ILPLYARLSNSEQNRVF 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  901 vkPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTS 980
Cdd:PRK11131  333 --QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSE 410
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  981 HHYNHqllKQQL--PEIQRVPLEQLclrikILEMfSAHNLQ--SVFSrLIEPPHT----DSLRAskirLRDLGALTPDE- 1051
Cdd:PRK11131  411 DDFLS---RPEFtdPEILRTNLASV-----ILQM-TALGLGdiAAFP-FVEAPDKrniqDGVRL----LEELGAITTDEq 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579 1052 ----RLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSPWDKKEEANQKKLEFAFANSDYLALLR 1127
Cdd:PRK11131  477 asayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVN 556
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 397493579 1128 AYKGWQLSTKEGVRASY-NYCRQNFLSGRVLQEMASLKRQFTELLSDIGF 1176
Cdd:PRK11131  557 LWNYLQEQQKALSSNQFrRLCRTDYLNYLRVREWQDIYTQLRQVVKELGI 606
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
554-1092 1.69e-78

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: 277.80  E-value: 1.69e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   554 ILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGppekvANIICTQPRRISAISVAERVAKERAERVGLTVGYQIRLE 633
Cdd:TIGR01970   10 LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   634 SVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSATLNAELFSDY 712
Cdd:TIGR01970   85 NKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   713 FNSCPVITIPGRTFPVDqffledaiavTRYvlqdgspymrsmkqiskeklKARRNRTAFEEveedlrlslhlQDQDSVKD 792
Cdd:TIGR01970  165 LPDAPVVESEGRSFPVE----------IRY--------------------LPLRGDQRLED-----------AVSRAVEH 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   793 AVPDQqldfkqllarykgvsksviktmsimdfekvnlelieallewivdgkhsypPGAILVFLPGLAEIKMLYEQLQSns 872
Cdd:TIGR01970  204 ALASE--------------------------------------------------TGSILVFLPGQAEIRRVQEQLAE-- 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   873 lfnnRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDT 952
Cdd:TIGR01970  232 ----RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETV 307
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   953 FVSQANALQRKGRAGRVASGVCFHLFtSHHYNHQLLKQQLPEIQRVPLEQLCLRIKILEMFSAHNLqsvfsRLIEPPHTD 1032
Cdd:TIGR01970  308 RISQASATQRAGRAGRLEPGVCYRLW-SEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDL-----RWLDAPPSV 381
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1033 SLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASL 1092
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 ...
819-978 9.86e-74

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: 242.44  E-value: 9.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  819 MSIMDFEKVNLELIEALLEWIVdgkHSYPPGAILVFLPGLAEIKMLYEQLQSNSLFNNrrSNRCVIHPLHSSLSSEEQQA 898
Cdd:cd18791    17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPD--LGKLLVLPLHSSLPPEEQQR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  899 VFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRYDASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLF 978
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 ...
545-721 3.38e-71

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: 235.89  E-value: 3.38e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 --TVGYQIRLESVKS-SATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMS 701
Cdd:cd17981    81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                         170       180
                  ....*....|....*....|
gi 397493579  702 ATLNAELFSDYFNSCPVITI 721
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
545-721 1.86e-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: 1.86e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSL-NGPPekvANIICTQPRRISAISVAERVAKERAERVG 623
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYaNGIP---CRIFCTQPRRLAAIAVAERVAAERGEKIG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSA 702
Cdd:cd17987    78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
                         170
                  ....*....|....*....
gi 397493579  703 TLNAELFSDYFNSCPVITI 721
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 ...
529-721 6.29e-69

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: 231.65  E-value: 6.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  529 KQASRQFQSILQERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAI 608
Cdd:cd17972    43 REQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  609 SVAERVAKERAERVGLTVGYQIRLESV-KSSATRLLYCTTGVLLRRLEgdTALQGVSHIIVDEVHERTEESDFLLLVLKD 687
Cdd:cd17972   123 SVAERVAFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLLVVLRD 200
                         170       180       190
                  ....*....|....*....|....*....|....
gi 397493579  688 IVSQRPGLQVILMSATLNAELFSDYFNSCPVITI 721
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 ...
545-721 1.04e-67

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: 225.95  E-value: 1.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSL-NGPPEKVANIICTQPRRISAISVAERVAKERAERVG 623
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 -----LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVI 698
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                         170       180
                  ....*....|....*....|...
gi 397493579  699 LMSATLNAELFSDYFNSCPVITI 721
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
544-1093 5.42e-67

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 243.29  E-value: 5.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  544 SLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIP-QFILDDSLNGppekvaNIICTQPRRISAISVAERVAKERAERV 622
Cdd:PRK11664    3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  623 GLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDiVSQ--RPGLQVILM 700
Cdd:PRK11664   77 GETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLD-VQQglRDDLKLLIM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  701 SATLNAELFSDYFNSCPVITIPGRTFPVDqffledaiavTRYvlqdgSPymrsmkqiskeklkarrnrtafeeveedlrL 780
Cdd:PRK11664  156 SATLDNDRLQQLLPDAPVIVSEGRSFPVE----------RRY-----QP------------------------------L 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  781 SLHLQDQDSVKDAVpdqqldfKQLLARykgvsksviktmsimdfekvnlelieallewivdgkhsyPPGAILVFLPGLAE 860
Cdd:PRK11664  191 PAHQRFDEAVARAT-------AELLRQ---------------------------------------ESGSLLLFLPGVGE 224
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  861 IKMLYEQLQsnslfnNRRSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDSGKMKEKRY 940
Cdd:PRK11664  225 IQRVQEQLA------SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARF 298
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  941 DASKGMESLEDTFVSQANALQRKGRAGRVASGVCFHLFTSHHYNHQLLkQQLPEIQRVPLEQLCLRikiLEMFSAHNLQS 1020
Cdd:PRK11664  299 DPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAA-QSEPEILHSDLSGLLLE---LLQWGCHDPAQ 374
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 397493579 1021 VfsRLIEPPHTDSLRASKIRLRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRclDPALTIAASLA 1093
Cdd:PRK11664  375 L--SWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLA 443
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
545-721 1.69e-65

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: 219.28  E-value: 1.69e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSAT 703
Cdd:cd17976    81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
                         170
                  ....*....|....*...
gi 397493579  704 LNAELFSDYFNSCPVITI 721
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 ...
534-721 9.33e-61

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: 206.11  E-value: 9.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  534 QFQSILQERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVanIICTQPRRISAISVAER 613
Cdd:cd17973     2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  614 VAKERAERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRP 693
Cdd:cd17973    80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
                         170       180
                  ....*....|....*....|....*...
gi 397493579  694 GLQVILMSATLNAELFSDYFNSCPVITI 721
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 ...
545-721 1.12e-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: 199.59  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppekvaNIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17979    74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
                         170
                  ....*....|....*..
gi 397493579  705 NAELFSDYFNSCPVITI 721
Cdd:cd17979   154 NIELFSGYFEGAPVVQV 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
545-721 6.93e-56

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: 191.80  E-value: 6.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA----RGGMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQR-----PGLQVIL 699
Cdd:cd17978    77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156
                         170       180
                  ....*....|....*....|..
gi 397493579  700 MSATLNAELFSDYFNSCPVITI 721
Cdd:cd17978   157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
545-715 8.93e-55

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: 188.86  E-value: 8.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgpPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPG-LQVILMSAT 703
Cdd:cd17988    79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSAT 158
                         170
                  ....*....|..
gi 397493579  704 LNAELFSDYFNS 715
Cdd:cd17988   159 ISCKEFADYFTT 170
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
545-721 2.91e-51

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: 178.47  E-value: 2.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDslnGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17974    78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
                         170
                  ....*....|....*..
gi 397493579  705 NAELFSDYFNSCPVITI 721
Cdd:cd17974   158 DAEKFSAFFDDAPIFRI 174
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
540-722 4.08e-51

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: 178.06  E-value: 4.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  540 QERQSLPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERA 619
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYT----SRGKIGCTQPRRVAAMSVAKRVAEEFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  620 ERVGLTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVIL 699
Cdd:cd17971    77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156
                         170       180
                  ....*....|....*....|...
gi 397493579  700 MSATLNAELFSDYFNSCPVITIP 722
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 ...
243-426 7.53e-51

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: 174.69  E-value: 7.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  243 DECMEQRQEEAFALKSICGEKFIERIQNRVWTIGLELEYLtsrfrkskpkestknvqensleickfylkgnckfgskcrf 322
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  323 khevppnqivgriersvddshlnaiedasFLYELEIRFSKDHKYPYQAPLVAFYSTNENLPLACRLHISEFLYDKALTFA 402
Cdd:cd23825    41 -----------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELA 91
                         170       180
                  ....*....|....*....|....
gi 397493579  403 ETSEPVVYSLITLLEEESEIVKLL 426
Cdd:cd23825    92 EDGEPVVFSLVSLLEDEEEILELL 115
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
545-715 9.27e-51

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: 177.28  E-value: 9.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDdslNGPPEKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAE---AGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSAT 703
Cdd:cd17980    78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157
                         170
                  ....*....|..
gi 397493579  704 LNAELFSDYFNS 715
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 ...
545-721 2.26e-48

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: 169.95  E-value: 2.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYT----DYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17983    77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
                         170
                  ....*....|....*..
gi 397493579  705 NAELFSDYFNSCPVITI 721
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 ...
545-721 1.12e-43

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: 156.85  E-value: 1.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppekVANIIC-TQPRRISAISVAERVAKERAERVG 623
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRG-----IRGLIGhTQPRRLAARSVAERIAEELKTELG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSAT 703
Cdd:cd17989    76 GAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSAT 155
                         170
                  ....*....|....*...
gi 397493579  704 LNAELFSDYFNSCPVITI 721
Cdd:cd17989   156 IDAERFSRHFNNAPIIEV 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
545-719 2.78e-42

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: 152.87  E-value: 2.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPpekvANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQ-RPGLQVILMSAT 703
Cdd:cd17990    77 TVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLlRDDLRLLAMSAT 156
                         170
                  ....*....|....*.
gi 397493579  704 LNAELFSDYFNSCPVI 719
Cdd:cd17990   157 LDGDGLAALLPEAPVV 172
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
545-721 1.82e-40

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: 148.27  E-value: 1.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVANII-CTQPRRISAISVAERVAKERAErVG 623
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIgITQPRRVAAVSMAKRVAEELNV-FG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQR----------- 692
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRaklylqdqtvk 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 397493579  693 PgLQVILMSATLNAELFSD----YFNSCPVITI 721
Cdd:cd17982   160 P-LKLVIMSATLRVEDFTEnkllFPRPPPVIKV 191
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
545-721 2.65e-37

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: 138.45  E-value: 2.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNgppeKVANIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS----QHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQR-PG----LQVIL 699
Cdd:cd17984    77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKsPNrkehLKVVV 156
                         170       180
                  ....*....|....*....|..
gi 397493579  700 MSATLNAELFSDYFNSCPVITI 721
Cdd:cd17984   157 MSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
545-719 1.08e-33

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: 128.02  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVAnIICTQPRRISAISVAERVAKERAERVGL 624
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  625 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILMSATL 704
Cdd:cd17977    80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
                         170
                  ....*....|....*
gi 397493579  705 NAELFSDYFNSCPVI 719
Cdd:cd17977   160 LSSKLLSYYGNVPLI 174
DEXDc smart00487
DEAD-like helicases superfamily;
551-731 2.11e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.96  E-value: 2.11e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579    551 RETILNLLRKHQVVVISGMTGCGKTTQIPQFILDDSLNGPPEKVaniICTQPRRISAISVAERVAKE----RAERVGLTV 626
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLgpslGLKVVGLYG 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579    627 GYQIR--LESVKSSATRLLYCTTGVLLRRLE-GDTALQGVSHIIVDEVHERTEES--DFLLLVLKDIvsqRPGLQVILMS 701
Cdd:smart00487   91 GDSKReqLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLL---PKNVQLLLLS 167
                           170       180       190
                    ....*....|....*....|....*....|....
gi 397493579    702 ATL--NAELFSDYFNSCPVITIPGRT--FPVDQF 731
Cdd:smart00487  168 ATPpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
545-721 2.81e-24

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 101.13  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  545 LPAWEERETILNLLRKHQ-VVVISGMTGCGKTTQIPQFILDDSLNGPPEKvANIICTQPRRISAISVAERVAKERAERVG 623
Cdd:cd17986     1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGFQK-GQVTVTQPHPLAARSLALRVADEMDLNLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  624 LTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHERTEESDFLLLVLKDIVSQRPGLQVILM-SA 702
Cdd:cd17986    80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVtSP 159
                         170
                  ....*....|....*....
gi 397493579  703 TLNAELFSdYFNSCPVITI 721
Cdd:cd17986   160 ALEPKLRA-FWGNPPVVHV 177
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
1044-1126 1.02e-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: 96.18  E-value: 1.02e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   1044 LGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFvsPWDKKEEANQKKLEFAFANSDYL 1123
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 397493579   1124 ALL 1126
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1041-1120 1.86e-23

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: 96.15  E-value: 1.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1041 LRDLGALTPDERLTPLGYHLASLPVDVRIGKLMLFGSIFRCLDPALTIAASLAFKSPFVSP----WDKKEEANQKKLEFA 1116
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldPRSAAKAARRRRRAA 84

                   ....
gi 397493579  1117 FANS 1120
Cdd:pfam04408   85 DEKA 88
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1214-1311 1.07e-22

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: 93.09  E-value: 1.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  1214 ISAMLCAALYPNVVqvkspegkfqktstgavRMQPKSAELKFVtKNDGYVHIHPSSVNYQVRHFDSPYLLYHEKIKTSRV 1293
Cdd:pfam07717    1 LRAALAAGLYPNVA-----------------RRDPKGKGYTTL-SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 397493579  1294 FIRDCSMVSVYPLVLFGG 1311
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
182-219 2.57e-17

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: 76.58  E-value: 2.57e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 397493579  182 VSPFAVQKLSRYGFNTERCQAVLRMCDGDVGASLEHLL 219
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
830-969 7.16e-14

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 69.16  E-value: 7.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   830 ELIEALLEWIvdgkHSYPPGAILVFLPGlaeIKMLYEQLqsnsLFNNRRSNrcvIHPLHSSLSSEEQQAVFVKPPAGVTK 909
Cdd:pfam00271    1 EKLEALLELL----KKERGGKVLIFSQT---KKTLEAEL----LLEKEGIK---VARLHGDLSQEEREEILEDFRKGKID 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   910 IIISTNIAETSITIDDVVYVIDsgkmkekrYDASKGMESLedtfvsqanaLQRKGRAGRV 969
Cdd:pfam00271   67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
554-972 7.56e-14

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 76.55  E-value: 7.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  554 ILNLLRKHQVVVISGMTGCGKTTQIPQFIL-----------DDSLNGPPEKvANIICTQPR----RISAISVAERVAKER 618
Cdd:PHA02653  172 IFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdnLDKIDPNFIE-RPIVLSLPRvalvRLHSITLLKSLGFDE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  619 AERVGLTVGY---QIRLESVKSSATRLLYCTTGVLLrrlegdTALQGVSHIIVDEVHERTEESDFLLLVL-KDIVSQRpg 694
Cdd:PHA02653  251 IDGSPISLKYgsiPDELINTNPKPYGLVFSTHKLTL------NKLFDYGTVIIDEVHEHDQIGDIIIAVArKHIDKIR-- 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  695 lQVILMSATL--NAELFSDYFNSCPVITIPGRT-FPVDQFfledaiavtrYVLQDGSPYMRsmkqiskeklkarrnrtaF 771
Cdd:PHA02653  323 -SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV----------YVKNKYNPKNK------------------R 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  772 EEVEEDLRLSLHlqdqdSVKDAVPDQQldfkqllarykgvsKSVI---KTMSIMDFEKVNLE-LIEALLEWIVDGKhsyp 847
Cdd:PHA02653  374 AYIEEEKKNIVT-----ALKKYTPPKG--------------SSGIvfvASVSQCEEYKKYLEkRLPIYDFYIIHGK---- 430
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  848 pgailvfLPGLAEIkmlyeqlqSNSLFNNRRsnrcvihplhsslsseeqqavfvkppagvTKIIISTNIAETSITIDDVV 927
Cdd:PHA02653  431 -------VPNIDEI--------LEKVYSSKN-----------------------------PSIIISTPYLESSVTIRNAT 466
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 397493579  928 YVIDSGKMKEKR-YDAskgmeslEDTFVSQANALQRKGRAGRVASG 972
Cdd:PHA02653  467 HVYDTGRVYVPEpFGG-------KEMFISKSMRTQRKGRVGRVSPG 505
HELICc smart00490
helicase superfamily c-terminal domain;
878-968 2.14e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.85  E-value: 2.14e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579    878 RSNRCVIHPLHSSLSSEEQQAVFVKPPAGVTKIIISTNIAETSITIDDVVYVIDsgkmkekrYDASKGMESLedtfvsqa 957
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDLPWSPASY-------- 71
                            90
                    ....*....|.
gi 397493579    958 naLQRKGRAGR 968
Cdd:smart00490   72 --IQRIGRAGR 80
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
551-708 3.18e-13

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: 68.81  E-value: 3.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   551 RETILNLLRKHQVVVISGmTGCGKTT--QIPqfILDDSLNGPPEKVANIICtqPRRISAISVAERvAKERAERVGLTV-- 626
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVas 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   627 ---GYQIRLESVKSSATRLLYCTTGVLLRRLEGDTALQGVSHIIVDEVHeRTEESDFlLLVLKDIVSQ-RPGLQVILMSA 702
Cdd:pfam00270   79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGF-GPDLEEILRRlPKKRQILLLSA 156

                   ....*.
gi 397493579   703 TLNAEL 708
Cdd:pfam00270  157 TLPRNL 162
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
564-703 4.36e-13

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: 68.20  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  564 VVISGMTGCGKTTQIPQFILDDSLNGPPeKVAnIICtqPRRISAISVAERVAKERAE--RVGLTVGY---QIRLESVKSS 638
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGK-KVL-VLV--PTKALALQTAERLRELFGPgiRVAVLVGGssaEEREKNKLGD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 397493579  639 AtRLLYCTTGVLLRRLEGDTAL--QGVSHIIVDEVHERTEESDFLLLV-LKDIVSQRPGLQVILMSAT 703
Cdd:cd00046    80 A-DIIIATPDMLLNLLLREDRLflKDLKLIIVDEAHALLIDSRGALILdLAVRKAGLKNAQVILLSAT 146
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
323-420 6.62e-07

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: 49.24  E-value: 6.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579   323 KHEVPPNQIVGRIERSVDDSHLNAIEDASFLYELEIRFSKDHKYPYQAPLVAFySTNENLPLACRLHISEFLYDKALTFa 402
Cdd:pfam05773   17 EFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISL-SSPWNLSDEQVLSLLEELEELAEEN- 94
                           90
                   ....*....|....*...
gi 397493579   403 eTSEPVVYSLITLLEEES 420
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 ...
306-324 1.07e-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: 45.87  E-value: 1.07e-06
                           10
                   ....*....|....*....
gi 397493579   306 CKFYLKGNCKFGSKCRFKH 324
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
ZnF_C3H1 smart00356
zinc finger;
304-324 1.49e-06

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 45.70  E-value: 1.49e-06
                            10        20
                    ....*....|....*....|.
gi 397493579    304 EICKFYLKGNCKFGSKCRFKH 324
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
564-722 2.00e-06

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: 49.57  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  564 VVISGMTGCGKTTQIPQFILDdSLNGPPEKVaniICTQPRRisAIsVAERVA--KERAERVGLTVGYQIRLESV---KSS 638
Cdd:cd17921    20 VLVSAPTSSGKTLIAELAILR-ALATSGGKA---VYIAPTR--AL-VNQKEAdlRERFGPLGKNVGLLTGDPSVnklLLA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  639 ATRLLYCTT---GVLLRRLEGDTaLQGVSHIIVDEVH--ERTEESDFLLLVLKDIVSQRPGLQVILMSATL-NAELFSDY 712
Cdd:cd17921    93 EADILVATPeklDLLLRNGGERL-IQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARFVGLSATLpNAEDLAEW 171
                         170
                  ....*....|
gi 397493579  713 FNSCPVITIP 722
Cdd:cd17921   172 LGVEDLIRFD 181
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
305-324 6.54e-06

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: 43.73  E-value: 6.54e-06
                           10        20
                   ....*....|....*....|
gi 397493579   305 ICKFYLKGNCKFGSKCRFKH 324
Cdd:pfam18044    2 LCRYFQKGGCRYGDNCRFSH 21
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
304-324 2.18e-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: 2.18e-05
                           10        20
                   ....*....|....*....|..
gi 397493579   304 EICKFYLK-GNCKFGSKCRFKH 324
Cdd:pfam00642    4 ELCRFFLRtGYCKYGDRCKFAH 25
zf-CCCH_2 pfam14608
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ...
305-324 3.67e-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: 39.03  E-value: 3.67e-04
                           10        20
                   ....*....|....*....|
gi 397493579   305 ICKFYlkGNCKFGSKCRFKH 324
Cdd:pfam14608    1 PCRFG--GNCTFGPKCPFSH 18
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
619-711 1.16e-03

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 43.39  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397493579  619 AERVGLTVGYqirlESVKSSAtRLLYCTTGVLLRRL-EGDTALQGVSHIIVDEVH-----ERT---EESdfLLLVLKDIv 689
Cdd:COG4581    94 AENVGLLTGD----ASVNPDA-PIVVMTTEILRNMLyREGADLEDVGVVVMDEFHyladpDRGwvwEEP--IIHLPARV- 165
                          90       100
                  ....*....|....*....|...
gi 397493579  690 sqrpglQVILMSATL-NAELFSD 711
Cdd:COG4581   166 ------QLVLLSATVgNAEEFAE 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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