NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|281427338|ref|NP_001163976|]
View 

putative ATP-dependent RNA helicase DHX57 [Xenopus tropicalis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
557-1109 1.40e-119

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: 390.21  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPShvsnIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGR----IGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSAT 715
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  716 LNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiakTRYvledgspyqrsskqLPGPDSARgkkgnsynelldELEQQIS 795
Cdd:COG1643   166 LDAERFARLLGDAPVIESSGRTYPVE----------VRY--------------RPLPADER------------DLEDAVA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  796 SSLRiqdskivkdsvpdqqlnvkelsvryngisksviktlssmdldkinldliEALLEwivngdhsyPPGAVLVFLPGLA 875
Cdd:COG1643   210 DAVR-------------------------------------------------EALAE---------EPGDILVFLPGER 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  876 EIKTLYDQLQsnalfnNRRSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKR 955
Cdd:COG1643   232 EIRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPR 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  956 YDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQyQLLDQQLPEIQR------IpLEQLCLRIKILEMF 1029
Cdd:COG1643   306 YDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRadlaslI-LELAAWGLGDPEDL 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338 1030 secrldlvfaRLIEPPRMESLHASKIRLQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLA 1109
Cdd:COG1643   384 ----------PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
246-424 2.66e-49

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: 170.07  E-value: 2.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  246 EECLERRQEEAFVLQSICGEKFVERIPNKVWTVGLEMDYLtkrlqkpkkkdsdkdlfqqmprnickyymkgencrfgskc 325
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  326 rfkheapkqnfkdeshlcangnnnCLYELEVRFPKDNKYPYQAPLLAFYSVNENLSMGCRLHITEYLYEKALNIAQTSDP 405
Cdd:cd23825    41 ------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAEDGEP 96
                         170
                  ....*....|....*....
gi 281427338  406 AVYTLVSCLEDEDEIVKLL 424
Cdd:cd23825    97 VVFSLVSLLEDEEEILELL 115
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
185-222 1.44e-16

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: 74.27  E-value: 1.44e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281427338  185 ISPFAVGKLSRYGFDKERCMNTLRSHDSDVGVSLEYLL 222
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
308-329 2.24e-05

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


:

Pssm-ID: 465626  Cd Length: 22  Bit Score: 42.19  E-value: 2.24e-05
                           10        20
                   ....*....|....*....|..
gi 281427338   308 NICKYYMKGeNCRFGSKCRFKH 329
Cdd:pfam18044    1 RLCRYFQKG-GCRYGDNCRFSH 21
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
557-1109 1.40e-119

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 390.21  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPShvsnIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGR----IGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSAT 715
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  716 LNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiakTRYvledgspyqrsskqLPGPDSARgkkgnsynelldELEQQIS 795
Cdd:COG1643   166 LDAERFARLLGDAPVIESSGRTYPVE----------VRY--------------RPLPADER------------DLEDAVA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  796 SSLRiqdskivkdsvpdqqlnvkelsvryngisksviktlssmdldkinldliEALLEwivngdhsyPPGAVLVFLPGLA 875
Cdd:COG1643   210 DAVR-------------------------------------------------EALAE---------EPGDILVFLPGER 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  876 EIKTLYDQLQsnalfnNRRSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKR 955
Cdd:COG1643   232 EIRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPR 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  956 YDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQyQLLDQQLPEIQR------IpLEQLCLRIKILEMF 1029
Cdd:COG1643   306 YDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRadlaslI-LELAAWGLGDPEDL 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338 1030 secrldlvfaRLIEPPRMESLHASKIRLQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLA 1109
Cdd:COG1643   384 ----------PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
557-733 1.86e-117

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: 361.08  E-value: 1.86e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATL 716
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 281427338  717 NAELFSCYFQDCPVLHI 733
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
555-1176 4.58e-87

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 308.62  E-value: 4.58e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   555 QKLPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASL--KGPPSHvsniicTQPRRISAISVAERVAQERAE 632
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRgsHGLIGH------TQPRRLAARTVAQRIAEELGT 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   633 RVGISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILM 712
Cdd:TIGR01967  138 PLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIIT 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   713 SATLNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiaktryvledgspyqrsskqlpgpdsargkkgnsynelldeleq 792
Cdd:TIGR01967  218 SATIDPERFSRHFNNAPIIEVSGRTYPVE--------------------------------------------------- 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   793 qissslriqdskivkdsvpdqqlnvkelsVRYNGISKsviktlssmDLDKINLDLIEALLEwIVNGDHSYPPGAVLVFLP 872
Cdd:TIGR01967  247 -----------------------------VRYRPLVE---------EQEDDDLDQLEAILD-AVDELFAEGPGDILIFLP 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   873 GLAEIKTLYDQLqsnalfNNRRSKRCVIYPLHSSLSSDEQQSVFlKPPPGvTKIIISTNIAETSITIDDVVYVIDSGKMR 952
Cdd:TIGR01967  288 GEREIRDAAEIL------RKRNLRHTEILPLYARLSNKEQQRVF-QPHSG-RRIVLATNVAETSLTVPGIHYVIDTGTAR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   953 EKRYDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQYQLLDQQlPEIQRIPLEQLCLRIKILemfsec 1032
Cdd:TIGR01967  360 ISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLAL------ 432
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  1033 RL-DLVFARLIEPPRMESLHASKIRLQDLGALTKEE---KLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASL 1108
Cdd:TIGR01967  433 RLgDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASAL 512
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281427338  1109 AFKSPFVCPWDKKEEANKKKQEFATANSDHLALLQAYQAWSSVIKESSRAAYQ-YCRDNFLS---VRVLQEI 1176
Cdd:TIGR01967  513 SIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFRnACRKQYLNylrVREWQDI 584
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
557-1176 2.05e-79

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 285.80  E-value: 2.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDAS--LKGPPSHvsniicTQPRRISAISVAERVAQERAERV 634
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGrgVKGLIGH------TQPRRLAARTVANRIAEELETEL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  635 GISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:PRK11131  147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  715 TLNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiakTRY--VLEDGSPYQRsskqlpgpdsargkkgnsynellDELEq 792
Cdd:PRK11131  227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRYrpIVEEADDTER-----------------------DQLQ- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  793 qissslriqdskivkdsvpdqqlnvkelsvrynGIsksviktlssmdldkinLDLIEALlewivnGDHSypPGAVLVFLP 872
Cdd:PRK11131  273 ---------------------------------AI-----------------FDAVDEL------GREG--PGDILIFMS 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  873 GLAEIKTLYDQLQSNALfnnrrsKRCVIYPLHSSLSSDEQQSVFlkPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMR 952
Cdd:PRK11131  295 GEREIRDTADALNKLNL------RHTEILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTAR 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  953 EKRYDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHY--QYQLLDqqlPEIQRIPLEQLclrikILEMFS 1030
Cdd:PRK11131  367 ISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFlsRPEFTD---PEILRTNLASV-----ILQMTA 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338 1031 ECRLDLVFARLIEPPRMESLHASKIRLQDLGALTKEE-----KLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIA 1105
Cdd:PRK11131  439 LGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIIT 518
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281427338 1106 ASLAFKSPFVCPWDKKEEANKKKQEFATANSDHLALLQAYQAWSSVIKESSRAAY-QYCRDNFLS---VRVLQEI 1176
Cdd:PRK11131  519 SALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLNylrVREWQDI 593
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
246-424 2.66e-49

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: 170.07  E-value: 2.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  246 EECLERRQEEAFVLQSICGEKFVERIPNKVWTVGLEMDYLtkrlqkpkkkdsdkdlfqqmprnickyymkgencrfgskc 325
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  326 rfkheapkqnfkdeshlcangnnnCLYELEVRFPKDNKYPYQAPLLAFYSVNENLSMGCRLHITEYLYEKALNIAQTSDP 405
Cdd:cd23825    41 ------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAEDGEP 96
                         170
                  ....*....|....*....
gi 281427338  406 AVYTLVSCLEDEDEIVKLL 424
Cdd:cd23825    97 VVFSLVSLLEDEEEILELL 115
DEXDc smart00487
DEAD-like helicases superfamily;
563-743 1.72e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 1.72e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338    563 QDQILE-LLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVsniICTQPRRISAISVAERVAQERAERVGISVGY- 640
Cdd:smart00487   13 QKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLGPSLGLKVVGLy 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338    641 -----QIRLESVKSAATRLLYCTTGVLLRRLE-GDTTLQNVTHVVVDEVHeRTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:smart00487   90 ggdskREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKNVQLLLLSA 168
                           170       180       190
                    ....*....|....*....|....*....|...
gi 281427338    715 TL--NAELFSCYFQDCPVLHIPGRT--FPVDQY 743
Cdd:smart00487  169 TPpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1057-1141 1.72e-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: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  1057 LQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLAFKSPFV-------------CPWDKKEE 1123
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVqpnfldprsaakaARRRRRAA 84
                           90       100
                   ....*....|....*....|
gi 281427338  1124 ANKKKQEFA--TANSDHLAL 1141
Cdd:pfam04408   85 DEKARAKFArlDLEGDHLTL 104
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
185-222 1.44e-16

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: 74.27  E-value: 1.44e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281427338  185 ISPFAVGKLSRYGFDKERCMNTLRSHDSDVGVSLEYLL 222
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
308-329 2.24e-05

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


Pssm-ID: 465626  Cd Length: 22  Bit Score: 42.19  E-value: 2.24e-05
                           10        20
                   ....*....|....*....|..
gi 281427338   308 NICKYYMKGeNCRFGSKCRFKH 329
Cdd:pfam18044    1 RLCRYFQKG-GCRYGDNCRFSH 21
ZnF_C3H1 smart00356
zinc finger;
309-329 1.39e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 39.92  E-value: 1.39e-04
                            10        20
                    ....*....|....*....|.
gi 281427338    309 ICKYYMKGeNCRFGSKCRFKH 329
Cdd:smart00356    6 LCKFFKRG-YCPRGDRCKFAH 25
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
345-417 4.44e-04

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: 41.16  E-value: 4.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281427338   345 NGNNNCLYELEVRFPKDnkYPYQAPLLAFySVNENLSMGCRLHITEYLYEKAlnIAQTSDPAVYTLVSCLEDE 417
Cdd:pfam05773   43 DSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELA--EENLGEVMIFELIEWLQEN 110
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
557-1109 1.40e-119

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 390.21  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPShvsnIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGR----IGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSAT 715
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  716 LNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiakTRYvledgspyqrsskqLPGPDSARgkkgnsynelldELEQQIS 795
Cdd:COG1643   166 LDAERFARLLGDAPVIESSGRTYPVE----------VRY--------------RPLPADER------------DLEDAVA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  796 SSLRiqdskivkdsvpdqqlnvkelsvryngisksviktlssmdldkinldliEALLEwivngdhsyPPGAVLVFLPGLA 875
Cdd:COG1643   210 DAVR-------------------------------------------------EALAE---------EPGDILVFLPGER 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  876 EIKTLYDQLQsnalfnNRRSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKR 955
Cdd:COG1643   232 EIRRTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPR 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  956 YDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQyQLLDQQLPEIQR------IpLEQLCLRIKILEMF 1029
Cdd:COG1643   306 YDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRadlaslI-LELAAWGLGDPEDL 383
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338 1030 secrldlvfaRLIEPPRMESLHASKIRLQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLA 1109
Cdd:COG1643   384 ----------PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
557-733 1.86e-117

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: 361.08  E-value: 1.86e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATL 716
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 281427338  717 NAELFSCYFQDCPVLHI 733
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) ...
574-733 1.21e-87

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 279.73  E-value: 1.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  574 QVLVVSGMTGCGKTTQIPQFILDASLKGPPSHvsNIICTQPRRISAISVAERVAQERAERVGISVGYQIRLESVKSAATR 653
Cdd:cd17917     2 QVVVIVGETGSGKTTQVPQFLLEDGLAKGGKG--RIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  654 LLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATLNAELFSCYFQDCPVLHI 733
Cdd:cd17917    80 IKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
555-1176 4.58e-87

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 308.62  E-value: 4.58e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   555 QKLPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASL--KGPPSHvsniicTQPRRISAISVAERVAQERAE 632
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRgsHGLIGH------TQPRRLAARTVAQRIAEELGT 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   633 RVGISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILM 712
Cdd:TIGR01967  138 PLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIIT 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   713 SATLNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiaktryvledgspyqrsskqlpgpdsargkkgnsynelldeleq 792
Cdd:TIGR01967  218 SATIDPERFSRHFNNAPIIEVSGRTYPVE--------------------------------------------------- 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   793 qissslriqdskivkdsvpdqqlnvkelsVRYNGISKsviktlssmDLDKINLDLIEALLEwIVNGDHSYPPGAVLVFLP 872
Cdd:TIGR01967  247 -----------------------------VRYRPLVE---------EQEDDDLDQLEAILD-AVDELFAEGPGDILIFLP 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   873 GLAEIKTLYDQLqsnalfNNRRSKRCVIYPLHSSLSSDEQQSVFlKPPPGvTKIIISTNIAETSITIDDVVYVIDSGKMR 952
Cdd:TIGR01967  288 GEREIRDAAEIL------RKRNLRHTEILPLYARLSNKEQQRVF-QPHSG-RRIVLATNVAETSLTVPGIHYVIDTGTAR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   953 EKRYDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQYQLLDQQlPEIQRIPLEQLCLRIKILemfsec 1032
Cdd:TIGR01967  360 ISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLAL------ 432
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  1033 RL-DLVFARLIEPPRMESLHASKIRLQDLGALTKEE---KLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASL 1108
Cdd:TIGR01967  433 RLgDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASAL 512
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281427338  1109 AFKSPFVCPWDKKEEANKKKQEFATANSDHLALLQAYQAWSSVIKESSRAAYQ-YCRDNFLS---VRVLQEI 1176
Cdd:TIGR01967  513 SIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFRnACRKQYLNylrVREWQDI 584
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
557-1176 2.05e-79

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 285.80  E-value: 2.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDAS--LKGPPSHvsniicTQPRRISAISVAERVAQERAERV 634
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGrgVKGLIGH------TQPRRLAARTVANRIAEELETEL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  635 GISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:PRK11131  147 GGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  715 TLNAELFSCYFQDCPVLHIPGRTFPVDqyfledaiakTRY--VLEDGSPYQRsskqlpgpdsargkkgnsynellDELEq 792
Cdd:PRK11131  227 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRYrpIVEEADDTER-----------------------DQLQ- 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  793 qissslriqdskivkdsvpdqqlnvkelsvrynGIsksviktlssmdldkinLDLIEALlewivnGDHSypPGAVLVFLP 872
Cdd:PRK11131  273 ---------------------------------AI-----------------FDAVDEL------GREG--PGDILIFMS 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  873 GLAEIKTLYDQLQSNALfnnrrsKRCVIYPLHSSLSSDEQQSVFlkPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMR 952
Cdd:PRK11131  295 GEREIRDTADALNKLNL------RHTEILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTAR 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  953 EKRYDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHY--QYQLLDqqlPEIQRIPLEQLclrikILEMFS 1030
Cdd:PRK11131  367 ISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFlsRPEFTD---PEILRTNLASV-----ILQMTA 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338 1031 ECRLDLVFARLIEPPRMESLHASKIRLQDLGALTKEE-----KLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIA 1105
Cdd:PRK11131  439 LGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIIT 518
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281427338 1106 ASLAFKSPFVCPWDKKEEANKKKQEFATANSDHLALLQAYQAWSSVIKESSRAAY-QYCRDNFLS---VRVLQEI 1176
Cdd:PRK11131  519 SALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLNylrVREWQDI 593
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
565-1165 1.30e-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: 276.65  E-value: 1.30e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   565 QILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGppshvSNIICTQPRRISAISVAERVAQERAERVGISVGYQIRL 644
Cdd:TIGR01970    9 ALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIG-----GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   645 ESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSATLNAELFSC 723
Cdd:TIGR01970   84 ENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQsSLREDLKILAMSATLDGERLSS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   724 YFQDCPVLHIPGRTFPVDqyfledaiakTRYvledgspyqrsskqLPGPDSARgkkgnsyneLLDELEQQISSSLRIQds 803
Cdd:TIGR01970  164 LLPDAPVVESEGRSFPVE----------IRY--------------LPLRGDQR---------LEDAVSRAVEHALASE-- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   804 kivkdsvpdqqlnvkelsvryngisksviktlssmdldkinldlieallewivngdhsypPGAVLVFLPGLAEIKTLYDQ 883
Cdd:TIGR01970  209 ------------------------------------------------------------TGSILVFLPGQAEIRRVQEQ 228
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   884 LQSnalfnnRRSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKRYDPGKSME 963
Cdd:TIGR01970  229 LAE------RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGIT 302
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   964 SLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQyQLLDQQLPEIQRIPLEQLCLriKILEMFSECRLDLvfaRLIE 1043
Cdd:TIGR01970  303 RLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLAL--ELAQWGAKDPSDL---RWLD 376
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  1044 PPRMESLHASKIRLQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLafkspfvcpwdkkEE 1123
Cdd:TIGR01970  377 APPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL-------------EE 443
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 281427338  1124 ANKKKQefatANSD-HLALLQAYQAWSSVIKESSRAAYQYCRD 1165
Cdd:TIGR01970  444 RGLPRQ----GGADlMNRLHRLQQGRQGRGQRAQQLAKKLRRR 482
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
836-994 4.12e-76

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: 248.60  E-value: 4.12e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  836 SSMDLDKINLDLIEALLEWIvngDHSYPPGAVLVFLPGLAEIKTLYDQLQSNALFNNrrSKRCVIYPLHSSLSSDEQQSV 915
Cdd:cd18791    18 SSEKEDPDYVDAAVRLILQI---HRTEEPGDILVFLPGQEEIERLCELLREELLSPD--LGKLLVLPLHSSLPPEEQQRV 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281427338  916 FLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKRYDPGKSMESLEDTWVSRANAMQRKGRAGRVASGVCFHLF 994
Cdd:cd18791    93 FEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
557-733 3.95e-69

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: 229.34  E-value: 3.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 --SVGYQIRLESVKS-AATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMS 713
Cdd:cd17981    81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                         170       180
                  ....*....|....*....|
gi 281427338  714 ATLNAELFSCYFQDCPVLHI 733
Cdd:cd17981   161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
557-733 8.10e-67

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: 222.78  E-value: 8.10e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLK-GPPSHvsnIICTQPRRISAISVAERVAQERAERVG 635
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYAnGIPCR---IFCTQPRRLAAIAVAERVAAERGEKIG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  636 ISVGYQIRLESVKSAATRLLYCTTGVLLRRL-EGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:cd17987    78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
                         170
                  ....*....|....*....
gi 281427338  715 TLNAELFSCYFQDCPVLHI 733
Cdd:cd17987   158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
557-733 9.42e-66

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 219.79  E-value: 9.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFIL-DASLKGPPSHVSNIICTQPRRISAISVAERVAQERAERVG 635
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLeDLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  636 IS-----VGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKII 710
Cdd:cd17975    81 PGgknslCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                         170       180
                  ....*....|....*....|...
gi 281427338  711 LMSATLNAELFSCYFQDCPVLHI 733
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
546-733 1.14e-64

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: 218.94  E-value: 1.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  546 NYQSMLEERQKLPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNIICTQPRRISAISVAER 625
Cdd:cd17972    48 NLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  626 VAQERAERVGISVGYQIRLESV-KSAATRLLYCTTGVLLRRLEgdTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLR 704
Cdd:cd17972   128 VAFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLE--AGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAY 205
                         170       180
                  ....*....|....*....|....*....
gi 281427338  705 PDLKIILMSATLNAELFSCYFQDCPVLHI 733
Cdd:cd17972   206 PDLRVILMSATIDTSMFCEYFFNCPVIEV 234
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
568-1109 5.17e-63

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 230.58  E-value: 5.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  568 ELLSKY----QVLVvSGMTGCGKTTQIP-QFILDASLKGppshvsNIICTQPRRISAISVAERVAQERAERVGISVGYQI 642
Cdd:PRK11664   12 ELLTALktapQVLL-KAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYRM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  643 RLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSATLNAELF 721
Cdd:PRK11664   85 RAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQqGLRDDLKLLIMSATLDNDRL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  722 SCYFQDCPVLHIPGRTFPVDqyfledaiakTRYvledgspyqrsskqlpgpdsargkkgnsynelldeleQQISSSLRIQ 801
Cdd:PRK11664  165 QQLLPDAPVIVSEGRSFPVE----------RRY-------------------------------------QPLPAHQRFD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  802 DSkivkdsvpdqqlnvkelsvryngisksVIKTLSSMdLDKinldlieallewivngdhsyPPGAVLVFLPGLAEIKTLY 881
Cdd:PRK11664  198 EA---------------------------VARATAEL-LRQ--------------------ESGSLLLFLPGVGEIQRVQ 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  882 DQLQsnalfnNRRSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSGKMREKRYDPGKS 961
Cdd:PRK11664  230 EQLA------SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTG 303
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  962 MESLEDTWVSRANAMQRKGRAGRVASGVCFHLFTSHHYQyQLLDQQLPEIQRIPLEQLclrikILEMFS-ECRlDLVFAR 1040
Cdd:PRK11664  304 LTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGL-----LLELLQwGCH-DPAQLS 376
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281427338 1041 LIEPPRMESLHASKIRLQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRclDPALTIAASLA 1109
Cdd:PRK11664  377 WLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLA 443
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
557-733 3.91e-61

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: 206.14  E-value: 3.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLkgppshvSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGF-------RHIACTQPRRIACISLAKRVAFESLNQYGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATL 716
Cdd:cd17979    74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
                         170
                  ....*....|....*..
gi 281427338  717 NAELFSCYFQDCPVLHI 733
Cdd:cd17979   154 NIELFSGYFEGAPVVQV 170
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
557-733 5.19e-61

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: 206.18  E-value: 5.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLES-VKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSAT 715
Cdd:cd17976    81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
                         170
                  ....*....|....*...
gi 281427338  716 LNAELFSCYFQDCPVLHI 733
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 ...
546-733 4.05e-59

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: 201.10  E-value: 4.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  546 NYQSMLEERQKLPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPShvSNIICTQPRRISAISVAER 625
Cdd:cd17973     2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPK--KLVACTQPRRVAAMSVAQR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  626 VAQERAERVGISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRP 705
Cdd:cd17973    80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
                         170       180
                  ....*....|....*....|....*...
gi 281427338  706 DLKIILMSATLNAELFSCYFQDCPVLHI 733
Cdd:cd17973   160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
557-733 2.76e-54

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 187.18  E-value: 2.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGppshVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFAR----GGMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLR-----PDLKIIL 711
Cdd:cd17978    77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156
                         170       180
                  ....*....|....*....|..
gi 281427338  712 MSATLNAELFSCYFQDCPVLHI 733
Cdd:cd17978   157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
557-725 8.94e-53

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 182.70  E-value: 8.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKgpPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYK--RGKYCNIVVTQPRRIAAISIARRVSQEREWTLGS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDvmVLRPD---LKIILMS 713
Cdd:cd17988    79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRR--LLRTNsrhVKIILMS 156
                         170
                  ....*....|..
gi 281427338  714 ATLNAELFSCYF 725
Cdd:cd17988   157 ATISCKEFADYF 168
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
557-733 1.01e-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: 179.62  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDAslkGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATL 716
Cdd:cd17974    78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
                         170
                  ....*....|....*..
gi 281427338  717 NAELFSCYFQDCPVLHI 733
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 ...
552-734 1.28e-50

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 176.52  E-value: 1.28e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  552 EERQKLPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLkgppSHVSNIICTQPRRISAISVAERVAQERA 631
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGY----TSRGKIGCTQPRRVAAMSVAKRVAEEFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  632 ERVGISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIIL 711
Cdd:cd17971    77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIV 156
                         170       180
                  ....*....|....*....|...
gi 281427338  712 MSATLNAELFSCYFQDCPVLHIP 734
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 ...
246-424 2.66e-49

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: 170.07  E-value: 2.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  246 EECLERRQEEAFVLQSICGEKFVERIPNKVWTVGLEMDYLtkrlqkpkkkdsdkdlfqqmprnickyymkgencrfgskc 325
Cdd:cd23825     1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  326 rfkheapkqnfkdeshlcangnnnCLYELEVRFPKDNKYPYQAPLLAFYSVNENLSMGCRLHITEYLYEKALNIAQTSDP 405
Cdd:cd23825    41 ------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALELAEDGEP 96
                         170
                  ....*....|....*....
gi 281427338  406 AVYTLVSCLEDEDEIVKLL 424
Cdd:cd23825    97 VVFSLVSLLEDEEEILELL 115
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
557-726 6.07e-49

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 171.88  E-value: 6.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDAslkGPPSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEA---GWTAGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLES-VKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSAT 715
Cdd:cd17980    78 EVGYCIRFDDcTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157
                         170
                  ....*....|.
gi 281427338  716 LNAELFSCYFQ 726
Cdd:cd17980   158 LDAEKFRDFFN 168
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
557-733 1.20e-44

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 159.16  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLkgppsHVSNII-CTQPRRISAISVAERVAQERAERVG 635
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGY-----TDYGMIgCTQPRRVAAMSVAKRVSEEMGVELG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  636 ISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSAT 715
Cdd:cd17983    76 EEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSAT 155
                         170
                  ....*....|....*...
gi 281427338  716 LNAELFSCYFQDCPVLHI 733
Cdd:cd17983   156 MDADKFADFFGNVPIFTI 173
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
557-733 6.82e-44

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 157.23  E-value: 6.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASL--KGPPSHvsniicTQPRRISAISVAERVAQERAERV 634
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRgiRGLIGH------TQPRRLAARSVAERIAEELKTEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  635 GISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:cd17989    75 GGAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSA 154
                         170
                  ....*....|....*....
gi 281427338  715 TLNAELFSCYFQDCPVLHI 733
Cdd:cd17989   155 TIDAERFSRHFNNAPIIEV 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
564-731 2.42e-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: 152.49  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  564 DQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPpshvSNIICTQPRRISAISVAERVAQERAERVGISVGYQIR 643
Cdd:cd17990     8 PALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAG----GKIIVLEPRRVAARAAARRLATLLGEAPGETVGYRVR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  644 LESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVM-VLRPDLKIILMSATLNAELFS 722
Cdd:cd17990    84 GESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSATLDGDGLA 163

                  ....*....
gi 281427338  723 CYFQDCPVL 731
Cdd:cd17990   164 ALLPEAPVV 172
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
557-722 5.92e-39

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: 143.65  E-value: 5.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSNII-CTQPRRISAISVAERVAQERAErVG 635
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIgITQPRRVAAVSMAKRVAEELNV-FG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  636 ISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPD--------- 706
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
                         170
                  ....*....|....*..
gi 281427338  707 -LKIILMSATLNAELFS 722
Cdd:cd17982   160 pLKLVIMSATLRVEDFT 176
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
557-733 2.00e-38

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: 141.53  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLkgppSHVSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF----SQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRP-----DLKIIL 711
Cdd:cd17984    77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVV 156
                         170       180
                  ....*....|....*....|..
gi 281427338  712 MSATLNAELFSCYFQDCPVLHI 733
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 ...
557-733 2.37e-32

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: 124.17  E-value: 2.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHvSNIICTQPRRISAISVAERVAQERAERVGI 636
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQH-GVVVCTQVHKQTAVWLALRVADEMDVNIGH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  637 SVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSATL 716
Cdd:cd17977    80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
                         170
                  ....*....|....*..
gi 281427338  717 NAELFSCYFQDCPVLHI 733
Cdd:cd17977   160 LSSKLLSYYGNVPLIEV 176
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
557-733 3.27e-28

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: 112.30  E-value: 3.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  557 LPAWQKQDQILELL-SKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVSnIICTQPRRISAISVAERVAQERAERVG 635
Cdd:cd17986     1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKGQ-VTVTQPHPLAARSLALRVADEMDLNLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  636 ISVGYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHERTEESDFLLLVLKDVMVLRPDLKIILMSAT 715
Cdd:cd17986    80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSP 159
                         170
                  ....*....|....*...
gi 281427338  716 LNAELFSCYFQDCPVLHI 733
Cdd:cd17986   160 ALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
563-743 1.72e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 1.72e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338    563 QDQILE-LLSKYQVLVVSGMTGCGKTTQIPQFILDASLKGPPSHVsniICTQPRRISAISVAERVAQERAERVGISVGY- 640
Cdd:smart00487   13 QKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELKKLGPSLGLKVVGLy 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338    641 -----QIRLESVKSAATRLLYCTTGVLLRRLE-GDTTLQNVTHVVVDEVHeRTEESDFLLLVLKDVMVLRPDLKIILMSA 714
Cdd:smart00487   90 ggdskREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKNVQLLLLSA 168
                           170       180       190
                    ....*....|....*....|....*....|...
gi 281427338    715 TL--NAELFSCYFQDCPVLHIPGRT--FPVDQY 743
Cdd:smart00487  169 TPpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
1060-1142 8.12e-25

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: 99.26  E-value: 8.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   1060 LGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLAFKSPFvcPWDKKEEANKKKQEFATANSDHL 1139
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 281427338   1140 ALL 1142
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1057-1141 1.72e-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: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  1057 LQDLGALTKEEKLTPLGYHLASLPVDVRIGKLMLFGAIFRCLDPALTIAASLAFKSPFV-------------CPWDKKEE 1123
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVqpnfldprsaakaARRRRRAA 84
                           90       100
                   ....*....|....*....|
gi 281427338  1124 ANKKKQEFA--TANSDHLAL 1141
Cdd:pfam04408   85 DEKARAKFArlDLEGDHLTL 104
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
185-222 1.44e-16

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: 74.27  E-value: 1.44e-16
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281427338  185 ISPFAVGKLSRYGFDKERCMNTLRSHDSDVGVSLEYLL 222
Cdd:cd14317     1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
563-988 2.80e-15

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 80.79  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  563 QDQILELLSKYQVLVVSGMTGCGKTTQIPQFIL----------DASLKGPPSHVSNIICTQPR----RISAISVAERVAQ 628
Cdd:PHA02653  169 QLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLwfnylfggfdNLDKIDPNFIERPIVLSLPRvalvRLHSITLLKSLGF 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  629 ERAERVGISVGY-QIRLESVKSA--ATRLLYCTTGVLLrrlegdTTLQNVTHVVVDEVHERTEESDFLLLVL-KDVMVLR 704
Cdd:PHA02653  249 DEIDGSPISLKYgSIPDELINTNpkPYGLVFSTHKLTL------NKLFDYGTVIIDEVHEHDQIGDIIIAVArKHIDKIR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  705 pdlKIILMSATL--NAELFSCYFQDCPVLHIPGRT-FPVdqyfledaiaKTRYVLEDGSPYQRSSkqlpgpdsargkkgn 781
Cdd:PHA02653  323 ---SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPI----------SEVYVKNKYNPKNKRA--------------- 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  782 sYNElldELEQQISSSLriqdskivKDSVPDQQlnvkelsvryngisKSVIktlssmdldkinldlieallewivngdhs 861
Cdd:PHA02653  375 -YIE---EEKKNIVTAL--------KKYTPPKG--------------SSGI----------------------------- 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  862 yppgavlVFLPGLAEIkTLYDQLQSnalfnnRRSKRCVIYPLHSSLSSDEQ--QSVFLKPPPgvtKIIISTNIAETSITI 939
Cdd:PHA02653  400 -------VFVASVSQC-EEYKKYLE------KRLPIYDFYIIHGKVPNIDEilEKVYSSKNP---SIIISTPYLESSVTI 462
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 281427338  940 DDVVYVIDSGKMREKRYDPGKSMesledtWVSRANAMQRKGRAGRVASG 988
Cdd:PHA02653  463 RNATHVYDTGRVYVPEPFGGKEM------FISKSMRTQRKGRVGRVSPG 505
HELICc smart00490
helicase superfamily c-terminal domain;
894-984 1.24e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.93  E-value: 1.24e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338    894 RSKRCVIYPLHSSLSSDEQQSVFLKPPPGVTKIIISTNIAETSITIDDVVYVIDSgkmrekrydpgksmesleDTWVSRA 973
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIY------------------DLPWSPA 69
                            90
                    ....*....|.
gi 281427338    974 NAMQRKGRAGR 984
Cdd:smart00490   70 SYIQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
846-985 2.62e-14

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 69.93  E-value: 2.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   846 DLIEALLEWIvngdHSYPPGAVLVFLPGlaeiktlYDQLQSNALFNNRRSKrcvIYPLHSSLSSDEQQSVFLKPPPGVTK 925
Cdd:pfam00271    1 EKLEALLELL----KKERGGKVLIFSQT-------KKTLEAELLLEKEGIK---VARLHGDLSQEEREEILEDFRKGKID 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   926 IIISTNIAETSITIDDVVYVIDsgkmrekrYDPGKSMESLedtwvsranaMQRKGRAGRV 985
Cdd:pfam00271   67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
582-715 5.72e-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: 67.43  E-value: 5.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  582 TGCGKTTQIPQFILDASL-KGPPSHVsniicTQPRRISAISVAERVAQERAE--RVGISVGYQiRLESVKSAATR---LL 655
Cdd:cd00046    10 TGSGKTLAALLAALLLLLkKGKKVLV-----LVPTKALALQTAERLRELFGPgiRVAVLVGGS-SAEEREKNKLGdadII 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281427338  656 YCTTGVLLRRLEGDT--TLQNVTHVVVDEVHERTEESDFLLLVLKDVMVL-RPDLKIILMSAT 715
Cdd:cd00046    84 IATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAgLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
563-720 1.08e-12

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: 67.27  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   563 QDQILELLSKYQVLVVSGMTGCGKTT--QIPqfILDAsLKGPPSHVSnIICTQPRRISAISVAERvAQERAERVGISV-- 638
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEA-LDKLDNGPQ-ALVLAPTRELAEQIYEE-LKKLGKGLGLKVas 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338   639 ---GYQIRLESVKSAATRLLYCTTGVLLRRLEGDTTLQNVTHVVVDEVHeRTEESDFLLLVLKDVMVLRPDLKIILMSAT 715
Cdd:pfam00270   79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKRQILLLSAT 157

                   ....*
gi 281427338   716 LNAEL 720
Cdd:pfam00270  158 LPRNL 162
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
576-734 2.29e-08

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: 54.96  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  576 LVVSGMTGCGKTTQIPQFILDASLKGPpshvSNIICTQPRRisAIsVAERVA--QERAERVGISVGYQIRLESV---KSA 650
Cdd:cd17921    20 VLVSAPTSSGKTLIAELAILRALATSG----GKAVYIAPTR--AL-VNQKEAdlRERFGPLGKNVGLLTGDPSVnklLLA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  651 ATRLLYCTT---GVLLRRLEGDTtLQNVTHVVVDEVH--ERTEESDFLLLVLKDVMVLRPDLKIILMSATL-NAELFSCY 724
Cdd:cd17921    93 EADILVATPeklDLLLRNGGERL-IQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARFVGLSATLpNAEDLAEW 171
                         170
                  ....*....|
gi 281427338  725 FQDCPVLHIP 734
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 ...
308-329 2.24e-05

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


Pssm-ID: 465626  Cd Length: 22  Bit Score: 42.19  E-value: 2.24e-05
                           10        20
                   ....*....|....*....|..
gi 281427338   308 NICKYYMKGeNCRFGSKCRFKH 329
Cdd:pfam18044    1 RLCRYFQKG-GCRYGDNCRFSH 21
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
310-329 2.55e-05

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: 42.02  E-value: 2.55e-05
                           10        20
                   ....*....|....*....|
gi 281427338   310 CKYYMKGeNCRFGSKCRFKH 329
Cdd:pfam18345    1 CKFFLKG-RCRYGDKCRFAH 19
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
307-329 3.28e-05

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 41.80  E-value: 3.28e-05
                           10        20
                   ....*....|....*....|...
gi 281427338   307 RNICKYYMKGENCRFGSKCRFKH 329
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAH 25
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
555-725 1.07e-04

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 44.51  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  555 QKLPAWQKqdqilELLSKYQV-----LVVSGMTGCGKTTqIPQFILdasLKgppshvsNIICtqpRRISAISVAERVA-- 627
Cdd:cd18026    15 KKLYDWQK-----ECLSLPGLlegrnLVYSLPTSGGKTL-VAEILM---LK-------RLLE---RRKKALFVLPYVSiv 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  628 QERA---ERVGISVGYQI--------RLESVKSAATRLLYCT---TGVLLRRLEGDTTLQNVTHVVVDEVHERTEESD-- 691
Cdd:cd18026    76 QEKVdalSPLFEELGFRVegyagnkgRSPPKRRKSLSVAVCTiekANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRga 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 281427338  692 FLLLVLKDVMVLRP-DLKIILMSAT----------LNAELFSCYF 725
Cdd:cd18026   156 LLELLLTKLLYAAQkNIQIVGMSATlpnleelaswLRAELYTTNF 200
ZnF_C3H1 smart00356
zinc finger;
309-329 1.39e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 39.92  E-value: 1.39e-04
                            10        20
                    ....*....|....*....|.
gi 281427338    309 ICKYYMKGeNCRFGSKCRFKH 329
Cdd:smart00356    6 LCKFFKRG-YCPRGDRCKFAH 25
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
345-417 4.44e-04

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: 41.16  E-value: 4.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281427338   345 NGNNNCLYELEVRFPKDnkYPYQAPLLAFySVNENLSMGCRLHITEYLYEKAlnIAQTSDPAVYTLVSCLEDE 417
Cdd:pfam05773   43 DSSHLPPLVLKFTLPED--YPDEPPKISL-SSPWNLSDEQVLSLLEELEELA--EENLGEVMIFELIEWLQEN 110
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
631-721 4.27e-03

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 41.46  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427338  631 AERVGISVGYqirlESVKSAAtRLLYCTTGVLLRRL-EGDTTLQNVTHVVVDEVH-----ERT---EESdfLLLvlkdvm 701
Cdd:COG4581    94 AENVGLLTGD----ASVNPDA-PIVVMTTEILRNMLyREGADLEDVGVVVMDEFHyladpDRGwvwEEP--IIH------ 160
                          90       100
                  ....*....|....*....|.
gi 281427338  702 vLRPDLKIILMSATL-NAELF 721
Cdd:COG4581   161 -LPARVQLVLLSATVgNAEEF 180
zf-CCCH_2 pfam14608
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ...
309-329 6.98e-03

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: 35.18  E-value: 6.98e-03
                           10        20
                   ....*....|....*....|.
gi 281427338   309 ICKYYMkgeNCRFGSKCRFKH 329
Cdd:pfam14608    1 PCRFGG---NCTFGPKCPFSH 18
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH