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Conserved domains on  [gi|2024491165|ref|XP_040524034|]
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putative ATP-dependent RNA helicase DHX57 isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
378-554 3.56e-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: 3.56e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17985    161 NAELFSDYFNSCPVIHI 177
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
378-1003 2.04e-115

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: 379.81  E-value: 2.04e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASL--QGSpnavanIICTQPRRISAISVAERVAKERTERV 455
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWgaGGR------IGMLEPRRLAARAAAERMAEELGEPV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIM-VQRPDLRIILMS 534
Cdd:COG1643     84 GETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  535 ATLNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvLEDSSPYRRktkqenkvtarhkrtafeeveedlrhagl 614
Cdd:COG1643    164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-RPLPADERD----------------------------- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  615 LEDtdtavkdsdpdqkltlkqllkrykGVNKTVLktmsvmdldkvnleliEALLEwivdgkhsyPPGAVLIFLPGLAEIK 694
Cdd:COG1643    204 LED------------------------AVADAVR----------------EALAE---------EPGDILVFLPGEREIR 234
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  695 MLYEQLQsnalfnNRHSKRCVVYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDP 774
Cdd:COG1643    235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  775 SKGMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNhQLIKQQLPEIQRVPLEQLCLRIKILEMFSAQSLhsvl 854
Cdd:COG1643    309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  855 sRLIEPPRTESLRASKLRLQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFvspw 934
Cdd:COG1643    384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR---- 458
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024491165  935 dkREEAnkkkldfavgNSDYLALLQAykgWRlstkegsqaSYNYCRENFLSGRVLQEIASLKRQFTELL 1003
Cdd:COG1643    459 --RGAA----------GSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
80-264 1.07e-47

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: 165.83  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   80 EECLEQRQEEAFALRSIYGEKFVERIQNRVWTFSLELEYLtnrlskskqkggcardtatqnskeickfylqggckfgskc 159
Cdd:cd23825      1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  160 rfrhefppnhplrsaknsvddshlrsnrdgPIYELEVRFPEENKYPLQAPLVAFYTTDENLPLACRLHIAEFLFGKALIA 239
Cdd:cd23825     41 ------------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALEL 90
                          170       180
                   ....*....|....*....|....*
gi 2024491165  240 AESNEPVVYALVTSLEDESEIGELL 264
Cdd:cd23825     91 AEDGEPVVFSLVSLLEDEEEILELL 115
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1047-1144 1.77e-22

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


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 92.32  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165 1047 ISAMLCAALYPNVVQvKKPEGKYQKTstgavkmqpkaeelkfvTKNDGYVHIHPSSVNYQTRHFESPYLVYHEKIKTSRV 1126
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTT-----------------LSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 2024491165 1127 FIRDCSMVSVYPLVLLGG 1144
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
19-56 6.45e-18

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: 78.12  E-value: 6.45e-18
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024491165   19 VSPFAVHKLSRYGFDSERCRTVLRSCNGNIGASLEHLL 56
Cdd:cd14317      1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
145-163 1.91e-06

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


:

Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 45.10  E-value: 1.91e-06
                           10
                   ....*....|....*....
gi 2024491165  145 CKFYLQGGCKFGSKCRFRH 163
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
 
Name Accession Description Interval E-value
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
378-554 3.56e-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: 3.56e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17985    161 NAELFSDYFNSCPVIHI 177
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
378-1003 2.04e-115

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 379.81  E-value: 2.04e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASL--QGSpnavanIICTQPRRISAISVAERVAKERTERV 455
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWgaGGR------IGMLEPRRLAARAAAERMAEELGEPV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIM-VQRPDLRIILMS 534
Cdd:COG1643     84 GETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  535 ATLNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvLEDSSPYRRktkqenkvtarhkrtafeeveedlrhagl 614
Cdd:COG1643    164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-RPLPADERD----------------------------- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  615 LEDtdtavkdsdpdqkltlkqllkrykGVNKTVLktmsvmdldkvnleliEALLEwivdgkhsyPPGAVLIFLPGLAEIK 694
Cdd:COG1643    204 LED------------------------AVADAVR----------------EALAE---------EPGDILVFLPGEREIR 234
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  695 MLYEQLQsnalfnNRHSKRCVVYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDP 774
Cdd:COG1643    235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  775 SKGMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNhQLIKQQLPEIQRVPLEQLCLRIKILEMFSAQSLhsvl 854
Cdd:COG1643    309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  855 sRLIEPPRTESLRASKLRLQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFvspw 934
Cdd:COG1643    384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR---- 458
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024491165  935 dkREEAnkkkldfavgNSDYLALLQAykgWRlstkegsqaSYNYCRENFLSGRVLQEIASLKRQFTELL 1003
Cdd:COG1643    459 --RGAA----------GSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
376-1132 6.41e-89

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: 314.40  E-value: 6.41e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  376 QKLPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqGSPNAVANiicTQPRRISAISVAERVAKERTERV 455
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGR-GSHGLIGH---TQPRRLAARTVAQRIAEELGTPL 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSA 535
Cdd:TIGR01967  140 GEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSA 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  536 TLNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvledsspyrrktkqenkvtarhkRTAFEEVEEDlrhagll 615
Cdd:TIGR01967  220 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-----------------------RPLVEEQEDD------- 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  616 edtdtavkDSDPDQKLtlkqllkrykgvnktvlktmsvmdLDKVNlELIEALlewivdgkhsypPGAVLIFLPGLAEIKM 695
Cdd:TIGR01967  260 --------DLDQLEAI------------------------LDAVD-ELFAEG------------PGDILIFLPGEREIRD 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  696 LYEQLqsnalfNNRHSKRCVVYPLHSSLSSEEQQSVFlRPPAGViKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPS 775
Cdd:TIGR01967  295 AAEIL------RKRNLRHTEILPLYARLSNKEQQRVF-QPHSGR-RIVLATNVAETSLTVPGIHYVIDTGTARISRYSYR 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  776 KGMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNHQLIKQQlPEIQRVPLEQLCLRIKILEMFSAQSLhsvls 855
Cdd:TIGR01967  367 TKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLALRLGDIAAF----- 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  856 RLIEPPRTESLRASKLRLQDLGALTADE---KLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFVS 932
Cdd:TIGR01967  441 PFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRER 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  933 PWDKREEANKKKLDFAVGNSDYLALLQAYKGWRLSTKEGSQASY-NYCRENFLSGRVLQEIASLKRQFTELLSDIGfvke 1011
Cdd:TIGR01967  521 PMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFrNACRKQYLNYLRVREWQDIYRQLTQVVKELG---- 596
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165 1012 glrardierkWSqggdgvldatgeeANSNAENFKLISAMLCAALYPNVVQvKKPEGKYQktstgavkmqpKAEELKFvtk 1091
Cdd:TIGR01967  597 ----------LK-------------LNEEPADYDAIHKALLSGLLSQIGM-KDEKHEYD-----------GARGRKF--- 638
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 2024491165 1092 ndgyvHIHPSSVNYQTRhfeSPYLVYHEKIKTSRVFIRDCS 1132
Cdd:TIGR01967  639 -----HIFPGSPLFKKP---PKWVMAAELVETSKLYARLVA 671
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
378-985 5.19e-76

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 275.79  E-value: 5.19e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqgspnAVANIIC-TQPRRISAISVAERVAKERTERVG 456
Cdd:PRK11131    73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGR-----GVKGLIGhTQPRRLAARTVANRIAEELETELG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  457 VTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:PRK11131   148 GCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  537 LNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvledsSPyrrktkqenkvtarhkrtafeeveedlrhagLLE 616
Cdd:PRK11131   228 IDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-----RP-------------------------------IVE 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  617 DTDtavkDSDPDQkltlkqllkrykgvnktvlktmsvmdldkvnlelIEALLEwIVDGKHSYPPGAVLIFLPGLAEIKML 696
Cdd:PRK11131   262 EAD----DTERDQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREIRDT 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  697 YEQLQSNALfnnRHSKrcvVYPLHSSLSSEEQQSVFlrPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSK 776
Cdd:PRK11131   303 ADALNKLNL---RHTE---ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRT 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  777 GMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNHqliKQQL--PEIQRVPLEQLclrikILEMfSAQSLHSVL 854
Cdd:PRK11131   375 KVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQM-TALGLGDIA 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  855 S-RLIEPPRTESLRASKLRLQDLGALTADE-----KLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKS 928
Cdd:PRK11131   446 AfPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQD 525
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024491165  929 PFVSPWDKREEANKKKLDFAVGNSDYLALLQAYKGWRLSTKEGSQASY-NYCRENFLS 985
Cdd:PRK11131   526 PRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLN 583
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
651-810 2.51e-66

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: 221.25  E-value: 2.51e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  651 MSVMDLDKVNLELIEALLEWIVdgkHSYPPGAVLIFLPGLAEIKMLYEQLQSNALFNNRHskRCVVYPLHSSLSSEEQQS 730
Cdd:cd18791     17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPDLG--KLLVLPLHSSLPPEEQQR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  731 VFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSKGMESLEDTFVSRANALQRKGRAGRVASGVCFHLF 810
Cdd:cd18791     92 VFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
80-264 1.07e-47

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: 165.83  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   80 EECLEQRQEEAFALRSIYGEKFVERIQNRVWTFSLELEYLtnrlskskqkggcardtatqnskeickfylqggckfgskc 159
Cdd:cd23825      1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  160 rfrhefppnhplrsaknsvddshlrsnrdgPIYELEVRFPEENKYPLQAPLVAFYTTDENLPLACRLHIAEFLFGKALIA 239
Cdd:cd23825     41 ------------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALEL 90
                          170       180
                   ....*....|....*....|....*
gi 2024491165  240 AESNEPVVYALVTSLEDESEIGELL 264
Cdd:cd23825     91 AEDGEPVVFSLVSLLEDEEEILELL 115
DEXDc smart00487
DEAD-like helicases superfamily;
384-564 4.65e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 4.65e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   384 RETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDAslqGSPNAVANIICTQPRRISAISVAERVAKERTERVGVTVGY-- 461
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEA---LKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyg 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   462 ----QIRLESVKSSATRLLYCTTGVLLRRLE-GDLTLQGITHVIVDEVHeRTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:smart00487   91 gdskREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
                           170       180       190
                    ....*....|....*....|....*....|..
gi 2024491165   537 L--NAELFSQYFHSCPIINIPGRT--FPVDQF 564
Cdd:smart00487  170 PpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
876-958 1.71e-23

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


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 95.41  E-value: 1.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   876 LGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFvsPWDKREEANKKKLDFAVGNSDYL 955
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 2024491165   956 ALL 958
Cdd:smart00847   80 TLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1047-1144 1.77e-22

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


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 92.32  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165 1047 ISAMLCAALYPNVVQvKKPEGKYQKTstgavkmqpkaeelkfvTKNDGYVHIHPSSVNYQTRHFESPYLVYHEKIKTSRV 1126
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTT-----------------LSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 2024491165 1127 FIRDCSMVSVYPLVLLGG 1144
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
873-957 3.65e-22

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


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 92.30  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  873 LQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFVSP-------------WDKREE 939
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarRRRRAA 84
                           90       100
                   ....*....|....*....|
gi 2024491165  940 ANKKKLDFAV--GNSDYLAL 957
Cdd:pfam04408   85 DEKARAKFARldLEGDHLTL 104
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
19-56 6.45e-18

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: 78.12  E-value: 6.45e-18
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024491165   19 VSPFAVHKLSRYGFDSERCRTVLRSCNGNIGASLEHLL 56
Cdd:cd14317      1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
384-541 1.17e-11

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 64.19  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  384 RETILDLLTSHQVLVVSGmTGCGKTT--QIPqfILDASLQGSPNAVANIICtqPRRISAISVAERvAKERTERVGVTV-- 459
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVas 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  460 ---GYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHeRTEESDF---LLLVLKDImvqRPDLRIILM 533
Cdd:pfam00270   79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLL 154

                   ....*...
gi 2024491165  534 SATLNAEL 541
Cdd:pfam00270  155 SATLPRNL 162
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
145-163 1.91e-06

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


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 45.10  E-value: 1.91e-06
                           10
                   ....*....|....*....
gi 2024491165  145 CKFYLQGGCKFGSKCRFRH 163
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
ZnF_C3H1 smart00356
zinc finger;
143-163 1.30e-05

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.00  E-value: 1.30e-05
                            10        20
                    ....*....|....*....|.
gi 2024491165   143 EICKFYLQGGCKFGSKCRFRH 163
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
23-56 2.21e-03

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 36.70  E-value: 2.21e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2024491165    23 AVHKLSRYGFDSERCRTVLRSCNGNIGASLEHLL 56
Cdd:smart00165    4 KIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
 
Name Accession Description Interval E-value
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
378-554 3.56e-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: 3.56e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17985    161 NAELFSDYFNSCPVIHI 177
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
378-1003 2.04e-115

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 379.81  E-value: 2.04e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASL--QGSpnavanIICTQPRRISAISVAERVAKERTERV 455
Cdd:COG1643     10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWgaGGR------IGMLEPRRLAARAAAERMAEELGEPV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIM-VQRPDLRIILMS 534
Cdd:COG1643     84 GETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALRPDLKLLVMS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  535 ATLNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvLEDSSPYRRktkqenkvtarhkrtafeeveedlrhagl 614
Cdd:COG1643    164 ATLDAERFARLLGDAPVIESSGRTYPVE----------VRY-RPLPADERD----------------------------- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  615 LEDtdtavkdsdpdqkltlkqllkrykGVNKTVLktmsvmdldkvnleliEALLEwivdgkhsyPPGAVLIFLPGLAEIK 694
Cdd:COG1643    204 LED------------------------AVADAVR----------------EALAE---------EPGDILVFLPGEREIR 234
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  695 MLYEQLQsnalfnNRHSKRCVVYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDP 774
Cdd:COG1643    235 RTAEALR------GRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  775 SKGMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNhQLIKQQLPEIQRVPLEQLCLRIKILEMFSAQSLhsvl 854
Cdd:COG1643    309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDL---- 383
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  855 sRLIEPPRTESLRASKLRLQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFvspw 934
Cdd:COG1643    384 -PFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR---- 458
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024491165  935 dkREEAnkkkldfavgNSDYLALLQAykgWRlstkegsqaSYNYCRENFLSGRVLQEIASLKRQFTELL 1003
Cdd:COG1643    459 --RGAA----------GSDLLARLNL---WR---------RLREQQREFLSYLRLREWRDLARQLRRLL 503
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
376-1132 6.41e-89

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: 314.40  E-value: 6.41e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  376 QKLPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqGSPNAVANiicTQPRRISAISVAERVAKERTERV 455
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGR-GSHGLIGH---TQPRRLAARTVAQRIAEELGTPL 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSA 535
Cdd:TIGR01967  140 GEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSA 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  536 TLNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvledsspyrrktkqenkvtarhkRTAFEEVEEDlrhagll 615
Cdd:TIGR01967  220 TIDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-----------------------RPLVEEQEDD------- 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  616 edtdtavkDSDPDQKLtlkqllkrykgvnktvlktmsvmdLDKVNlELIEALlewivdgkhsypPGAVLIFLPGLAEIKM 695
Cdd:TIGR01967  260 --------DLDQLEAI------------------------LDAVD-ELFAEG------------PGDILIFLPGEREIRD 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  696 LYEQLqsnalfNNRHSKRCVVYPLHSSLSSEEQQSVFlRPPAGViKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPS 775
Cdd:TIGR01967  295 AAEIL------RKRNLRHTEILPLYARLSNKEQQRVF-QPHSGR-RIVLATNVAETSLTVPGIHYVIDTGTARISRYSYR 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  776 KGMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNHQLIKQQlPEIQRVPLEQLCLRIKILEMFSAQSLhsvls 855
Cdd:TIGR01967  367 TKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLALRLGDIAAF----- 440
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  856 RLIEPPRTESLRASKLRLQDLGALTADE---KLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFVS 932
Cdd:TIGR01967  441 PFIEAPDPRAIRDGFRLLEELGALDDDEaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRER 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  933 PWDKREEANKKKLDFAVGNSDYLALLQAYKGWRLSTKEGSQASY-NYCRENFLSGRVLQEIASLKRQFTELLSDIGfvke 1011
Cdd:TIGR01967  521 PMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFrNACRKQYLNYLRVREWQDIYRQLTQVVKELG---- 596
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165 1012 glrardierkWSqggdgvldatgeeANSNAENFKLISAMLCAALYPNVVQvKKPEGKYQktstgavkmqpKAEELKFvtk 1091
Cdd:TIGR01967  597 ----------LK-------------LNEEPADYDAIHKALLSGLLSQIGM-KDEKHEYD-----------GARGRKF--- 638
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 2024491165 1092 ndgyvHIHPSSVNYQTRhfeSPYLVYHEKIKTSRVFIRDCS 1132
Cdd:TIGR01967  639 -----HIFPGSPLFKKP---PKWVMAAELVETSKLYARLVA 671
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
394-554 9.09e-89

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


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 283.20  E-value: 9.09e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  394 HQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAvaNIICTQPRRISAISVAERVAKERTERVGVTVGYQIRLESVKSSAT 473
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKG--RIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  474 RLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATLNAELFSQYFHSCPIIN 553
Cdd:cd17917     79 RIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIH 158

                   .
gi 2024491165  554 I 554
Cdd:cd17917    159 I 159
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
387-952 3.34e-76

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: 270.10  E-value: 3.34e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  387 ILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSpnavaNIICTQPRRISAISVAERVAKERTERVGVTVGYQIRLE 466
Cdd:TIGR01970   10 LRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGG-----KIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYRVRGE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  467 SVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQ-RPDLRIILMSATLNAELFSQY 545
Cdd:TIGR01970   85 NKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLKILAMSATLDGERLSSL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  546 FHSCPIINIPGRTFPVDqffledviamTRYVledssPYRRKTKQENKVtarhKRTafeeVEEDLRHAglledtdtavkds 625
Cdd:TIGR01970  165 LPDAPVVESEGRSFPVE----------IRYL-----PLRGDQRLEDAV----SRA----VEHALASE------------- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  626 dpdqkltlkqllkrykgvnktvlktmsvmdldkvnlelieallewivdgkhsypPGAVLIFLPGLAEIKMLYEQLQSnal 705
Cdd:TIGR01970  209 ------------------------------------------------------TGSILVFLPGQAEIRRVQEQLAE--- 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  706 fnnRHSKRCVVYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSKGMESLEDTF 785
Cdd:TIGR01970  232 ---RLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVR 308
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  786 VSRANALQRKGRAGRVASGVCFHLFSSHHYNhQLIKQQLPEIQRVPLEQLCLRikiLEMFSAQSLhSVLSRLIEPPRTES 865
Cdd:TIGR01970  309 ISQASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALE---LAQWGAKDP-SDLRWLDAPPSVAL 383
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  866 LRASKLrLQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAA-----------------SLAFKS 928
Cdd:TIGR01970  384 AAARQL-LQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAAlleerglprqggadlmnRLHRLQ 462
                          570       580
                   ....*....|....*....|....
gi 2024491165  929 PFVSPWDKREEANKKKLDFAVGNS 952
Cdd:TIGR01970  463 QGRQGRGQRAQQLAKKLRRRLRFS 486
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
378-985 5.19e-76

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 275.79  E-value: 5.19e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqgspnAVANIIC-TQPRRISAISVAERVAKERTERVG 456
Cdd:PRK11131    73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGR-----GVKGLIGhTQPRRLAARTVANRIAEELETELG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  457 VTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:PRK11131   148 GCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSAT 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  537 LNAELFSQYFHSCPIINIPGRTFPVDqffledviamTRYvledsSPyrrktkqenkvtarhkrtafeeveedlrhagLLE 616
Cdd:PRK11131   228 IDPERFSRHFNNAPIIEVSGRTYPVE----------VRY-----RP-------------------------------IVE 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  617 DTDtavkDSDPDQkltlkqllkrykgvnktvlktmsvmdldkvnlelIEALLEwIVDGKHSYPPGAVLIFLPGLAEIKML 696
Cdd:PRK11131   262 EAD----DTERDQ----------------------------------LQAIFD-AVDELGREGPGDILIFMSGEREIRDT 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  697 YEQLQSNALfnnRHSKrcvVYPLHSSLSSEEQQSVFlrPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSK 776
Cdd:PRK11131   303 ADALNKLNL---RHTE---ILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRT 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  777 GMESLEDTFVSRANALQRKGRAGRVASGVCFHLFSSHHYNHqliKQQL--PEIQRVPLEQLclrikILEMfSAQSLHSVL 854
Cdd:PRK11131   375 KVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLS---RPEFtdPEILRTNLASV-----ILQM-TALGLGDIA 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  855 S-RLIEPPRTESLRASKLRLQDLGALTADE-----KLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKS 928
Cdd:PRK11131   446 AfPFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQD 525
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024491165  929 PFVSPWDKREEANKKKLDFAVGNSDYLALLQAYKGWRLSTKEGSQASY-NYCRENFLS 985
Cdd:PRK11131   526 PRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQFrRLCRTDYLN 583
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
368-554 2.53e-68

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 229.34  E-value: 2.53e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  368 FQSMLHERQKLPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERV 447
Cdd:cd17972     49 LQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAVSVAERV 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  448 AKERTERVGVTVGYQIRLESV-KSSATRLLYCTTGVLLRRLEGDltLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRP 526
Cdd:cd17972    129 AFERGEEVGKSCGYSVRFESVlPRPHASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQAYP 206
                          170       180
                   ....*....|....*....|....*...
gi 2024491165  527 DLRIILMSATLNAELFSQYFHSCPIINI 554
Cdd:cd17972    207 DLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
378-554 4.03e-68

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: 226.65  E-value: 4.03e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 --TVGYQIRLESVKS-SATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMS 534
Cdd:cd17981     81 gnSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                          170       180
                   ....*....|....*....|
gi 2024491165  535 ATLNAELFSQYFHSCPIINI 554
Cdd:cd17981    161 ATLNAEKFSDYFNNCPMIHI 180
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
651-810 2.51e-66

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: 221.25  E-value: 2.51e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  651 MSVMDLDKVNLELIEALLEWIVdgkHSYPPGAVLIFLPGLAEIKMLYEQLQSNALFNNRHskRCVVYPLHSSLSSEEQQS 730
Cdd:cd18791     17 ISSEKEDPDYVDAAVRLILQIH---RTEEPGDILVFLPGQEEIERLCELLREELLSPDLG--KLLVLPLHSSLPPEEQQR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  731 VFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSKGMESLEDTFVSRANALQRKGRAGRVASGVCFHLF 810
Cdd:cd18791     92 VFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
378-554 1.91e-65

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: 219.02  E-value: 1.91e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFIL-DASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVG 456
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLeDLLLNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  457 -----VTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRII 531
Cdd:cd17975     81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                          170       180
                   ....*....|....*....|...
gi 2024491165  532 LMSATLNAELFSQYFHSCPIINI 554
Cdd:cd17975    161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
378-554 6.74e-65

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: 217.39  E-value: 6.74e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQ-GSPnavANIICTQPRRISAISVAERVAKERTERVG 456
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYAnGIP---CRIFCTQPRRLAAIAVAERVAAERGEKIG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  457 VTVGYQIRLESVKSSATRLLYCTTGVLLRRL-EGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSA 535
Cdd:cd17987     78 QTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSA 157
                          170
                   ....*....|....*....
gi 2024491165  536 TLNAELFSQYFHSCPIINI 554
Cdd:cd17987    158 ALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
378-554 8.85e-64

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: 214.27  E-value: 8.85e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:cd17976     81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
                          170
                   ....*....|....*...
gi 2024491165  537 LNAELFSQYFHSCPIINI 554
Cdd:cd17976    161 GDNQRLSRYFGGCPVVRV 178
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
390-925 3.62e-61

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 225.57  E-value: 3.62e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  390 LLTSHQVLVvSGMTGCGKTTQIP-QFILDASLQGspnavaNIICTQPRRISAISVAERVAKERTERVGVTVGYQIRLESV 468
Cdd:PRK11664    17 LKTAPQVLL-KAPTGAGKSTWLPlQLLQHGGING------KIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYRMRAESK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  469 KSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDimVQ---RPDLRIILMSATLNAELFSQY 545
Cdd:PRK11664    90 VGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLD--VQqglRDDLKLLIMSATLDNDRLQQL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  546 FHSCPIINIPGRTFPVDqffledviamTRYvledsspyrrktkqenKVTARHKRtaFEEveedlrhaglledtdtavkds 625
Cdd:PRK11664   168 LPDAPVIVSEGRSFPVE----------RRY----------------QPLPAHQR--FDE--------------------- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  626 dpdqkltlkqllkrykGVNKTVLKTMsvmdldkvNLElieallewivdgkhsypPGAVLIFLPGLAEIKMLYEQLQsnal 705
Cdd:PRK11664   199 ----------------AVARATAELL--------RQE-----------------SGSLLLFLPGVGEIQRVQEQLA---- 233
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  706 fnNRHSKRCVVYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSGKMKEKRYDPSKGMESLEDTF 785
Cdd:PRK11664   234 --SRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQR 311
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  786 VSRANALQRKGRAGRVASGVCFHLFSSHHYNhQLIKQQLPEIQRVPLEQLCLRikiLEMFSAQSLHSvLSRLIEPPRTeS 865
Cdd:PRK11664   312 ISQASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLE---LLQWGCHDPAQ-LSWLDQPPAA-A 385
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  866 LRASKLRLQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRclDPALTIAASLA 925
Cdd:PRK11664   386 LAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLA 443
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
367-554 4.33e-60

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 204.19  E-value: 4.33e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  367 RFQSMLHERQKLPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVanIICTQPRRISAISVAER 446
Cdd:cd17973      2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKL--VACTQPRRVAAMSVAQR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  447 VAKERTERVGVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRP 526
Cdd:cd17973     80 VAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRP 159
                          170       180
                   ....*....|....*....|....*...
gi 2024491165  527 DLRIILMSATLNAELFSQYFHSCPIINI 554
Cdd:cd17973    160 DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
378-554 2.10e-58

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 198.44  E-value: 2.10e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQgspnavaNIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFR-------HIACTQPRRIACISLAKRVAFESLNQYGS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17979     74 KVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATI 153
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17979    154 NIELFSGYFEGAPVVQV 170
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
378-561 2.20e-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: 184.63  E-value: 2.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAvaNIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYC--NIVVTQPRRIAAISIARRVSQEREWTLGS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIM-VQRPDLRIILMSAT 536
Cdd:cd17988     79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLrTNSRHVKIILMSAT 158
                          170       180
                   ....*....|....*....|....*
gi 2024491165  537 LNAELFSQYFHScpiINIPGRTFPV 561
Cdd:cd17988    159 ISCKEFADYFTT---PNNPAYVFEV 180
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
378-554 6.56e-53

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: 183.32  E-value: 6.56e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSpnavANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARG----GMIGITQPRRVAAVSVAKRVAEEMGVELGQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQR-----PDLRIIL 532
Cdd:cd17978     77 LVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVII 156
                          170       180
                   ....*....|....*....|..
gi 2024491165  533 MSATLNAELFSQYFHSCPIINI 554
Cdd:cd17978    157 MSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
374-555 2.48e-51

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


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 178.83  E-value: 2.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  374 ERQKLPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSpnavANIICTQPRRISAISVAERVAKERTE 453
Cdd:cd17971      2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSR----GKIGCTQPRRVAAMSVAKRVAEEFGC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  454 RVGVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILM 533
Cdd:cd17971     78 CLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVT 157
                          170       180
                   ....*....|....*....|..
gi 2024491165  534 SATLNAELFSQYFHSCPIINIP 555
Cdd:cd17971    158 SATLDAVKFSQYFYEAPIFTIP 179
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
378-554 2.57e-51

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 178.47  E-value: 2.57e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDAslqGSPNAVANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEA---GYTKGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGN 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17974     78 EVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATM 157
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17974    158 DAEKFSAFFDDAPIFRI 174
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
378-548 2.33e-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: 173.42  E-value: 2.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVAniiCTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVG---CTQPRRVAAVTVAGRVAEEMGAVLGH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSS-ATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:cd17980     78 EVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASAT 157
                          170
                   ....*....|..
gi 2024491165  537 LNAELFSQYFHS 548
Cdd:cd17980    158 LDAEKFRDFFNQ 169
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
80-264 1.07e-47

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: 165.83  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   80 EECLEQRQEEAFALRSIYGEKFVERIQNRVWTFSLELEYLtnrlskskqkggcardtatqnskeickfylqggckfgskc 159
Cdd:cd23825      1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYL---------------------------------------- 40
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  160 rfrhefppnhplrsaknsvddshlrsnrdgPIYELEVRFPEENKYPLQAPLVAFYTTDENLPLACRLHIAEFLFGKALIA 239
Cdd:cd23825     41 ------------------------------PWFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITERLMEEALEL 90
                          170       180
                   ....*....|....*....|....*
gi 2024491165  240 AESNEPVVYALVTSLEDESEIGELL 264
Cdd:cd23825     91 AEDGEPVVFSLVSLLEDEEEILELL 115
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
378-554 2.66e-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: 158.39  E-value: 2.66e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqGSPNAVANiicTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGR-GIRGLIGH---TQPRRLAARSVAERIAEELKTELGG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17989     77 AVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATI 156
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17989    157 DAERFSRHFNNAPIIEV 173
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
378-554 1.21e-43

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: 156.47  E-value: 1.21e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSpnavANIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDY----GMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17983     77 EVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATM 156
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
Cdd:cd17983    157 DADKFADFFGNVPIFTI 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
387-552 3.74e-43

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


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 155.18  E-value: 3.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  387 ILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqgspNAVANIICTQPRRISAISVAERVAKERTERVGVTVGYQIRLE 466
Cdd:cd17990     10 LRAALDAGGQVVLEAPPGAGKTTRVPLALLAELW----IAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGYRVRGE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  467 SVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIM-VQRPDLRIILMSATLNAELFSQY 545
Cdd:cd17990     86 SRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSATLDGDGLAAL 165

                   ....*..
gi 2024491165  546 FHSCPII 552
Cdd:cd17990    166 LPEAPVV 172
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
378-544 4.66e-40

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 146.73  E-value: 4.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqGSPNAVAN--IICTQPRRISAISVAERVAKErTERV 455
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGF-GSPESDNPgmIGITQPRRVAAVSMAKRVAEE-LNVF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  456 GVTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPD-------- 527
Cdd:cd17982     79 GKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtv 158
                          170
                   ....*....|....*....
gi 2024491165  528 --LRIILMSATLNAELFSQ 544
Cdd:cd17982    159 kpLKLVIMSATLRVEDFTE 177
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
378-554 3.91e-37

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 138.06  E-value: 3.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLqgSPNAVanIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGF--SQHGM--IGVTQPRRVAAISVAQRVAEEMKCTLGS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRP-----DLRIIL 532
Cdd:cd17984     77 KVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVV 156
                          170       180
                   ....*....|....*....|..
gi 2024491165  533 MSATLNAELFSQYFHSCPIINI 554
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 ...
378-554 2.85e-34

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 129.56  E-value: 2.85e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVAnIICTQPRRISAISVAERVAKERTERVGV 457
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGV-VVCTQVHKQTAVWLALRVADEMDVNIGH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  458 TVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSATL 537
Cdd:cd17977     80 EVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPH 159
                          170
                   ....*....|....*..
gi 2024491165  538 NAELFSQYFHSCPIINI 554
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 ...
378-554 8.21e-27

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: 108.45  E-value: 8.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  378 LPAWQERETILDLLTSHQ-VLVVSGMTGCGKTTQIPQFILDASLqGSPNAVANIICTQPRRISAISVAERVAKERTERVG 456
Cdd:cd17986      1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFAL-SRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  457 VTVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHERTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:cd17986     80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSP 159
                          170
                   ....*....|....*...
gi 2024491165  537 LNAELFSQYFHSCPIINI 554
Cdd:cd17986    160 ALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
384-564 4.65e-24

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 101.03  E-value: 4.65e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   384 RETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDAslqGSPNAVANIICTQPRRISAISVAERVAKERTERVGVTVGY-- 461
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEA---LKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLyg 90
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   462 ----QIRLESVKSSATRLLYCTTGVLLRRLE-GDLTLQGITHVIVDEVHeRTEESDFLLLVLKDIMVQRPDLRIILMSAT 536
Cdd:smart00487   91 gdskREQLRKLESGKTDILVTTPGRLLDLLEnDKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
                           170       180       190
                    ....*....|....*....|....*....|..
gi 2024491165   537 L--NAELFSQYFHSCPIINIPGRT--FPVDQF 564
Cdd:smart00487  170 PpeEIENLLELFLNDPVFIDVGFTplEPIEQF 201
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
876-958 1.71e-23

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


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 95.41  E-value: 1.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   876 LGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFvsPWDKREEANKKKLDFAVGNSDYL 955
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHL 79

                    ...
gi 2024491165   956 ALL 958
Cdd:smart00847   80 TLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1047-1144 1.77e-22

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


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 92.32  E-value: 1.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165 1047 ISAMLCAALYPNVVQvKKPEGKYQKTstgavkmqpkaeelkfvTKNDGYVHIHPSSVNYQTRHFESPYLVYHEKIKTSRV 1126
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTT-----------------LSDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*...
gi 2024491165 1127 FIRDCSMVSVYPLVLLGG 1144
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAP 80
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
873-957 3.65e-22

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


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 92.30  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  873 LQDLGALTADEKLTPLGYHLASLPVDVRIGKLMLFGTIFRCLDPALTIAASLAFKSPFVSP-------------WDKREE 939
Cdd:pfam04408    5 LYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarRRRRAA 84
                           90       100
                   ....*....|....*....|
gi 2024491165  940 ANKKKLDFAV--GNSDYLAL 957
Cdd:pfam04408   85 DEKARAKFARldLEGDHLTL 104
UBA_DHX57 cd14317
UBA domain found in putative ATP-dependent RNA helicase DHX57 and similar proteins; DHX57, ...
19-56 6.45e-18

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: 78.12  E-value: 6.45e-18
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024491165   19 VSPFAVHKLSRYGFDSERCRTVLRSCNGNIGASLEHLL 56
Cdd:cd14317      1 VSPFAVGKLSRYGFDKERCIQALRSNDGDIGAALEHLL 38
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
387-804 1.62e-13

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 75.01  E-value: 1.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  387 ILDLLTSHQVLVVSGMTGCGKTTQIPQFI------------LDASlqgSPNAVAN-IICTQPR----RISAISVAERVAK 449
Cdd:PHA02653   172 IFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnylfggfdnLDKI---DPNFIERpIVLSLPRvalvRLHSITLLKSLGF 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  450 ERTERVGVTVGY---QIRLESVKSSATRLLYCTTgvllrrlegDLTLQGITH---VIVDEVHERTEESDFLLLVL-KDIM 522
Cdd:PHA02653   249 DEIDGSPISLKYgsiPDELINTNPKPYGLVFSTH---------KLTLNKLFDygtVIIDEVHEHDQIGDIIIAVArKHID 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  523 VQRpdlRIILMSATL--NAELFSQYFHSCPIINIPGRT-FPVDQFfledviamtrYVLEDSSPYRRktkqenkvtarhkr 599
Cdd:PHA02653   320 KIR---SLFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEV----------YVKNKYNPKNK-------------- 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  600 taFEEVEEDLRhaglleDTDTAVKDSDPDQKltlkqllkrYKGVnkTVLKTMSVMDLDKVNLE-LIEALLEWIVDGKhsy 678
Cdd:PHA02653   373 --RAYIEEEKK------NIVTALKKYTPPKG---------SSGI--VFVASVSQCEEYKKYLEkRLPIYDFYIIHGK--- 430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  679 ppgavlifLPGLAEIkmlyeqlqSNALFNNRHskrcvvyplhsslsseeqqsvflrppagvIKIIISTNIAETSVTIDDV 758
Cdd:PHA02653   431 --------VPNIDEI--------LEKVYSSKN-----------------------------PSIIISTPYLESSVTIRNA 465
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2024491165  759 VYVIDSGKMKEKRydPSKGMEsledTFVSRANALQRKGRAGRVASG 804
Cdd:PHA02653   466 THVYDTGRVYVPE--PFGGKE----MFISKSMRTQRKGRVGRVSPG 505
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
403-536 2.35e-13

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 68.58  E-value: 2.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  403 TGCGKTTQIPQFILDASLQGSPNAVanIICtqPRRISAISVAERVAKERTE--RVGVTVGY---QIRLESVKSSAtRLLY 477
Cdd:cd00046     10 TGSGKTLAALLAALLLLLKKGKKVL--VLV--PTKALALQTAERLRELFGPgiRVAVLVGGssaEEREKNKLGDA-DIII 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024491165  478 CTTGVLLRRLEGD--LTLQGITHVIVDEVHERTEESDFLLLV-LKDIMVQRPDLRIILMSAT 536
Cdd:cd00046     85 ATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILdLAVRKAGLKNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
384-541 1.17e-11

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 64.19  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  384 RETILDLLTSHQVLVVSGmTGCGKTT--QIPqfILDASLQGSPNAVANIICtqPRRISAISVAERvAKERTERVGVTV-- 459
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAP-TGSGKTLafLLP--ALEALDKLDNGPQALVLA--PTRELAEQIYEE-LKKLGKGLGLKVas 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  460 ---GYQIRLESVKSSATRLLYCTTGVLLRRLEGDLTLQGITHVIVDEVHeRTEESDF---LLLVLKDImvqRPDLRIILM 533
Cdd:pfam00270   79 llgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLL 154

                   ....*...
gi 2024491165  534 SATLNAEL 541
Cdd:pfam00270  155 SATLPRNL 162
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
662-801 3.88e-09

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: 55.29  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  662 ELIEALLEWIvdgkHSYPPGAVLIFLPGlaeikmlYEQLQSNALFNNRHSKrcvVYPLHSSLSSEEQQSVFLRPPAGVIK 741
Cdd:pfam00271    1 EKLEALLELL----KKERGGKVLIFSQT-------KKTLEAELLLEKEGIK---VARLHGDLSQEEREEILEDFRKGKID 66
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  742 IIISTNIAETSVTIDDVVYVIDsgkmkekrYDPSKGMESLedtfvsranaLQRKGRAGRV 801
Cdd:pfam00271   67 VLVATDVAERGLDLPDVDLVIN--------YDLPWNPASY----------IQRIGRAGRA 108
HELICc smart00490
helicase superfamily c-terminal domain;
716-800 8.99e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 53.37  E-value: 8.99e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165   716 VYPLHSSLSSEEQQSVFLRPPAGVIKIIISTNIAETSVTIDDVVYVIDSgkmkekrydpskgmesleDTFVSRANALQRK 795
Cdd:smart00490   14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIY------------------DLPWSPASYIQRI 75

                    ....*
gi 2024491165   796 GRAGR 800
Cdd:smart00490   76 GRAGR 80
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
381-555 3.04e-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: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  381 WQeRETILDLLTSHQVLVVSGMTGCGKTTQIPQFILDASLQGSPNAVAniicTQPRRisAIsVAERVA--KERTERVGVT 458
Cdd:cd17921      5 IQ-REALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVY----IAPTR--AL-VNQKEAdlRERFGPLGKN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024491165  459 VGYQIRLESV---KSSATRLLYCTT---GVLLRRLEGDLtLQGITHVIVDEVH--ERTEESDFLLLVLKDIMVQRPDLRI 530
Cdd:cd17921     77 VGLLTGDPSVnklLLAEADILVATPeklDLLLRNGGERL-IQDVRLVVVDEAHliGDGERGVVLELLLSRLLRINKNARF 155
                          170       180
                   ....*....|....*....|....*.
gi 2024491165  531 ILMSATL-NAELFSQYFHSCPIINIP 555
Cdd:cd17921    156 VGLSATLpNAEDLAEWLGVEDLIRFD 181
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
145-163 1.91e-06

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


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 45.10  E-value: 1.91e-06
                           10
                   ....*....|....*....
gi 2024491165  145 CKFYLQGGCKFGSKCRFRH 163
Cdd:pfam18345    1 CKFFLKGRCRYGDKCRFAH 19
zf-CCCH_4 pfam18044
CCCH-type zinc finger; This short zinc binding domain has the pattern of three cysteines and ...
144-163 2.28e-06

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


Pssm-ID: 465626  Cd Length: 22  Bit Score: 44.89  E-value: 2.28e-06
                           10        20
                   ....*....|....*....|
gi 2024491165  144 ICKFYLQGGCKFGSKCRFRH 163
Cdd:pfam18044    2 LCRYFQKGGCRYGDNCRFSH 21
ZnF_C3H1 smart00356
zinc finger;
143-163 1.30e-05

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 43.00  E-value: 1.30e-05
                            10        20
                    ....*....|....*....|.
gi 2024491165   143 EICKFYLQGGCKFGSKCRFRH 163
Cdd:smart00356    5 ELCKFFKRGYCPRGDRCKFAH 25
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
142-163 1.69e-04

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.87  E-value: 1.69e-04
                           10        20
                   ....*....|....*....|...
gi 2024491165  142 KEICKFYLQGG-CKFGSKCRFRH 163
Cdd:pfam00642    3 TELCRFFLRTGyCKYGDRCKFAH 25
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
23-56 2.21e-03

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 36.70  E-value: 2.21e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2024491165    23 AVHKLSRYGFDSERCRTVLRSCNGNIGASLEHLL 56
Cdd:smart00165    4 KIDQLLEMGFSREEALKALRAANGNVERAAEYLL 37
zf-CCCH_2 pfam14608
RNA-binding, Nab2-type zinc finger; This is an unusual zinc-finger family, and is represented ...
144-163 2.34e-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: 36.34  E-value: 2.34e-03
                           10        20
                   ....*....|....*....|
gi 2024491165  144 ICKFYlqGGCKFGSKCRFRH 163
Cdd:pfam14608    1 PCRFG--GNCTFGPKCPFSH 18
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
739-800 3.92e-03

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 37.30  E-value: 3.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024491165  739 VIKIIISTNIAETSVTIDDVVYVIdsgkmkekRYDPSKgmesledtfvSRANALQRKGRAGR 800
Cdd:cd18785     22 SLEILVATNVLGEGIDVPSLDTVI--------FFDPPS----------SAASYIQRVGRAGR 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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