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Conserved domains on  [gi|1958649627|ref|XP_038946776|]
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probable ATP-dependent RNA helicase DHX34 isoform X1 [Rattus norvegicus]

Protein Classification

ATP-dependent RNA helicase( domain architecture ID 13388279)

DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA, similar to DEAH box protein 34 (DHX34) that is required for nonsense-mediated decay (NMD) degradation of mRNA transcripts containing premature stop codons

CATH:  3.40.50.300
EC:  3.6.4.13
Gene Ontology:  GO:0005524|GO:0003724|GO:0003676|GO:0016887|GO:0003723
PubMed:  34680866|19747077|22922795|20206133|21779027|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
161-627 1.06e-161

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: 500.76  E-value: 1.06e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  161 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 237
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  238 GYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 316
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  317 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQsasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 391
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  392 ISTVLDAAQAyaTLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 471
Cdd:COG1643    233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  472 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 551
Cdd:COG1643    311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649627  552 AASVETAILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 627
Cdd:COG1643    391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 798-909 4.52e-08

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: 51.48  E-value: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  798 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgpeasgregsqdgkdqMSCKhqLL 877
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958649627  878 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 909
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
161-627 1.06e-161

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 500.76  E-value: 1.06e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  161 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 237
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  238 GYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 316
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  317 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQsasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 391
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  392 ISTVLDAAQAyaTLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 471
Cdd:COG1643    233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  472 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 551
Cdd:COG1643    311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649627  552 AASVETAILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 627
Cdd:COG1643    391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 125-697 4.77e-125

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: 414.94  E-value: 4.77e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  125 GLPPERVSEFRRALLHYLDFQQKQAFGRLAKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQ 198
Cdd:TIGR01967   22 KLRKDHDQDRAIAALAKFRERIDAACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  199 YLLAAGF-SH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQ 275
Cdd:TIGR01967  102 ICLELGRgSHglIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  276 VLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQSASKS 355
Cdd:TIGR01967  182 TIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPLVEEQEDDDL 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  356 EKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEIStvlDAAQAYATLTQRWV-VLPLHSALSVADQDKVFDvaPAGV 434
Cdd:TIGR01967  262 DQLEA-----ILDAVD-ELFAEGPGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQQRVFQ--PHSG 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  435 RKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFA 514
Cdd:TIGR01967  331 RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRP 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  515 PYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAASVETAILYLQDQGALDSSEA---LTPIGSLLAQLPVDVVIG 591
Cdd:TIGR01967  411 EFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLA 490

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  592 KMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSGNS-RKWCRR 670
Cdd:TIGR01967  491 RMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQfRNACRK 570

                          570       580
                   ....*....|....*....|....*..
gi 1958649627  671 RGVEEHRLYEMANLRRQFKELLEDHGL 697
Cdd:TIGR01967  571 QYLNYLRVREWQDIYRQLTQVVKELGL 597
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 120-669 4.32e-122

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 407.14  E-value: 4.32e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  120 HGPGKGLPPERvsefRRALLHYLDFQQKQAFGRLAKLQRERAA------LPIAQYGNRILQTLKEHQVVVVAGDTGCGKS 193
Cdd:PRK11131    28 HGAKKIKNPDA----QQAIFQEIAKEIAQAAQRVLLREAARPEitypenLPVSQKKQDILEAIRDHQVVIVAGETGSGKT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  194 TQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPR 270
Cdd:PRK11131   104 TQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRL 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  271 LPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQ 350
Cdd:PRK11131   184 LMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEA 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  351 SASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEIStvlDAAQAYATLTQRWV-VLPLHSALSVADQDKVFDv 429
Cdd:PRK11131   264 DDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIR---DTADALNKLNLRHTeILPLYARLSNSEQNRVFQ- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  430 aPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESD 509
Cdd:PRK11131   334 -SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDD 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  510 YDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAASVETAILYLQDQGALDSSEA-----LTPIGSLLAQL 584
Cdd:PRK11131   413 FLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQL 492

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  585 PVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSGNS 664
Cdd:PRK11131   493 PVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQ 572


                   ....*.
gi 1958649627  665 -RKWCR 669
Cdd:PRK11131   573 fRRLCR 578
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 163-332 3.98e-107

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: 332.49  E-value: 3.98e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 242
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  243 FESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSS 322
Cdd:cd17979     81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160

                          170
                   ....*....|
gi 1958649627  323 YFSHAPVVQV 332
Cdd:cd17979    161 YFEGAPVVQV 170
DEXDc smart00487
DEAD-like helicases superfamily;
176-341 1.49e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 93.71  E-value: 1.49e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   176 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 244
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   245 STRSAATKIVFLTVGLLLRQIQCEP-RLPQYQVLIVDEVHER--HLHNDFLLGVLQRLlpqRPDLKVILMSATI--NISL 319
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176

                           170       180
                    ....*....|....*....|..
gi 1958649627   320 FSSYFSHAPVVQVPGRLFPITV 341
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 558-646 1.87e-19

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: 84.60  E-value: 1.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  558 AILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDC-------- 629
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 1958649627  630 -------ATARRPLESDQGDPFTL 646
Cdd:pfam04408   81 rraadekARAKFARLDLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 798-909 4.52e-08

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: 51.48  E-value: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  798 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgpeasgregsqdgkdqMSCKhqLL 877
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958649627  878 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 909
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
161-627 1.06e-161

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 500.76  E-value: 1.06e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  161 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 237
Cdd:COG1643      8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  238 GYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 316
Cdd:COG1643     88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  317 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQsasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 391
Cdd:COG1643    168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  392 ISTVLDAAQAyaTLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 471
Cdd:COG1643    233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  472 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 551
Cdd:COG1643    311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958649627  552 AASVETAILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 627
Cdd:COG1643    391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 125-697 4.77e-125

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: 414.94  E-value: 4.77e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  125 GLPPERVSEFRRALLHYLDFQQKQAFGRLAKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQ 198
Cdd:TIGR01967   22 KLRKDHDQDRAIAALAKFRERIDAACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  199 YLLAAGF-SH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQ 275
Cdd:TIGR01967  102 ICLELGRgSHglIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  276 VLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQSASKS 355
Cdd:TIGR01967  182 TIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPLVEEQEDDDL 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  356 EKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEIStvlDAAQAYATLTQRWV-VLPLHSALSVADQDKVFDvaPAGV 434
Cdd:TIGR01967  262 DQLEA-----ILDAVD-ELFAEGPGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQQRVFQ--PHSG 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  435 RKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFA 514
Cdd:TIGR01967  331 RRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRP 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  515 PYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAASVETAILYLQDQGALDSSEA---LTPIGSLLAQLPVDVVIG 591
Cdd:TIGR01967  411 EFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLA 490

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  592 KMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSGNS-RKWCRR 670
Cdd:TIGR01967  491 RMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQfRNACRK 570

                          570       580
                   ....*....|....*....|....*..
gi 1958649627  671 RGVEEHRLYEMANLRRQFKELLEDHGL 697
Cdd:TIGR01967  571 QYLNYLRVREWQDIYRQLTQVVKELGL 597
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 120-669 4.32e-122

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 407.14  E-value: 4.32e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  120 HGPGKGLPPERvsefRRALLHYLDFQQKQAFGRLAKLQRERAA------LPIAQYGNRILQTLKEHQVVVVAGDTGCGKS 193
Cdd:PRK11131    28 HGAKKIKNPDA----QQAIFQEIAKEIAQAAQRVLLREAARPEitypenLPVSQKKQDILEAIRDHQVVIVAGETGSGKT 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  194 TQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPR 270
Cdd:PRK11131   104 TQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRL 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  271 LPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQ 350
Cdd:PRK11131   184 LMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEA 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  351 SASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEIStvlDAAQAYATLTQRWV-VLPLHSALSVADQDKVFDv 429
Cdd:PRK11131   264 DDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIR---DTADALNKLNLRHTeILPLYARLSNSEQNRVFQ- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  430 aPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESD 509
Cdd:PRK11131   334 -SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDD 412

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  510 YDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAASVETAILYLQDQGALDSSEA-----LTPIGSLLAQL 584
Cdd:PRK11131   413 FLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQL 492

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  585 PVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSGNS 664
Cdd:PRK11131   493 PVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSSNQ 572


                   ....*.
gi 1958649627  665 -RKWCR 669
Cdd:PRK11131   573 fRRLCR 578
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 163-332 3.98e-107

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: 332.49  E-value: 3.98e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 242
Cdd:cd17979      1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  243 FESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSS 322
Cdd:cd17979     81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160

                          170
                   ....*....|
gi 1958649627  323 YFSHAPVVQV 332
Cdd:cd17979    161 YFEGAPVVQV 170
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 163-618 9.38e-93

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: 315.94  E-value: 9.38e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 240
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGgkIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  241 IRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHND----FLLGVLQRLlpqRPDLKVILMSATIN 316
Cdd:TIGR01970   81 VRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADlglaLALDVQSSL---REDLKILAMSATLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  317 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQsaskseKLDPRPFLRVLEAIdnkypPEERGDLLVFLSGMAEISTVl 396
Cdd:TIGR01970  158 GERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQ------RLEDAVSRAVEHAL-----ASETGSILVFLPGQAEIRRV- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  397 dAAQAYATLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRL 476
Cdd:TIGR01970  226 -QEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRL 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  477 QEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAASVE 556
Cdd:TIGR01970  305 ETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALA 384

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649627  557 TAILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSP 618
Cdd:TIGR01970  385 AARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 163-634 1.51e-82

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 287.21  E-value: 1.51e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVP-QYLLAAGFS-HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 240
Cdd:PRK11664     4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINgKIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  241 IRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHND----FLLGVLQRLlpqRPDLKVILMSATIN 316
Cdd:PRK11664    84 MRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADlalaLLLDVQQGL---RDDLKLLIMSATLD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  317 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEAEQsaskseKLDP---RPFLRVLEaidnkyppEERGDLLVFLSGMAEIS 393
Cdd:PRK11664   161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQ------RFDEavaRATAELLR--------QESGSLLLFLPGVGEIQ 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  394 TVldAAQAYATLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKL 473
Cdd:PRK11664   227 RV--QEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGL 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  474 QRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPAA 553
Cdd:PRK11664   305 TRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAA 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  554 SVETAILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAepVLTIAAALSV---QSPftRSAQSNLDCA 630
Cdd:PRK11664   385 ALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDDEA--ALATAAKLAAileEPP--RSGSSDLGVA 460


                   ....
gi 1958649627  631 TARR 634
Cdd:PRK11664   461 LSRK 464
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 179-332 3.04e-78

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: 253.54  E-value: 3.04e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  179 HQVVVVAGDTGCGKSTQVPQYLLAAGFS-----HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKI 253
Cdd:cd17917      1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkggkgRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649627  254 VFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 332
Cdd:cd17917     81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 337-505 3.89e-77

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: 250.91  E-value: 3.89e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  337 FPITVVYQPQEAEQSASKSEKLDPRPFLRVLEAIDNKYPPEERGDLLVFLSGMAEISTVLDAAQAYATL--TQRWVVLPL 414
Cdd:cd18791      1 FPVEVYYLEDILELLGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSpdLGKLLVLPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  415 HSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAG 494
Cdd:cd18791     81 HSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAG 160

                          170
                   ....*....|.
gi 1958649627  495 RTGPGVCYRLY 505
Cdd:cd18791    161 RTRPGKCYRLY 171
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 163-332 6.66e-60

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: 202.97  E-value: 6.66e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 239
Cdd:cd17978      1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARggmIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  240 QIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVL-----QRLLPQRPDLKVILMSAT 314
Cdd:cd17978     81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVksaqrRRKEQKLSPLKVIIMSAT 160

                          170
                   ....*....|....*...
gi 1958649627  315 INISLFSSYFSHAPVVQV 332
Cdd:cd17978    161 LDADLFSEYFNGAPVLYI 178
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 163-332 8.77e-57

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: 194.50  E-value: 8.77e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--------VACTQPRRIACISLAKRVGFEsLSQYG 234
Cdd:cd17982      1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSpesdnpgmIGITQPRRVAAVSMAKRVAEE-LNVFG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  235 SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPD--------- 305
Cdd:cd17982     80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958649627  306 -LKVILMSATINISLFSS---YFSHAP-VVQV 332
Cdd:cd17982    160 pLKLVIMSATLRVEDFTEnklLFPRPPpVIKV 191
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 152-332 3.56e-56

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: 192.63  E-value: 3.56e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  152 RLAKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVG 226
Cdd:cd17973      2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHqpkklVACTQPRRVAAMSVAQRVA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  227 FESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDL 306
Cdd:cd17973     82 EEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDL 161

                          170       180
                   ....*....|....*....|....*.
gi 1958649627  307 KVILMSATINISLFSSYFSHAPVVQV 332
Cdd:cd17973    162 KLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 163-332 4.10e-56

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: 192.36  E-value: 4.10e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGF----SHVA---CTQPRRIACISLAKRVGFESLSQYGS 235
Cdd:cd17985      1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLqgppLPVAniiCTQPRRISAISVAERVAQERAERVGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  236 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATI 315
Cdd:cd17985     81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160

                          170
                   ....*....|....*..
gi 1958649627  316 NISLFSSYFSHAPVVQV 332
Cdd:cd17985    161 NAELFSDYFNSCPVIHI 177
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 163-332 3.15e-55

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: 189.64  E-value: 3.15e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 238
Cdd:cd17974      1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKgggkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  239 YQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINIS 318
Cdd:cd17974     81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160

                          170
                   ....*....|....
gi 1958649627  319 LFSSYFSHAPVVQV 332
Cdd:cd17974    161 KFSAFFDDAPIFRI 174
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 163-332 8.16e-54

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: 185.89  E-value: 8.16e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL--------AAGFSHVACTQPRRIACISLAKRVGFESLSQYG 234
Cdd:cd17975      1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLedlllnggTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  235 -----SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVI 309
Cdd:cd17975     81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160

                          170       180
                   ....*....|....*....|...
gi 1958649627  310 LMSATINISLFSSYFSHAPVVQV 332
Cdd:cd17975    161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 163-324 1.65e-53

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: 184.98  E-value: 1.65e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 238
Cdd:cd17980      1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAggrvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  239 YQIRFES-TRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINI 317
Cdd:cd17980     81 YCIRFDDcTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160


                   ....*..
gi 1958649627  318 SLFSSYF 324
Cdd:cd17980    161 EKFRDFF 167
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 159-333 4.57e-53

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


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 183.45  E-value: 4.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  159 ERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGS 235
Cdd:cd17971      2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSrgkIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  236 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATI 315
Cdd:cd17971     82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161

                          170
                   ....*....|....*...
gi 1958649627  316 NISLFSSYFSHAPVVQVP 333
Cdd:cd17971    162 DAVKFSQYFYEAPIFTIP 179
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 163-332 5.04e-53

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: 183.04  E-value: 5.04e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 239
Cdd:cd17989      1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIrglIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  240 QIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISL 319
Cdd:cd17989     81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160

                          170
                   ....*....|...
gi 1958649627  320 FSSYFSHAPVVQV 332
Cdd:cd17989    161 FSRHFNNAPIIEV 173
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 121-332 4.40e-52

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: 182.73  E-value: 4.40e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  121 GPGKGLPPERVSEfrrALLHYLDFQQKQAfGRLAKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYL 200
Cdd:cd17972     21 GPLAFATPEQISM---DLKNELMYQREQD-HNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYI 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  201 L-------AAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFEST--RSAATkIVFLTVGLLLRQIqcEPRL 271
Cdd:cd17972     97 LddfiqndRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVlpRPHAS-ILFCTVGVLLRKL--EAGI 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649627  272 PQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 332
Cdd:cd17972    174 RGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 163-332 4.90e-51

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: 177.73  E-value: 4.90e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-------AAGFSHVACTQPRRIACISLAKRVGFESLSQY-- 233
Cdd:cd17981      1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiergKGSSCRIVCTQPRRISAISVAERVAAERAESCgl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  234 GSQVGYQIRFES--TRSAATkIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILM 311
Cdd:cd17981     81 GNSTGYQIRLESrkPRKQGS-ILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159

                          170       180
                   ....*....|....*....|.
gi 1958649627  312 SATINISLFSSYFSHAPVVQV 332
Cdd:cd17981    160 SATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 163-329 5.54e-49

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: 171.49  E-value: 5.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 239
Cdd:cd17983      1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDygmIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  240 QIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISL 319
Cdd:cd17983     81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160

                          170
                   ....*....|
gi 1958649627  320 FSSYFSHAPV 329
Cdd:cd17983    161 FADFFGNVPI 170
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 163-332 7.91e-47

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: 165.74  E-value: 7.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFS-------HVACTQPRRIACISLAKRVGFESLSQYGS 235
Cdd:cd17976      1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLrgrgarcNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  236 QVGYQIRFES---TRSAAtkIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMS 312
Cdd:cd17976     81 NVGYQVRLESrppPRGGA--LLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158

                          170       180
                   ....*....|....*....|
gi 1958649627  313 ATINISLFSSYFSHAPVVQV 332
Cdd:cd17976    159 ATGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 163-332 1.52e-46

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: 165.03  E-value: 1.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 239
Cdd:cd17984      1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQhgmIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  240 QIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRP-----DLKVILMSAT 314
Cdd:cd17984     81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160

                          170
                   ....*....|....*...
gi 1958649627  315 INISLFSSYFSHAPVVQV 332
Cdd:cd17984    161 LELAKLSAFFGNCPVFDI 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 163-332 2.16e-44

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: 158.45  E-value: 2.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVGFESLSQYGSQV 237
Cdd:cd17987      1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANgipcrIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  238 GYQIRFESTRSAATKIVFLTVGLLLRQIQC-EPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATIN 316
Cdd:cd17987     81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160

                          170
                   ....*....|....*.
gi 1958649627  317 ISLFSSYFSHAPVVQV 332
Cdd:cd17987    161 VNLFIRYFGSCPVIYI 176
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 163-339 5.69e-41

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: 148.80  E-value: 5.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-----AAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQV 237
Cdd:cd17988      1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILdhyykRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  238 GYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPD-LKVILMSATIN 316
Cdd:cd17988     81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATIS 160

                          170       180
                   ....*....|....*....|...
gi 1958649627  317 ISLFSSYFShapVVQVPGRLFPI 339
Cdd:cd17988    161 CKEFADYFT---TPNNPAYVFEV 180
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 163-330 2.26e-35

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: 132.46  E-value: 2.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAA---GFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGY 239
Cdd:cd17990      1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAElwiAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  240 QIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVL---QRLLpqRPDLKVILMSATIN 316
Cdd:cd17990     81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLlevQQLL--RDDLRLLAMSATLD 158

                          170
                   ....*....|....
gi 1958649627  317 ISLFSSYFSHAPVV 330
Cdd:cd17990    159 GDGLAALLPEAPVV 172
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 163-332 6.28e-34

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


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 128.79  E-value: 6.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  163 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQ 236
Cdd:cd17977      1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHgvVVCTQVHKQTAVWLALRVADEMDVNIGHE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  237 VGYQIRFESTRSAATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATIN 316
Cdd:cd17977     81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160

                          170
                   ....*....|....*.
gi 1958649627  317 ISLFSSYFSHAPVVQV 332
Cdd:cd17977    161 SSKLLSYYGNVPLIEV 176
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 181-332 5.34e-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: 108.83  E-value: 5.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  181 VVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIV 254
Cdd:cd17986     20 IVLVSGEPGSGKSTQVPQwcaeFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPNTILR 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649627  255 FLTVGLLLRQIQCEPRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 332
Cdd:cd17986    100 FCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
176-341 1.49e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 93.71  E-value: 1.49e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   176 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 244
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   245 STRSAATKIVFLTVGLLLRQIQCEP-RLPQYQVLIVDEVHER--HLHNDFLLGVLQRLlpqRPDLKVILMSATI--NISL 319
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176

                           170       180
                    ....*....|....*....|..
gi 1958649627   320 FSSYFSHAPVVQVPGRLFPITV 341
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 164-505 6.54e-20

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 95.43  E-value: 6.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  164 PIAQygNRILQTLKEHQVVVVAGDTGCGKSTQVPQYL-----LAAGFSH------------VACTQPR----RIACISLA 222
Cdd:PHA02653   166 PDVQ--LKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnyLFGGFDNldkidpnfierpIVLSLPRvalvRLHSITLL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  223 KRVGFESLSqyGSQVgyQIRFES-------TRSAATKIVFLTVGLLLRqiqcepRLPQYQVLIVDEVHERHLHNDFLLGV 295
Cdd:PHA02653   244 KSLGFDEID--GSPI--SLKYGSipdelinTNPKPYGLVFSTHKLTLN------KLFDYGTVIIDEVHEHDQIGDIIIAV 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  296 LQRLLPQRPDLkvILMSATI-----NISLFssyFSHAPVVQVPG-RLFPITVVY-----QPQEAEQSASKSEKLdprpfl 364
Cdd:PHA02653   314 ARKHIDKIRSL--FLMTATLeddrdRIKEF---FPNPAFVHIPGgTLFPISEVYvknkyNPKNKRAYIEEEKKN------ 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  365 rVLEAIdNKYPPEERGDLLVFLSGMAEIstvldaaQAYA-TLTQRwvvLPLHSALSVadQDKVFDVAP------AGVRKC 437
Cdd:PHA02653   383 -IVTAL-KKYTPPKGSSGIVFVASVSQC-------EEYKkYLEKR---LPIYDFYII--HGKVPNIDEilekvySSKNPS 448

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958649627  438 IL-STNIAETSVTIDGIRFVVDSGKVkemsYDPQAKLQRlqEFWISQASAEQRKGRAGRTGPGVCYRLY 505
Cdd:PHA02653   449 IIiSTPYLESSVTIRNATHVYDTGRV----YVPEPFGGK--EMFISKSMRTQRKGRVGRVSPGTYVYFY 511
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 558-646 1.87e-19

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: 84.60  E-value: 1.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  558 AILYLQDQGALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDC-------- 629
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSaakaarrr 80

                           90       100
                   ....*....|....*....|....
gi 1958649627  630 -------ATARRPLESDQGDPFTL 646
Cdd:pfam04408   81 rraadekARAKFARLDLEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 566-646 4.79e-19

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: 82.70  E-value: 4.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   566 GALDSSEALTPIGSLLAQLPVDVVIGKMMILGSMFSLAEPVLTIAAALSVQSPFTRSAQSnlDCATARRPLESDQGDPFT 645
Cdd:smart00847    3 GALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKRE--DADAARRRFADPESDHLT 80


                    .
gi 1958649627   646 L 646
Cdd:smart00847   81 L 81
HELICc smart00490
helicase superfamily c-terminal domain;
411-497 1.67e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.85  E-value: 1.67e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627   411 VLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRK 490
Cdd:smart00490   14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDL----------PWSPASYIQRI 75


                    ....*..
gi 1958649627   491 GRAGRTG 497
Cdd:smart00490   76 GRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 367-497 1.96e-10

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: 59.15  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  367 LEAIDNKYPPEERGDLLVFLSgmaeisTVLDAAQAYATLTQRWVVLPLHSALSVADQDKVFDVAPAGVRKCILSTNIAET 446
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFSQ------TKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958649627  447 SVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRKGRAGRTG 497
Cdd:pfam00271   77 GLDLPDVDLVIN--------YDL----------PWNPASYIQRIGRAGRAG 109
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 182-314 1.70e-09

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: 57.41  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  182 VVVAGDTGCGKSTQVP----QYLLAAGF-SHVACtqPRRIACISLAKRvgFESLSQYGSQVGYQIRFES--TRSAAT--- 251
Cdd:cd00046      4 VLITAPTGSGKTLAALlaalLLLLKKGKkVLVLV--PTKALALQTAER--LRELFGPGIRVAVLVGGSSaeEREKNKlgd 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958649627  252 -KIVFLTVGLLLRQIQCE--PRLPQYQVLIVDEVHERHLHNDFLLGVLQRLLP-QRPDLKVILMSAT 314
Cdd:cd00046     80 aDIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKaGLKNAQVILLSAT 146
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 798-909 4.52e-08

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: 51.48  E-value: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  798 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgpeasgregsqdgkdqMSCKhqLL 877
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958649627  878 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 909
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 172-319 1.36e-07

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: 52.24  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  172 ILQTLKEHQVVVVAgDTGCGKSTQvpqYLLAAgFSHVACTQPRRIACI-----SLAKRVgFESLSQYGSQVGYQIRFEST 246
Cdd:pfam00270    8 IPAILEGRDVLVQA-PTGSGKTLA---FLLPA-LEALDKLDNGPQALVlaptrELAEQI-YEELKKLGKGLGLKVASLLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  247 RS---------AATKIVFLTVGLLLRQIQCEPRLPQYQVLIVDEVHeRHLHNDF---LLGVLQRLLPQRpdlKVILMSAT 314
Cdd:pfam00270   82 GDsrkeqleklKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRLPKKR---QILLLSAT 157


                   ....*
gi 1958649627  315 INISL 319
Cdd:pfam00270  158 LPRNL 162
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 181-315 1.18e-03

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 41.20  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  181 VVVVAGDTGCGKSTQVPQ---YLLAAGFS-HVACTQPRRIAcislakrvGFESLSQYGSQVGYQIRFESTRSAATKIVFl 256
Cdd:cd03115      2 VILLVGLQGSGKTTTLAKlarYYQEKGKKvLLIAADTFRAA--------AVEQLKTLAEKLGVPVFESYTGTDPASIAQ- 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  257 tvglllRQIQcEPRLPQYQVLIVDEVHeRHLHNDFLLGVLQRLLP-QRPDLKVILMSATI 315
Cdd:cd03115     73 ------EAVE-KAKLEGYDVLLVDTAG-RLQKDEPLMEELKKVKEvESPDEVLLVLDATT 124
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 438-505 3.49e-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: 3.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649627  438 ILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRKGRAGRTG--PGVCYRLY 505
Cdd:cd18785     26 LVATNVLGEGIDVPSLDTVIF--------FDP----------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
 
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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