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Conserved domains on  [gi|311033371|sp|Q14147|]
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RecName: Full=Probable ATP-dependent RNA helicase DHX34; AltName: Full=DEAH box protein 34; AltName: Full=DExH-box helicase 34

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];
160-624 6.81e-162

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: 501.53  E-value: 6.81e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  160 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 236
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  237 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPT-RPDLKVILMSATIN 315
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  316 ISLFSSYFSNAPVVQVPGRLFPITVVYQPQEAEpttskseklDPRPFLRVLESIDHKYPpEERGDLLVFLSGMAEISAVL 395
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPAD---------ERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  396 EA-AQTYASHTqrwVVLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQR 474
Cdd:COG1643   238 EAlRGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  475 LQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASL 554
Cdd:COG1643   315 LPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAI 394

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  555 ETAILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQS 624
Cdd:COG1643   395 ADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGS 464
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 800-911 1.31e-07

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: 49.94  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   800 LKLVLGRGLYPQLAVPDAfnssrkDSDQIFHTQAKQGAVLHPTCVFAgspevlhaqeleasncdgsrddkDKMSSKHQLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLF-----------------------NEKTFPPEWV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 311033371   880 SFVSLLETNKPYLVNCVRIPALQsLLLFSRSL 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
160-624 6.81e-162

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 501.53  E-value: 6.81e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  160 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 236
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  237 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPT-RPDLKVILMSATIN 315
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  316 ISLFSSYFSNAPVVQVPGRLFPITVVYQPQEAEpttskseklDPRPFLRVLESIDHKYPpEERGDLLVFLSGMAEISAVL 395
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPAD---------ERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  396 EA-AQTYASHTqrwVVLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQR 474
Cdd:COG1643   238 EAlRGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  475 LQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASL 554
Cdd:COG1643   315 LPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAI 394

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  555 ETAILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQS 624
Cdd:COG1643   395 ADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGS 464
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 147-703 2.02e-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: 416.09  E-value: 2.02e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   147 QAFGRLAKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGF-SH--VACTQPRRIAC 217
Cdd:TIGR01967   45 AACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRgSHglIGHTQPRRLAA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   218 ISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQR 297
Cdd:TIGR01967  125 RTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQ 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   298 LLPTRPDLKVILMSATINISLFSSYFSNAPVVQVPGRLFPITVVYQpqeaePTTSKSEKLDPRPFLRVLESIDhKYPPEE 377
Cdd:TIGR01967  205 LLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYR-----PLVEEQEDDDLDQLEAILDAVD-ELFAEG 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   378 RGDLLVFLSGMAEISavlEAAQTYASHTQRWV-VLPLHSALSVADQDKVFDvaPPGVRKCILSTNIAETSVTIDGIRFVV 456
Cdd:TIGR01967  279 PGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVI 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   457 DSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMS 536
Cdd:TIGR01967  354 DTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALR 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   537 VGDPRTFPFIEPPPPASLETAILYLRDQGALDSSEA---LTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALS 613
Cdd:TIGR01967  434 LGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALS 513

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   614 VQSPFTRSAQSSPECAAARRPLESDQGDPFTLFNVFNAWVQVKSERSRNS-RKWCRRRGIEEHRLYEMANLRRQFKELLE 692
Cdd:TIGR01967  514 IQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQfRNACRKQYLNYLRVREWQDIYRQLTQVVK 593

                          570
                   ....*....|.
gi 311033371   693 DHGLLAGAQAA 703
Cdd:TIGR01967  594 ELGLKLNEEPA 604
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 162-704 3.64e-124

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 412.92  E-value: 3.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGY 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISL 318
Cdd:PRK11131  153 KVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPER 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  319 FSSYFSNAPVVQVPGRLFPITVVYQPQEAEPTTSKSEKLDPrpflrVLESIDhKYPPEERGDLLVFLSGMAEISAVLEAA 398
Cdd:PRK11131  233 FSRHFNNAPIIEVSGRTYPVEVRYRPIVEEADDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIRDTADAL 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  399 QTYA-SHTQrwvVLPLHSALSVADQDKVFDvaPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQE 477
Cdd:PRK11131  307 NKLNlRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  478 FWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASLETA 557
Cdd:PRK11131  382 EPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDG 461

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  558 ILYLRDQGALDSSEA-----LTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSA---QSSPEca 629
Cdd:PRK11131  462 VRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkqQASDE-- 539

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311033371  630 aARRPLESDQGDPFTLFNVFNAWVQVKSERSRNS-RKWCRRRGIEEHRLYEMANLRRQFKELLEDHGLLAGAQAAQ 704
Cdd:PRK11131  540 -KHRRFADKESDFLAFVNLWNYLQEQQKALSSNQfRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAE 614
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 162-331 1.17e-109

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: 339.42  E-value: 1.17e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 241
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  242 FESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISLFSS 321
Cdd:cd17979    81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160

                         170
                  ....*....|
gi 311033371  322 YFSNAPVVQV 331
Cdd:cd17979   161 YFEGAPVVQV 170
DEXDc smart00487
DEAD-like helicases superfamily;
175-340 2.06e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.41  E-value: 2.06e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    175 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 243
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    244 STRSAATKIVFLTVGLLLRQIQREP-SLPQYEVLIVDEVHER--HLHNDFLLGVLQRLlptRPDLKVILMSATI--NISL 318
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176

                           170       180
                    ....*....|....*....|..
gi 311033371    319 FSSYFSNAPVVQVPGRLFPITV 340
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 557-633 1.62e-20

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: 87.68  E-value: 1.62e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311033371   557 AILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQSSPECAAARR 633
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAA 77
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 800-911 1.31e-07

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: 49.94  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   800 LKLVLGRGLYPQLAVPDAfnssrkDSDQIFHTQAKQGAVLHPTCVFAgspevlhaqeleasncdgsrddkDKMSSKHQLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLF-----------------------NEKTFPPEWV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 311033371   880 SFVSLLETNKPYLVNCVRIPALQsLLLFSRSL 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
160-624 6.81e-162

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 501.53  E-value: 6.81e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  160 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 236
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  237 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPT-RPDLKVILMSATIN 315
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  316 ISLFSSYFSNAPVVQVPGRLFPITVVYQPQEAEpttskseklDPRPFLRVLESIDHKYPpEERGDLLVFLSGMAEISAVL 395
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPAD---------ERDLEDAVADAVREALA-EEPGDILVFLPGEREIRRTA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  396 EA-AQTYASHTqrwVVLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQR 474
Cdd:COG1643   238 EAlRGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  475 LQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASL 554
Cdd:COG1643   315 LPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAI 394

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  555 ETAILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQS 624
Cdd:COG1643   395 ADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGS 464
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
 147-703 2.02e-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: 416.09  E-value: 2.02e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   147 QAFGRLAKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGF-SH--VACTQPRRIAC 217
Cdd:TIGR01967   45 AACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRgSHglIGHTQPRRLAA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   218 ISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQR 297
Cdd:TIGR01967  125 RTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQ 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   298 LLPTRPDLKVILMSATINISLFSSYFSNAPVVQVPGRLFPITVVYQpqeaePTTSKSEKLDPRPFLRVLESIDhKYPPEE 377
Cdd:TIGR01967  205 LLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYR-----PLVEEQEDDDLDQLEAILDAVD-ELFAEG 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   378 RGDLLVFLSGMAEISavlEAAQTYASHTQRWV-VLPLHSALSVADQDKVFDvaPPGVRKCILSTNIAETSVTIDGIRFVV 456
Cdd:TIGR01967  279 PGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQQRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVI 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   457 DSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMS 536
Cdd:TIGR01967  354 DTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALR 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   537 VGDPRTFPFIEPPPPASLETAILYLRDQGALDSSEA---LTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALS 613
Cdd:TIGR01967  434 LGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALS 513

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   614 VQSPFTRSAQSSPECAAARRPLESDQGDPFTLFNVFNAWVQVKSERSRNS-RKWCRRRGIEEHRLYEMANLRRQFKELLE 692
Cdd:TIGR01967  514 IQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQfRNACRKQYLNYLRVREWQDIYRQLTQVVK 593

                          570
                   ....*....|.
gi 311033371   693 DHGLLAGAQAA 703
Cdd:TIGR01967  594 ELGLKLNEEPA 604
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 162-704 3.64e-124

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 412.92  E-value: 3.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGY 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISL 318
Cdd:PRK11131  153 KVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPER 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  319 FSSYFSNAPVVQVPGRLFPITVVYQPQEAEPTTSKSEKLDPrpflrVLESIDhKYPPEERGDLLVFLSGMAEISAVLEAA 398
Cdd:PRK11131  233 FSRHFNNAPIIEVSGRTYPVEVRYRPIVEEADDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIRDTADAL 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  399 QTYA-SHTQrwvVLPLHSALSVADQDKVFDvaPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQE 477
Cdd:PRK11131  307 NKLNlRHTE---ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPI 381

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  478 FWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASLETA 557
Cdd:PRK11131  382 EPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDG 461

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  558 ILYLRDQGALDSSEA-----LTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSA---QSSPEca 629
Cdd:PRK11131  462 VRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkqQASDE-- 539

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311033371  630 aARRPLESDQGDPFTLFNVFNAWVQVKSERSRNS-RKWCRRRGIEEHRLYEMANLRRQFKELLEDHGLLAGAQAAQ 704
Cdd:PRK11131  540 -KHRRFADKESDFLAFVNLWNYLQEQQKALSSNQfRRLCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAE 614
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 162-331 1.17e-109

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: 339.42  E-value: 1.17e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 241
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  242 FESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISLFSS 321
Cdd:cd17979    81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160

                         170
                  ....*....|
gi 311033371  322 YFSNAPVVQV 331
Cdd:cd17979   161 YFEGAPVVQV 170
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 162-617 4.04e-91

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: 311.31  E-value: 4.04e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 239
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGgkIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   240 IRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHND----FLLGVLQRLlptRPDLKVILMSATIN 315
Cdd:TIGR01970   81 VRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADlglaLALDVQSSL---REDLKILAMSATLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   316 ISLFSSYFSNAPVVQVPGRLFPITVVYQPQEAEpttsksEKLDPRPFLRVLESIDHkyppeERGDLLVFLSGMAEISAVL 395
Cdd:TIGR01970  158 GERLSSLLPDAPVVESEGRSFPVEIRYLPLRGD------QRLEDAVSRAVEHALAS-----ETGSILVFLPGQAEIRRVQ 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   396 EA-AQTYASHTQrwvVLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQR 474
Cdd:TIGR01970  227 EQlAERLDSDVL---ICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITR 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   475 LQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPPASL 554
Cdd:TIGR01970  304 LETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVAL 383

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311033371   555 ETAILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSP 617
Cdd:TIGR01970  384 AAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 162-612 1.06e-85

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 296.07  E-value: 1.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVP-QYLLAAGFS-HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 239
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINgKIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  240 IRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHND----FLLGVLQRLlptRPDLKVILMSATIN 315
Cdd:PRK11664   84 MRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADlalaLLLDVQQGL---RDDLKLLIMSATLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  316 ISLFSSYFSNAPVVQVPGRLFPITVVYQPqeaeptTSKSEKLDP---RPFLRVLEsidhkyppEERGDLLVFLSGMAEIS 392
Cdd:PRK11664  161 NDRLQQLLPDAPVIVSEGRSFPVERRYQP------LPAHQRFDEavaRATAELLR--------QESGSLLLFLPGVGEIQ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  393 AVLEA-AQTYASHTqrwVVLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAK 471
Cdd:PRK11664  227 RVQEQlASRVASDV---LLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  472 LQRLQEFWISQASAEQRKGRAGRTGPGVCFRLYAESDYDAFAPYPVPEIRRVALDSLVLQMKSMSVGDPRTFPFIEPPPP 551
Cdd:PRK11664  304 LTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPA 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311033371  552 ASLETAILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSlvEPVLTIAAAL 612
Cdd:PRK11664  384 AALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKL 442
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 178-331 2.97e-79

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: 256.62  E-value: 2.97e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  178 HQVVVVAGDTGCGKSTQVPQYLLAAGFS-----HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKI 252
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkggkgRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311033371  253 VFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISLFSSYFSNAPVVQV 331
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 ...
 336-504 1.44e-78

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: 255.15  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  336 FPITVVYQPQEAEPTTSKSEKLDPRPFLRVLESIDHKYPPEERGDLLVFLSGMAEISAVLEAAQTYASH--TQRWVVLPL 413
Cdd:cd18791     1 FPVEVYYLEDILELLGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSpdLGKLLVLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  414 HSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAG 493
Cdd:cd18791    81 HSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAG 160

                         170
                  ....*....|.
gi 311033371  494 RTGPGVCFRLY 504
Cdd:cd18791   161 RTRPGKCYRLY 171
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 162-331 1.26e-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: 204.90  E-value: 1.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARggmIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVL-----QRLLPTRPDLKVILMSAT 313
Cdd:cd17978    81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVksaqrRRKEQKLSPLKVIIMSAT 160

                         170
                  ....*....|....*...
gi 311033371  314 INISLFSSYFSNAPVVQV 331
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 ...
 162-331 6.66e-59

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: 200.66  E-value: 6.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--------VACTQPRRIACISLAKRVGFEsLSQYG 233
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSpesdnpgmIGITQPRRVAAVSMAKRVAEE-LNVFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  234 SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPD--------- 304
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 311033371  305 -LKVILMSATINISLFSS---YFSNAP-VVQV 331
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 ...
 151-331 2.54e-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: 193.02  E-value: 2.54e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  151 RLAKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVG 225
Cdd:cd17973     2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHqpkklVACTQPRRVAAMSVAQRVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  226 FESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDL 305
Cdd:cd17973    82 EEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDL 161

                         170       180
                  ....*....|....*....|....*.
gi 311033371  306 KVILMSATINISLFSSYFSNAPVVQV 331
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 ...
 162-331 3.61e-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: 3.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGF----SHVA---CTQPRRIACISLAKRVGFESLSQYGS 234
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLqgppLPVAniiCTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  235 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATI 314
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160

                         170
                  ....*....|....*..
gi 311033371  315 NISLFSSYFSNAPVVQV 331
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 162-331 1.22e-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: 190.79  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 237
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKgggkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  238 YQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINIS 317
Cdd:cd17974    81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160

                         170
                  ....*....|....
gi 311033371  318 LFSSYFSNAPVVQV 331
Cdd:cd17974   161 KFSAFFDDAPIFRI 174
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 162-331 4.87e-54

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: 186.12  E-value: 4.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIrglIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISL 318
Cdd:cd17989    81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160

                         170
                  ....*....|...
gi 311033371  319 FSSYFSNAPVVQV 331
Cdd:cd17989   161 FSRHFNNAPIIEV 173
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 158-332 9.14e-54

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: 185.38  E-value: 9.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  158 ERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGS 234
Cdd:cd17971     2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSrgkIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  235 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATI 314
Cdd:cd17971    82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161

                         170
                  ....*....|....*...
gi 311033371  315 NISLFSSYFSNAPVVQVP 332
Cdd:cd17971   162 DAVKFSQYFYEAPIFTIP 179
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 137-331 2.39e-53

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: 186.58  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  137 LLHYLDFgQKQAFGRLAKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-------AAGFSHVAC 209
Cdd:cd17972    35 LKNELMY-QREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILddfiqndRAAECNIVV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  210 TQPRRIACISLAKRVGFESLSQYGSQVGYQIRFEST--RSAATkIVFLTVGLLLRQIqrEPSLPQYEVLIVDEVHERHLH 287
Cdd:cd17972   114 TQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVlpRPHAS-ILFCTVGVLLRKL--EAGIRGISHVIVDEIHERDIN 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 311033371  288 NDFLLGVLQRLLPTRPDLKVILMSATINISLFSSYFSNAPVVQV 331
Cdd:cd17972   191 TDFLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 162-323 5.12e-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: 183.82  E-value: 5.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 237
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAggrvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  238 YQIRFES-TRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINI 316
Cdd:cd17980    81 YCIRFDDcTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160


                  ....*..
gi 311033371  317 SLFSSYF 323
Cdd:cd17980   161 EKFRDFF 167
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 162-331 6.43e-53

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: 183.19  E-value: 6.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL--------AAGFSHVACTQPRRIACISLAKRVGFESLSQYG 233
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLedlllnggTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  234 -----SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVI 308
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160

                         170       180
                  ....*....|....*....|...
gi 311033371  309 LMSATINISLFSSYFSNAPVVQV 331
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 162-331 3.38e-52

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: 181.19  E-value: 3.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-------AAGFSHVACTQPRRIACISLAKRVGFESLSQY-- 232
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiergKGSSCRIVCTQPRRISAISVAERVAAERAESCgl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  233 GSQVGYQIRFES--TRSAATkIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILM 310
Cdd:cd17981    81 GNSTGYQIRLESrkPRKQGS-ILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159

                         170       180
                  ....*....|....*....|.
gi 311033371  311 SATINISLFSSYFSNAPVVQV 331
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 ...
 162-328 7.81e-51

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: 176.88  E-value: 7.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDygmIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISL 318
Cdd:cd17983    81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160

                         170
                  ....*....|
gi 311033371  319 FSSYFSNAPV 328
Cdd:cd17983   161 FADFFGNVPI 170
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 162-331 1.59e-46

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: 164.97  E-value: 1.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFS-------HVACTQPRRIACISLAKRVGFESLSQYGS 234
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLrgrgarcNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  235 QVGYQIRFES---TRSAAtkIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMS 311
Cdd:cd17976    81 NVGYQVRLESrppPRGGA--LLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158

                         170       180
                  ....*....|....*....|
gi 311033371  312 ATINISLFSSYFSNAPVVQV 331
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 ...
 162-331 2.01e-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: 164.64  E-value: 2.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQhgmIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRP-----DLKVILMSAT 313
Cdd:cd17984    81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160

                         170
                  ....*....|....*...
gi 311033371  314 INISLFSSYFSNAPVVQV 331
Cdd:cd17984   161 LELAKLSAFFGNCPVFDI 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 162-331 1.28e-45

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: 161.92  E-value: 1.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVGFESLSQYGSQV 236
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANgipcrIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  237 GYQIRFESTRSAATKIVFLTVGLLLRQIQ-REPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATIN 315
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160

                         170
                  ....*....|....*.
gi 311033371  316 ISLFSSYFSNAPVVQV 331
Cdd:cd17987   161 VNLFIRYFGSCPVIYI 176
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 162-338 1.84e-42

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: 153.04  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-----AAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQV 236
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILdhyykRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  237 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPD-LKVILMSATIN 315
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATIS 160

                         170       180
                  ....*....|....*....|...
gi 311033371  316 ISLFSSYFSnapVVQVPGRLFPI 338
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 ...
 162-329 9.86e-37

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: 136.69  E-value: 9.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAA---GFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGY 238
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAElwiAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  239 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVL---QRLLptRPDLKVILMSATIN 315
Cdd:cd17990    81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLlevQQLL--RDDLRLLAMSATLD 158

                         170
                  ....*....|....
gi 311033371  316 ISLFSSYFSNAPVV 329
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 ...
 162-331 6.73e-35

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: 131.49  E-value: 6.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  162 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQ 235
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHgvVVCTQVHKQTAVWLALRVADEMDVNIGHE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  236 VGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATIN 315
Cdd:cd17977    81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160

                         170
                  ....*....|....*.
gi 311033371  316 ISLFSSYFSNAPVVQV 331
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 ...
 180-331 8.74e-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: 108.06  E-value: 8.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  180 VVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIV 253
Cdd:cd17986    20 IVLVSGEPGSGKSTQVPQwcaeFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPNTILR 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311033371  254 FLTVGLLLRQIQREPSLPQYEVLIVDEVHERHLHNDFLLGVLQRLLPTRPDLKVILMSATINISLFSSYFSNAPVVQV 331
Cdd:cd17986   100 FCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
175-340 2.06e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.41  E-value: 2.06e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    175 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 243
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    244 STRSAATKIVFLTVGLLLRQIQREP-SLPQYEVLIVDEVHER--HLHNDFLLGVLQRLlptRPDLKVILMSATI--NISL 318
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176

                           170       180
                    ....*....|....*....|..
gi 311033371    319 FSSYFSNAPVVQVPGRLFPITV 340
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 143-504 3.41e-22

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 102.75  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  143 FGQKQAFGR--LAKLQreraalPIAQygNRILQTLKEHQVVVVAGDTGCGKSTQVPQYL-----LAAGFSH--------- 206
Cdd:PHA02653  150 LGNPEPFSKipLASLQ------PDVQ--LKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnyLFGGFDNldkidpnfi 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  207 ---VACTQPR----RIACISLAKRVGFESLSqyGSQVgyQIRFES-------TRSAATKIVFLTVGLLLRqiqrepSLPQ 272
Cdd:PHA02653  222 erpIVLSLPRvalvRLHSITLLKSLGFDEID--GSPI--SLKYGSipdelinTNPKPYGLVFSTHKLTLN------KLFD 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  273 YEVLIVDEVHERHLHNDFLLGVLqRLLPTRPDlKVILMSATI-----NISLFssyFSNAPVVQVPG-RLFPITVVYQPQE 346
Cdd:PHA02653  292 YGTVIIDEVHEHDQIGDIIIAVA-RKHIDKIR-SLFLMTATLeddrdRIKEF---FPNPAFVHIPGgTLFPISEVYVKNK 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  347 AEPTTSKS----EKldprpflRVLESIDHKYPPEERGDLLVFLsgmAEISAVLEAAQTYASHTQRWVVLPLHS-ALSVAD 421
Cdd:PHA02653  367 YNPKNKRAyieeEK-------KNIVTALKKYTPPKGSSGIVFV---ASVSQCEEYKKYLEKRLPIYDFYIIHGkVPNIDE 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  422 Q-DKVFDVAPPGVrkcILSTNIAETSVTIDGIRFVVDSGKVkemsYDPQAKLQRlqEFWISQASAEQRKGRAGRTGPGVC 500
Cdd:PHA02653  437 IlEKVYSSKNPSI---IISTPYLESSVTIRNATHVYDTGRV----YVPEPFGGK--EMFISKSMRTQRKGRVGRVSPGTY 507


                  ....
gi 311033371  501 FRLY 504
Cdd:PHA02653  508 VYFY 511
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 557-633 1.62e-20

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: 87.68  E-value: 1.62e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311033371   557 AILYLRDQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQSSPECAAARR 633
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAA 77
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 565-645 5.13e-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: 5.13e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    565 GALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLVEPVLTIAAALSVQSPFTRSAQSspECAAARRPLESDQGDPFT 644
Cdd:smart00847    3 GALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKRE--DADAARRRFADPESDHLT 80


                    .
gi 311033371    645 L 645
Cdd:smart00847   81 L 81
HELICc smart00490
helicase superfamily c-terminal domain;
410-496 3.73e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 65.70  E-value: 3.73e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371    410 VLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRK 489
Cdd:smart00490   14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDL----------PWSPASYIQRI 75


                    ....*..
gi 311033371    490 GRAGRTG 496
Cdd:smart00490   76 GRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 410-496 5.72e-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: 57.61  E-value: 5.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   410 VLPLHSALSVADQDKVFDVAPPGVRKCILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRK 489
Cdd:pfam00271   41 VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVIN--------YDL----------PWNPASYIQRI 102


                   ....*..
gi 311033371   490 GRAGRTG 496
Cdd:pfam00271  103 GRAGRAG 109
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 181-313 2.34e-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: 57.03  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  181 VVVAGDTGCGKSTQVP----QYLLAAGFShVACTQPRRIACISLAKRvgFESLSQYGSQVGYQIRFES--TRSAAT---- 250
Cdd:cd00046     4 VLITAPTGSGKTLAALlaalLLLLKKGKK-VLVLVPTKALALQTAER--LRELFGPGIRVAVLVGGSSaeEREKNKlgda 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311033371  251 KIVFLTVGLLLRQIQRE--PSLPQYEVLIVDEVHER----HLHNDFLLGVLQRLLptrPDLKVILMSAT 313
Cdd:cd00046    81 DIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALlidsRGALILDLAVRKAGL---KNAQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 171-318 1.30e-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: 52.63  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   171 ILQTLKEHQVVVVAgDTGCGKSTQvpqYLLAAgFSHVACTQPRRIACI-----SLAKRVgFESLSQYGSQVGYQIRFEST 245
Cdd:pfam00270    8 IPAILEGRDVLVQA-PTGSGKTLA---FLLPA-LEALDKLDNGPQALVlaptrELAEQI-YEELKKLGKGLGLKVASLLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   246 RS---------AATKIVFLTVGLLLRQIQREPSLPQYEVLIVDEVHeRHLHNDF---LLGVLQRLlptRPDLKVILMSAT 313
Cdd:pfam00270   82 GDsrkeqleklKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL---PKKRQILLLSAT 157


                   ....*
gi 311033371   314 INISL 318
Cdd:pfam00270  158 LPRNL 162
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
 800-911 1.31e-07

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: 49.94  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371   800 LKLVLGRGLYPQLAVPDAfnssrkDSDQIFHTQAKQGAVLHPTCVFAgspevlhaqeleasncdgsrddkDKMSSKHQLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLF-----------------------NEKTFPPEWV 51

                           90       100       110
                   ....*....|....*....|....*....|..
gi 311033371   880 SFVSLLETNKPYLVNCVRIPALQsLLLFSRSL 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 180-314 2.15e-04

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: 43.52  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  180 VVVVAGDTGCGKSTQVPQ---YLLAAGFS-HVACTQPRRIAcislakrvGFESLSQYGSQVGYQIRFESTRSAATKIVFl 255
Cdd:cd03115     2 VILLVGLQGSGKTTTLAKlarYYQEKGKKvLLIAADTFRAA--------AVEQLKTLAEKLGVPVFESYTGTDPASIAQ- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  256 tvglllrQIQREPSLPQYEVLIVDEVHeRHLHNDFLLGVLQRLLP-TRPDLKVILMSATI 314
Cdd:cd03115    73 -------EAVEKAKLEGYDVLLVDTAG-RLQKDEPLMEELKKVKEvESPDEVLLVLDATT 124
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 437-504 1.97e-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: 38.07  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033371  437 ILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRKGRAGRTG--PGVCFRLY 504
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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