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Conserved domains on  [gi|552953797|ref|NP_001272860|]
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probable ATP-dependent RNA helicase DHX34 [Mus musculus]

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

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];
162-628 2.26e-164

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: 508.08  E-value: 2.26e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  162 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 238
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  239 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 317
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  318 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEADQtasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 392
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  393 ITTVLDAAQAyaSLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 472
Cdd:COG1643   233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  473 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 552
Cdd:COG1643   311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552953797  553 PASVETAILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 628
Cdd:COG1643   391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
800-911 4.53e-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: 4.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   800 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgqeasgqegsqdgrdqMSCKhqLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51
                           90       100       110
                   ....*....|....*....|....*....|..
gi 552953797   880 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
162-628 2.26e-164

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 508.08  E-value: 2.26e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  162 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 238
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  239 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 317
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  318 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEADQtasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 392
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  393 ITTVLDAAQAyaSLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 472
Cdd:COG1643   233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  473 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 552
Cdd:COG1643   311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552953797  553 PASVETAILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 628
Cdd:COG1643   391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
118-698 2.50e-127

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: 421.48  E-value: 2.50e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   118 RGRHGPGR---GLPPERVSEFRRALLHYLDFQQKQAFGRLVKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGD 188
Cdd:TIGR01967   11 RDRHRLRRrlhKLRKDHDQDRAIAALAKFRERIDAACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   189 TGCGKSTQVPQYLLAAGF-SH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQ 265
Cdd:TIGR01967   91 TGSGKTTQLPKICLELGRgSHglIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   266 IQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQ 345
Cdd:TIGR01967  171 TQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYR 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   346 PQEADQTASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEITtvlDAAQAYASLTQRWV-VLPLHSALSVSDQ 424
Cdd:TIGR01967  251 PLVEEQEDDDLDQLEA-----ILDAVD-ELFAEGPGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   425 DKVFDvaPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYR 504
Cdd:TIGR01967  322 QRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   505 LYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPASVETAILYLQEQGALDSSEA---LTPIGSL 581
Cdd:TIGR01967  400 LYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   582 LAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSER 661
Cdd:TIGR01967  480 LAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQAL 559
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 552953797   662 SGNS-RKWCRRRGVEEHRLYEMANLRRQFKELLEDHGL 698
Cdd:TIGR01967  560 SANQfRNACRKQYLNYLRVREWQDIYRQLTQVVKELGL 597
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
121-670 8.99e-123

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 409.06  E-value: 8.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  121 HGPGRGLPPERvsefRRALLHYLDFQQKQAFGRLvkLQRERA--------ALPIAQYGNRILQTLKEHQVVVVAGDTGCG 192
Cdd:PRK11131   28 HGAKKIKNPDA----QQAIFQEIAKEIAQAAQRV--LLREAArpeitypeNLPVSQKKQDILEAIRDHQVVIVAGETGSG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  193 KSTQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQRE 269
Cdd:PRK11131  102 KTTQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  270 PSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEA 349
Cdd:PRK11131  182 RLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  350 DQTASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEITtvlDAAQAYASLTQRWV-VLPLHSALSVSDQDKVF 428
Cdd:PRK11131  262 EADDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIR---DTADALNKLNLRHTeILPLYARLSNSEQNRVF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  429 DvaPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAE 508
Cdd:PRK11131  333 Q--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSE 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  509 SDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPASVETAILYLQEQGALDSSEA-----LTPIGSLLA 583
Cdd:PRK11131  411 DDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLA 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  584 QLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSG 663
Cdd:PRK11131  491 QLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSS 570

                  ....*...
gi 552953797  664 NS-RKWCR 670
Cdd:PRK11131  571 NQfRRLCR 578
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
164-333 1.82e-108

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: 335.95  E-value: 1.82e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 243
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  244 FESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSS 323
Cdd:cd17979    81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160
                         170
                  ....*....|
gi 552953797  324 YFSHAPVVQV 333
Cdd:cd17979   161 YFEGAPVVQV 170
DEXDc smart00487
DEAD-like helicases superfamily;
177-342 3.12e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.02  E-value: 3.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    177 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 245
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    246 STRSAATKIVFLTVGLLLRQIQREP-SLPQYQVLIVDEVHER--HLHNDFLLGVLQRLlpqRPDLKVILMSATI--NISL 320
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176
                           170       180
                    ....*....|....*....|..
gi 552953797    321 FSSYFSHAPVVQVPGRLFPITV 342
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
559-647 6.44e-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: 85.75  E-value: 6.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   559 AILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDC-------- 630
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 552953797   631 -------ATARRPLESDQGDPFTL 647
Cdd:pfam04408   81 rraadekARAKFARLDLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
800-911 4.53e-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: 4.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   800 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgqeasgqegsqdgrdqMSCKhqLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51
                           90       100       110
                   ....*....|....*....|....*....|..
gi 552953797   880 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
162-628 2.26e-164

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 508.08  E-value: 2.26e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  162 AALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQV 238
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAggrIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  239 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQ-RPDLKVILMSATIN 317
Cdd:COG1643    88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  318 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEADQtasksekldpRPFLR-----VLEAIDnkyppEERGDLLVFLSGMAE 392
Cdd:COG1643   168 AERFARLLGDAPVIESSGRTYPVEVRYRPLPADE----------RDLEDavadaVREALA-----EEPGDILVFLPGERE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  393 ITTVLDAAQAyaSLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQA 472
Cdd:COG1643   233 IRRTAEALRG--RLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  473 KLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPP 552
Cdd:COG1643   311 GVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPP 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552953797  553 PASVETAILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNL 628
Cdd:COG1643   391 ARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRGAAGSDL 466
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
118-698 2.50e-127

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: 421.48  E-value: 2.50e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   118 RGRHGPGR---GLPPERVSEFRRALLHYLDFQQKQAFGRLVKLQRERA------ALPIAQYGNRILQTLKEHQVVVVAGD 188
Cdd:TIGR01967   11 RDRHRLRRrlhKLRKDHDQDRAIAALAKFRERIDAACDKVEARRQAVPeirypdNLPVSAKREDIAEAIAENQVVIIAGE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   189 TGCGKSTQVPQYLLAAGF-SH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQ 265
Cdd:TIGR01967   91 TGSGKTTQLPKICLELGRgSHglIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   266 IQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQ 345
Cdd:TIGR01967  171 TQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYR 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   346 PQEADQTASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEITtvlDAAQAYASLTQRWV-VLPLHSALSVSDQ 424
Cdd:TIGR01967  251 PLVEEQEDDDLDQLEA-----ILDAVD-ELFAEGPGDILIFLPGEREIR---DAAEILRKRNLRHTeILPLYARLSNKEQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   425 DKVFDvaPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYR 504
Cdd:TIGR01967  322 QRVFQ--PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   505 LYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPASVETAILYLQEQGALDSSEA---LTPIGSL 581
Cdd:TIGR01967  400 LYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   582 LAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSER 661
Cdd:TIGR01967  480 LAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQAL 559
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 552953797   662 SGNS-RKWCRRRGVEEHRLYEMANLRRQFKELLEDHGL 698
Cdd:TIGR01967  560 SANQfRNACRKQYLNYLRVREWQDIYRQLTQVVKELGL 597
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
121-670 8.99e-123

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 409.06  E-value: 8.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  121 HGPGRGLPPERvsefRRALLHYLDFQQKQAFGRLvkLQRERA--------ALPIAQYGNRILQTLKEHQVVVVAGDTGCG 192
Cdd:PRK11131   28 HGAKKIKNPDA----QQAIFQEIAKEIAQAAQRV--LLREAArpeitypeNLPVSQKKQDILEAIRDHQVVIVAGETGSG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  193 KSTQVPQYLLAAG---FSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQRE 269
Cdd:PRK11131  102 KTTQLPKICLELGrgvKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  270 PSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQVPGRLFPITVVYQPQEA 349
Cdd:PRK11131  182 RLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  350 DQTASKSEKLDPrpflrVLEAIDnKYPPEERGDLLVFLSGMAEITtvlDAAQAYASLTQRWV-VLPLHSALSVSDQDKVF 428
Cdd:PRK11131  262 EADDTERDQLQA-----IFDAVD-ELGREGPGDILIFMSGEREIR---DTADALNKLNLRHTeILPLYARLSNSEQNRVF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  429 DvaPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAE 508
Cdd:PRK11131  333 Q--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSE 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  509 SDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPASVETAILYLQEQGALDSSEA-----LTPIGSLLA 583
Cdd:PRK11131  411 DDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLA 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  584 QLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDCATARRPLESDQGDPFTLFNVFNAWVQVKSERSG 663
Cdd:PRK11131  491 QLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLWNYLQEQQKALSS 570

                  ....*...
gi 552953797  664 NS-RKWCR 670
Cdd:PRK11131  571 NQfRRLCR 578
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
164-333 1.82e-108

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: 335.95  E-value: 1.82e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIR 243
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRHIACTQPRRIACISLAKRVAFESLNQYGSKVAYQIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  244 FESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSS 323
Cdd:cd17979    81 FERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIELFSG 160
                         170
                  ....*....|
gi 552953797  324 YFSHAPVVQV 333
Cdd:cd17979   161 YFEGAPVVQV 170
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
164-619 2.17e-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: 317.48  E-value: 2.17e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 241
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPGIGgkIIMLEPRRLAARSAAQRLASQLGEAVGQTVGYR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   242 IRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHND----FLLGVLQRLlpqRPDLKVILMSATIN 317
Cdd:TIGR01970   81 VRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADlglaLALDVQSSL---REDLKILAMSATLD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   318 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEADQtaskseKLDPRPFLRVLEAIdnkypPEERGDLLVFLSGMAEITTVl 397
Cdd:TIGR01970  158 GERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQ------RLEDAVSRAVEHAL-----ASETGSILVFLPGQAEIRRV- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   398 dAAQAYASLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRL 477
Cdd:TIGR01970  226 -QEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   478 QEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPASVE 557
Cdd:TIGR01970  305 ETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALA 384
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552953797   558 TAILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSP 619
Cdd:TIGR01970  385 AARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
164-635 1.70e-84

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 292.60  E-value: 1.70e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVP-QYLLAAGFS-HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQ 241
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINgKIIMLEPRRLAARNVAQRLAEQLGEKPGETVGYR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  242 IRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHND----FLLGVLQRLlpqRPDLKVILMSATIN 317
Cdd:PRK11664   84 MRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADlalaLLLDVQQGL---RDDLKLLIMSATLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  318 ISLFSSYFSHAPVVQVPGRLFPITVVYQPQEADQtaskseKLDP---RPFLRVLEaidnkyppEERGDLLVFLSGMAEIT 394
Cdd:PRK11664  161 NDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQ------RFDEavaRATAELLR--------QESGSLLLFLPGVGEIQ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  395 TVldAAQAYASLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKL 474
Cdd:PRK11664  227 RV--QEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  475 QRLQEFWISQASAEQRKGRAGRTGPGVCYRLYAESDYDAFAPYPVPEIRRVALDALVLQMKSMSVGDPRTFPFIEPPPPA 554
Cdd:PRK11664  305 TRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAA 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  555 SVETAILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAepVLTIAAALSV---QSPftRSAQSNLDCA 631
Cdd:PRK11664  385 ALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDDEA--ALATAAKLAAileEPP--RSGSSDLGVA 460

                  ....
gi 552953797  632 TARR 635
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) ...
180-333 4.64e-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: 255.85  E-value: 4.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  180 HQVVVVAGDTGCGKSTQVPQYLLAAGFS-----HVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKI 254
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkggkgRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552953797  255 VFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 333
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 ...
338-506 7.62e-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: 250.14  E-value: 7.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  338 FPITVVYQPQEADQTASKSEKLDPRPFLRVLEAIDNKYPPEERGDLLVFLSGMAEITTVLDAAQAYASL--TQRWVVLPL 415
Cdd:cd18791     1 FPVEVYYLEDILELLGISSEKEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSpdLGKLLVLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  416 HSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDSGKVKEMSYDPQAKLQRLQEFWISQASAEQRKGRAG 495
Cdd:cd18791    81 HSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAG 160
                         170
                  ....*....|.
gi 552953797  496 RTGPGVCYRLY 506
Cdd:cd18791   161 RTRPGKCYRLY 171
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
164-333 4.66e-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: 203.36  E-value: 4.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 240
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARggmIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  241 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVL-----QRLLPQRPDLKVILMSAT 315
Cdd:cd17978    81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVksaqrRRKEQKLSPLKVIIMSAT 160
                         170
                  ....*....|....*...
gi 552953797  316 INISLFSSYFSHAPVVQV 333
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 ...
164-333 7.68e-58

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: 197.58  E-value: 7.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH--------VACTQPRRIACISLAKRVGFEsLSQYG 235
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSpesdnpgmIGITQPRRVAAVSMAKRVAEE-LNVFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  236 SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPD--------- 306
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 552953797  307 -LKVILMSATINISLFSS---YFSHAP-VVQV 333
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 ...
153-333 1.09e-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: 194.17  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  153 RLVKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVG 227
Cdd:cd17973     2 RYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHqpkklVACTQPRRVAAMSVAQRVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  228 FESLSQYGSQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDL 307
Cdd:cd17973    82 EEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDL 161
                         170       180
                  ....*....|....*....|....*.
gi 552953797  308 KVILMSATINISLFSSYFSHAPVVQV 333
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 ...
164-333 2.79e-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: 192.75  E-value: 2.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGF----SHVA---CTQPRRIACISLAKRVGFESLSQYGS 236
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLqgppLPVAniiCTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  237 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATI 316
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 552953797  317 NISLFSSYFSHAPVVQV 333
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
164-333 2.55e-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: 2.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 239
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKgggkIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  240 YQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINIS 319
Cdd:cd17974    81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
                         170
                  ....*....|....
gi 552953797  320 LFSSYFSHAPVVQV 333
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 ...
164-333 3.62e-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: 187.04  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL--------AAGFSHVACTQPRRIACISLAKRVGFESLSQYG 235
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLedlllnggTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  236 -----SQVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVI 310
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                         170       180
                  ....*....|....*....|...
gi 552953797  311 LMSATINISLFSSYFSHAPVVQV 333
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
164-333 2.19e-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: 184.20  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 240
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIrglIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  241 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISL 320
Cdd:cd17989    81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
                         170
                  ....*....|...
gi 552953797  321 FSSYFSHAPVVQV 333
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 ...
160-334 2.88e-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: 184.22  E-value: 2.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  160 ERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGS 236
Cdd:cd17971     2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSrgkIGCTQPRRVAAMSVAKRVAEEFGCCLGQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  237 QVGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATI 316
Cdd:cd17971    82 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSATL 161
                         170
                  ....*....|....*...
gi 552953797  317 NISLFSSYFSHAPVVQVP 334
Cdd:cd17971   162 DAVKFSQYFYEAPIFTIP 179
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
164-325 3.13e-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: 184.21  E-value: 3.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRVGFESLSQYGSQVG 239
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAggrvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  240 YQIRFES-TRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINI 318
Cdd:cd17980    81 YCIRFDDcTDPQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160

                  ....*..
gi 552953797  319 SLFSSYF 325
Cdd:cd17980   161 EKFRDFF 167
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
122-333 5.35e-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: 5.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  122 GPGRGLPPERVSEfrrALLHYLDFQQKQAfGRLVKLQRERAALPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYL 201
Cdd:cd17972    21 GPLAFATPEQISM---DLKNELMYQREQD-HNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  202 L-------AAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFEST--RSAATkIVFLTVGLLLRQIqrEPSL 272
Cdd:cd17972    97 LddfiqndRAAECNIVVTQPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVlpRPHAS-ILFCTVGVLLRKL--EAGI 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552953797  273 PQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 333
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 ...
164-333 5.20e-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: 5.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-------AAGFSHVACTQPRRIACISLAKRVGFESLSQY-- 234
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiergKGSSCRIVCTQPRRISAISVAERVAAERAESCgl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  235 GSQVGYQIRFES--TRSAATkIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILM 312
Cdd:cd17981    81 GNSTGYQIRLESrkPRKQGS-ILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
                         170       180
                  ....*....|....*....|.
gi 552953797  313 SATINISLFSSYFSHAPVVQV 333
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 ...
164-330 2.08e-50

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: 175.73  E-value: 2.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 240
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDygmIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  241 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISL 320
Cdd:cd17983    81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
                         170
                  ....*....|
gi 552953797  321 FSSYFSHAPV 330
Cdd:cd17983   161 FADFFGNVPI 170
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
164-333 6.89e-47

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: 165.80  E-value: 6.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH---VACTQPRRIACISLAKRVGFESLSQYGSQVGY 240
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQhgmIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  241 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRP-----DLKVILMSAT 315
Cdd:cd17984    81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160
                         170
                  ....*....|....*...
gi 552953797  316 INISLFSSYFSHAPVVQV 333
Cdd:cd17984   161 LELAKLSAFFGNCPVFDI 178
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
164-333 1.50e-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: 1.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFS-------HVACTQPRRIACISLAKRVGFESLSQYGS 236
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLrgrgarcNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  237 QVGYQIRFES---TRSAAtkIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMS 313
Cdd:cd17976    81 NVGYQVRLESrppPRGGA--LLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMS 158
                         170       180
                  ....*....|....*....|
gi 552953797  314 ATINISLFSSYFSHAPVVQV 333
Cdd:cd17976   159 ATGDNQRLSRYFGGCPVVRV 178
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
164-333 3.01e-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: 161.15  E-value: 3.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH-----VACTQPRRIACISLAKRVGFESLSQYGSQV 238
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANgipcrIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  239 GYQIRFESTRSAATKIVFLTVGLLLRQIQ-REPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATIN 317
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
                         170
                  ....*....|....*.
gi 552953797  318 ISLFSSYFSHAPVVQV 333
Cdd:cd17987   161 VNLFIRYFGSCPVIYI 176
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
164-340 1.32e-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: 150.73  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLL-----AAGFSHVACTQPRRIACISLAKRVGFESLSQYGSQV 238
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILdhyykRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  239 GYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPD-LKVILMSATIN 317
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATIS 160
                         170       180
                  ....*....|....*....|...
gi 552953797  318 ISLFSSYFShapVVQVPGRLFPI 340
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 ...
164-331 2.34e-36

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: 135.54  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQYLLAA---GFSHVACTQPRRIACISLAKRVGFESLSQYGSQVGY 240
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAElwiAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  241 QIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVL---QRLLpqRPDLKVILMSATIN 317
Cdd:cd17990    81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLlevQQLL--RDDLRLLAMSATLD 158
                         170
                  ....*....|....
gi 552953797  318 ISLFSSYFSHAPVV 331
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 ...
164-333 4.94e-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: 4.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  164 LPIAQYGNRILQTLKEHQVVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQ 237
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHgvVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  238 VGYQIRFESTRSAATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATIN 317
Cdd:cd17977    81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
                         170
                  ....*....|....*.
gi 552953797  318 ISLFSSYFSHAPVVQV 333
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 ...
182-333 4.17e-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: 109.22  E-value: 4.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  182 VVVVAGDTGCGKSTQVPQ----YLLAAGFSH--VACTQPRRIACISLAKRVGFESLSQYGSQVGYQIRFESTRSAATKIV 255
Cdd:cd17986    20 IVLVSGEPGSGKSTQVPQwcaeFALSRGFQKgqVTVTQPHPLAARSLALRVADEMDLNLGHEVGYSIPQEDCTGPNTILR 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552953797  256 FLTVGLLLRQIQREPSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLPQRPDLKVILMSATINISLFSSYFSHAPVVQV 333
Cdd:cd17986   100 FCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPALEPKLRAFWGNPPVVHV 177
DEXDc smart00487
DEAD-like helicases superfamily;
177-342 3.12e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 96.02  E-value: 3.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    177 LKEHQVVVVAGDTGCGKSTQVPQYLLAAGFSH----VACTQPRRIACISLAKRV-------GFESLSQYGSQVgYQIRFE 245
Cdd:smart00487   21 LSGLRDVILAAPTGSGKTLAALLPALEALKRGkggrVLVLVPTRELAEQWAEELkklgpslGLKVVGLYGGDS-KREQLR 99
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    246 STRSAATKIVFLTVGLLLRQIQREP-SLPQYQVLIVDEVHER--HLHNDFLLGVLQRLlpqRPDLKVILMSATI--NISL 320
Cdd:smart00487  100 KLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLldGGFGDQLEKLLKLL---PKNVQLLLLSATPpeEIEN 176
                           170       180
                    ....*....|....*....|..
gi 552953797    321 FSSYFSHAPVVQVPGRLFPITV 342
Cdd:smart00487  177 LLELFLNDPVFIDVGFTPLEPI 198
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
165-506 2.22e-20

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 96.97  E-value: 2.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  165 PIAQygNRILQTLKEHQVVVVAGDTGCGKSTQVPQYL-----LAAGFSH------------VACTQPR----RIACISLA 223
Cdd:PHA02653  166 PDVQ--LKIFEAWISRKPVVLTGGTGVGKTSQVPKLLlwfnyLFGGFDNldkidpnfierpIVLSLPRvalvRLHSITLL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  224 KRVGFESLSqyGSQVgyQIRFES-------TRSAATKIVFLTVGLLLRqiqrepSLPQYQVLIVDEVHERHLHNDFLLGV 296
Cdd:PHA02653  244 KSLGFDEID--GSPI--SLKYGSipdelinTNPKPYGLVFSTHKLTLN------KLFDYGTVIIDEVHEHDQIGDIIIAV 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  297 LQRLLPQRPDLkvILMSATI-----NISLFssyFSHAPVVQVPG-RLFPITVVYQPQEADQTASKS----EKLDprpflr 366
Cdd:PHA02653  314 ARKHIDKIRSL--FLMTATLeddrdRIKEF---FPNPAFVHIPGgTLFPISEVYVKNKYNPKNKRAyieeEKKN------ 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  367 VLEAIdNKYPPEERGDLLVFLSGMAEITtvldaaqAYAS-LTQRwvvLPLHSALSVsdQDKVFDVAP------AGVRKCI 439
Cdd:PHA02653  383 IVTAL-KKYTPPKGSSGIVFVASVSQCE-------EYKKyLEKR---LPIYDFYII--HGKVPNIDEilekvySSKNPSI 449
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552953797  440 L-STNIAETSVTIDGIRFVVDSGKVkemsYDPQAKLQRlqEFWISQASAEQRKGRAGRTGPGVCYRLY 506
Cdd:PHA02653  450 IiSTPYLESSVTIRNATHVYDTGRV----YVPEPFGGK--EMFISKSMRTQRKGRVGRVSPGTYVYFY 511
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
559-647 6.44e-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: 85.75  E-value: 6.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   559 AILYLQEQGALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSNLDC-------- 630
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 552953797   631 -------ATARRPLESDQGDPFTL 647
Cdd:pfam04408   81 rraadekARAKFARLDLEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
567-647 1.45e-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: 84.24  E-value: 1.45e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    567 GALDSSEALTPIGSLLAQLPVDVVIGKMLILGSMFSLAEPVLTIAAALSVQSPFTRSAQSnlDCATARRPLESDQGDPFT 646
Cdd:smart00847    3 GALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKRE--DADAARRRFADPESDHLT 80

                    .
gi 552953797    647 L 647
Cdd:smart00847   81 L 81
HELICc smart00490
helicase superfamily c-terminal domain;
412-498 2.12e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 66.47  E-value: 2.12e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797    412 VLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRK 491
Cdd:smart00490   14 VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVII--------YDL----------PWSPASYIQRI 75

                    ....*..
gi 552953797    492 GRAGRTG 498
Cdd:smart00490   76 GRAGRAG 82
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
368-498 2.63e-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: 58.76  E-value: 2.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   368 LEAIDNKYPPEERGDLLVFLsgmaeiTTVLDAAQAYASLTQRWVVLPLHSALSVSDQDKVFDVAPAGVRKCILSTNIAET 447
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFS------QTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 552953797   448 SVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRKGRAGRTG 498
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 ...
183-315 3.54e-10

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: 59.34  E-value: 3.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  183 VVVAGDTGCGKSTQVP----QYLLAAGFShVACTQPRRIACISLAKRvgFESLSQYGSQVGYQIRFES--TRSAAT---- 252
Cdd:cd00046     4 VLITAPTGSGKTLAALlaalLLLLKKGKK-VLVLVPTKALALQTAER--LRELFGPGIRVAVLVGGSSaeEREKNKlgda 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552953797  253 KIVFLTVGLLLRQIQRE--PSLPQYQVLIVDEVHERHLHNDFLLGVLQRLLP-QRPDLKVILMSAT 315
Cdd:cd00046    81 DIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKaGLKNAQVILLSAT 146
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
800-911 4.53e-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: 4.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   800 LKLVLGRGLYPQLAVPDAfnsgrkDSDQIFHTQAKQGTVLHPTCVFANSPEvlhtqgqeasgqegsqdgrdqMSCKhqLL 879
Cdd:pfam07717    1 LRAALAAGLYPNVARRDP------KGKGYTTLSDNQRVFIHPSSVLFNEKT---------------------FPPE--WV 51
                           90       100       110
                   ....*....|....*....|....*....|..
gi 552953797   880 AFVSLLETNKPYLVNCVRIPALQsLLLFSRSI 911
Cdd:pfam07717   52 VYQELVETTKVYIRTVTAISPEW-LLLFAPHI 82
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
173-320 1.22e-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: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   173 ILQTLKEHQVVVVAgDTGCGKSTQvpqYLLAAgFSHVACTQPRRIACI-----SLAKRVgFESLSQYGSQVGYQIRFEST 247
Cdd:pfam00270    8 IPAILEGRDVLVQA-PTGSGKTLA---FLLPA-LEALDKLDNGPQALVlaptrELAEQI-YEELKKLGKGLGLKVASLLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797   248 RS---------AATKIVFLTVGLLLRQIQREPSLPQYQVLIVDEVHeRHLHNDF---LLGVLQRLLPQRpdlKVILMSAT 315
Cdd:pfam00270   82 GDsrkeqleklKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRLPKKR---QILLLSAT 157

                   ....*
gi 552953797   316 INISL 320
Cdd:pfam00270  158 LPRNL 162
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
182-316 1.08e-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: 41.59  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  182 VVVVAGDTGCGKSTQVPQ---YLLAAGFS-HVACTQPRRIAcislakrvGFESLSQYGSQVGYQIRFESTRSAATKIVFl 257
Cdd:cd03115     2 VILLVGLQGSGKTTTLAKlarYYQEKGKKvLLIAADTFRAA--------AVEQLKTLAEKLGVPVFESYTGTDPASIAQ- 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 552953797  258 tvglllrQIQREPSLPQYQVLIVDEVHeRHLHNDFLLGVLQRLLP-QRPDLKVILMSATI 316
Cdd:cd03115    73 -------EAVEKAKLEGYDVLLVDTAG-RLQKDEPLMEELKKVKEvESPDEVLLVLDATT 124
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
439-506 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 552953797  439 ILSTNIAETSVTIDGIRFVVDsgkvkemsYDPqaklqrlqefWISQASAEQRKGRAGRTG--PGVCYRLY 506
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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