NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|521031816|gb|EPQ13602|]
View 

ATP-dependent RNA helicase DHX8 [Myotis brandtii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
558-1162 2.96e-180

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: 557.77  E-value: 2.96e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  558 MSILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFG 637
Cdd:COG1643     1 MSLITYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  638 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQK-RQDMKLI 716
Cdd:COG1643    81 EPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  717 VTSATLDAVKFSQYFYEAPIFTIPGRTYPVEILYT--KEPETDYLDASLITVMQIhLTEPPGDILVFLTGQEEIDTACEI 794
Cdd:COG1643   161 VMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  795 LyerMKSLGPDVpelIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGID 874
Cdd:COG1643   240 L---RGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  875 QLVVTPISQAQAKQRAGRAGRTGPGKCYRLYTE-----RACRDEmlttnvPEIQRTNLASTVLSLKAMGINDLLSFDFMN 949
Cdd:COG1643   314 RLPTERISQASANQRAGRAGRLAPGICYRLWSEedfarRPAFTD------PEILRADLASLILELAAWGLGDPEDLPFLD 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  950 APPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRpkdkqal 1029
Cdd:COG1643   388 PPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRG------- 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1030 adqkkakfhQTEGDHLTLLAVYNSWKNNKfsnpwcyENFIQARSLHRAQDICKQMLGIMDRHKLDVVScgkSTVRVQKAI 1109
Cdd:COG1643   461 ---------AAGSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLL 521
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 521031816 1110 CSGFFQNAAKKDPQEG-YRtLIDHQVVYIHPSSALFNRqpEWVVYHELVLTTKE 1162
Cdd:COG1643   522 ALAYPDRIARRRGEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAE 572
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
267-345 1.88e-43

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


:

Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 152.39  E-value: 1.88e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLRKRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMKDVDQETG 345
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
GH2-like_DHX8 cd21691
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ...
25-92 6.56e-40

GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. This model corresponds to the GH2-like domain that shows high sequence similarity with the GH2 domain found in GIPC (GAIP C-terminus-interacting protein) family of proteins, which mediate endocytosis by tethering cargo proteins to the motor myosin VI.


:

Pssm-ID: 409668  Cd Length: 68  Bit Score: 141.91  E-value: 6.56e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816   25 LEYLSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKTSLVKNGAEFTDSLISNLLRLIQTM 92
Cdd:cd21691     1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKENGAEFPDSFVESLLRLIQRM 68
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
1197-1279 1.37e-33

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: 124.30  E-value: 1.37e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   1197 LGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNvfYRPKDKQALADQKKAKFHQTEGDHL 1276
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 521031816   1277 TLL 1279
Cdd:smart00847   80 TLL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1336-1412 2.24e-29

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: 112.35  E-value: 2.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1336 VQKAICSGFFRNAAKKDPQE-GYRTLIDQQVVYIHPSSALFN---RQPEWVVYHELVLTTKEYMREVTTIDPRWLVEFAP 1411
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNektFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                   .
gi 521031816  1412 A 1412
Cdd:pfam07717   81 H 81
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
558-1162 2.96e-180

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 557.77  E-value: 2.96e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  558 MSILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFG 637
Cdd:COG1643     1 MSLITYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  638 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQK-RQDMKLI 716
Cdd:COG1643    81 EPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  717 VTSATLDAVKFSQYFYEAPIFTIPGRTYPVEILYT--KEPETDYLDASLITVMQIhLTEPPGDILVFLTGQEEIDTACEI 794
Cdd:COG1643   161 VMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  795 LyerMKSLGPDVpelIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGID 874
Cdd:COG1643   240 L---RGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  875 QLVVTPISQAQAKQRAGRAGRTGPGKCYRLYTE-----RACRDEmlttnvPEIQRTNLASTVLSLKAMGINDLLSFDFMN 949
Cdd:COG1643   314 RLPTERISQASANQRAGRAGRLAPGICYRLWSEedfarRPAFTD------PEILRADLASLILELAAWGLGDPEDLPFLD 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  950 APPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRpkdkqal 1029
Cdd:COG1643   388 PPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRG------- 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1030 adqkkakfhQTEGDHLTLLAVYNSWKNNKfsnpwcyENFIQARSLHRAQDICKQMLGIMDRHKLDVVScgkSTVRVQKAI 1109
Cdd:COG1643   461 ---------AAGSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLL 521
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 521031816 1110 CSGFFQNAAKKDPQEG-YRtLIDHQVVYIHPSSALFNRqpEWVVYHELVLTTKE 1162
Cdd:COG1643   522 ALAYPDRIARRRGEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAE 572
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
565-1170 4.37e-148

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: 485.04  E-value: 4.37e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   565 ESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   645 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDA 724
Cdd:TIGR01967  144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   725 VKFSQYFYEAPIFTIPGRTYPVEILY------TKEPETDYLDASLITVMQIhLTEPPGDILVFLTGQEEIDTACEILYER 798
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEAILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   799 mkslgpDVPELIILPVYSALPSEMQTRIFDPAppGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVV 878
Cdd:TIGR01967  303 ------NLRHTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPI 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   879 TPISQAQAKQRAGRAGRTGPGKCYRLYTERACRDEMLTTNvPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPMETLIT 958
Cdd:TIGR01967  375 EPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRD 453
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   959 AMEQLYTLGALDDE---GLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQALADQKKA 1035
Cdd:TIGR01967  454 GFRLLEELGALDDDeaePQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHA 533
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1036 KFHQTEGDHLTLLAVYNSWKN-------NKFSNpWCYENFIQARSLHRAQDICKQMLGIMDRHKLDVVSCGKSTVRVQKA 1108
Cdd:TIGR01967  534 RFKDPRSDFLSRVNLWRHIEEqrqalsaNQFRN-ACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKA 612
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521031816  1109 ICSGFFQNAAKKDPQEGYrTLIDHQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREAMGI 1170
Cdd:TIGR01967  613 LLSGLLSQIGMKDEKHEY-DGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKI 673
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
565-1170 1.85e-140

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 464.53  E-value: 1.85e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  565 ESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:PRK11131   71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  645 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDA 724
Cdd:PRK11131  151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  725 VKFSQYFYEAPIFTIPGRTYPVEILY------TKEPETDYLDASLITVMQIHlTEPPGDILVFLTGQEEI-DTAcEILYE 797
Cdd:PRK11131  231 ERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGEREIrDTA-DALNK 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  798 RmkslgpDVPELIILPVYSALPSEMQTRIFDPAppGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLV 877
Cdd:PRK11131  309 L------NLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLP 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  878 VTPISQAQAKQRAGRAGRTGPGKCYRLYTEracrDEMLT----TNvPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPM 953
Cdd:PRK11131  381 IEPISQASANQRKGRCGRVSEGICIRLYSE----DDFLSrpefTD-PEILRTNLASVILQMTALGLGDIAAFPFVEAPDK 455
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  954 ETLITAMEQLYTLGALDDEG-----LLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQA 1028
Cdd:PRK11131  456 RNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQ 535
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1029 LADQKKAKFHQTEGDHLTLLAVYNSWK-------NNKFSNpWCYENFIQARSLHRAQDICKQMLGIMDRHKLDVVSCGKS 1101
Cdd:PRK11131  536 ASDEKHRRFADKESDFLAFVNLWNYLQeqqkalsSNQFRR-LCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAE 614
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816 1102 TVRVQKAICSGFFQNAAKKDPQEGYRTLIDHQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREAMGI 1170
Cdd:PRK11131  615 YREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARI 683
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
562-740 2.71e-126

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: 389.15  E-value: 2.71e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  562 EQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLG 641
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  642 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSAT 721
Cdd:cd17971    81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
                         170
                  ....*....|....*....
gi 521031816  722 LDAVKFSQYFYEAPIFTIP 740
Cdd:cd17971   161 LDAVKFSQYFYEAPIFTIP 179
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
267-345 1.88e-43

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 152.39  E-value: 1.88e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLRKRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMKDVDQETG 345
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
GH2-like_DHX8 cd21691
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ...
25-92 6.56e-40

GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. This model corresponds to the GH2-like domain that shows high sequence similarity with the GH2 domain found in GIPC (GAIP C-terminus-interacting protein) family of proteins, which mediate endocytosis by tethering cargo proteins to the motor myosin VI.


Pssm-ID: 409668  Cd Length: 68  Bit Score: 141.91  E-value: 6.56e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816   25 LEYLSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKTSLVKNGAEFTDSLISNLLRLIQTM 92
Cdd:cd21691     1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKENGAEFPDSFVESLLRLIQRM 68
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
966-1048 1.37e-33

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: 124.30  E-value: 1.37e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816    966 LGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNvfYRPKDKQALADQKKAKFHQTEGDHL 1045
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 521031816   1046 TLL 1048
Cdd:smart00847   80 TLL 82
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
1197-1279 1.37e-33

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: 124.30  E-value: 1.37e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   1197 LGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNvfYRPKDKQALADQKKAKFHQTEGDHL 1276
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 521031816   1277 TLL 1279
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1190-1278 1.89e-31

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: 119.26  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1190 AMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRP------KDKQALADQ 1263
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprSAAKAARRR 80
                           90       100
                   ....*....|....*....|....
gi 521031816  1264 KKAKFHQ---------TEGDHLTL 1278
Cdd:pfam04408   81 RRAADEKarakfarldLEGDHLTL 104
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
959-1047 1.89e-31

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: 119.26  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   959 AMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRP------KDKQALADQ 1032
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprSAAKAARRR 80
                           90       100
                   ....*....|....*....|....
gi 521031816  1033 KKAKFHQ---------TEGDHLTL 1047
Cdd:pfam04408   81 RRAADEKarakfarldLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1336-1412 2.24e-29

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: 112.35  E-value: 2.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1336 VQKAICSGFFRNAAKKDPQE-GYRTLIDQQVVYIHPSSALFN---RQPEWVVYHELVLTTKEYMREVTTIDPRWLVEFAP 1411
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNektFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                   .
gi 521031816  1412 A 1412
Cdd:pfam07717   81 H 81
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
263-341 1.14e-21

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 101.66  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  263 EPAIGDIYNGKVTSIMQFGCFVQLegLRKRwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFT-GTKTSLSMKDVD 341
Cdd:PRK11824  618 EPEVGEIYEGKVVRIVDFGAFVEI--LPGK-DGLVHISEIADE-RVEKVEDVLKEGDEVKVKVLEIDkRGRIRLSRKAVL 693
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
262-355 1.65e-20

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 88.70  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELrREGRVANVADVVSKGQRVKVKVLSFTGT-KTSLSMKDV 340
Cdd:COG1098     1 MSIEVGDIVEGKVTGITPFGAFVELPE---GTTGLVHISEI-ADGYVKDINDYLKVGDEVKVKVLSIDEDgKISLSIKQA 76
                          90
                  ....*....|....*
gi 521031816  341 DQETGEDLNPNRRRN 355
Cdd:COG1098    77 EEKPKRPPRPRRNSR 91
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
266-354 2.72e-19

CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator.


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 84.79  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEglrKRWEGLVHISELrREGRVANVADVVSKGQRVKVKVLS---FTGtKTSLSMKDVDQ 342
Cdd:NF040579    3 IGDIVEGKVTGIQPYGAFVALD---EHTQGLIHISEI-KHGYVKDINDFLKVGQEVKVKVLDideYTG-KISLSLRALEE 77
                          90
                  ....*....|..
gi 521031816  343 ETGEDLNPNRRR 354
Cdd:NF040579   78 APEKHRKRRKHR 89
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
266-338 1.42e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 69.94  E-value: 1.42e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521031816    266 IGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFTGTK--TSLSMK 338
Cdd:smart00316    2 VGDVVEGTVTEITPGGAFVDLGN---GVEGLIPISELSDK-RVKDPEEVLKVGDEVKVKVLSVDEEKgrIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
264-326 4.17e-11

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 59.99  E-value: 4.17e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816   264 PAIGDIYNGKVTSIMQFGCFVQLEGLRkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVL 326
Cdd:pfam00575    1 PEKGDVVEGEVTRVTKGGAFVDLGNGV---EGFIPISELSDD-HVEDPDEVIKVGDEVKVKVL 59
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
254-338 3.20e-09

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 61.29  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   254 KHVDRPPPEEPA----IGDIYNGKVTSIMQFGCFVQL-EGLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSF 328
Cdd:TIGR00717  256 KQLGEDPWEAIEkkfpVGDKITGRVTNLTDYGVFVEIeEGI----EGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILDI 331
                           90
                   ....*....|..
gi 521031816   329 --TGTKTSLSMK 338
Cdd:TIGR00717  332 dpERRRLSLGLK 343
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
1169-1227 7.45e-06

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 50.69  E-value: 7.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816 1169 GINDLLSFDFMDAPPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLI 1227
Cdd:PRK11664  368 GCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLV 426
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
558-1162 2.96e-180

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 557.77  E-value: 2.96e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  558 MSILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFG 637
Cdd:COG1643     1 MSLITYPPDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  638 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQK-RQDMKLI 716
Cdd:COG1643    81 EPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  717 VTSATLDAVKFSQYFYEAPIFTIPGRTYPVEILYT--KEPETDYLDASLITVMQIhLTEPPGDILVFLTGQEEIDTACEI 794
Cdd:COG1643   161 VMSATLDAERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  795 LyerMKSLGPDVpelIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGID 874
Cdd:COG1643   240 L---RGRLPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  875 QLVVTPISQAQAKQRAGRAGRTGPGKCYRLYTE-----RACRDEmlttnvPEIQRTNLASTVLSLKAMGINDLLSFDFMN 949
Cdd:COG1643   314 RLPTERISQASANQRAGRAGRLAPGICYRLWSEedfarRPAFTD------PEILRADLASLILELAAWGLGDPEDLPFLD 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  950 APPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRpkdkqal 1029
Cdd:COG1643   388 PPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPRRG------- 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1030 adqkkakfhQTEGDHLTLLAVYNSWKNNKfsnpwcyENFIQARSLHRAQDICKQMLGIMDRHKLDVVScgkSTVRVQKAI 1109
Cdd:COG1643   461 ---------AAGSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLL 521
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 521031816 1110 CSGFFQNAAKKDPQEG-YRtLIDHQVVYIHPSSALFNRqpEWVVYHELVLTTKE 1162
Cdd:COG1643   522 ALAYPDRIARRRGEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAE 572
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
565-1170 4.37e-148

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: 485.04  E-value: 4.37e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   565 ESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:TIGR01967   64 DNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKV 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   645 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDA 724
Cdd:TIGR01967  144 GYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDP 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   725 VKFSQYFYEAPIFTIPGRTYPVEILY------TKEPETDYLDASLITVMQIhLTEPPGDILVFLTGQEEIDTACEILYER 798
Cdd:TIGR01967  224 ERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEAILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   799 mkslgpDVPELIILPVYSALPSEMQTRIFDPAppGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVV 878
Cdd:TIGR01967  303 ------NLRHTEILPLYARLSNKEQQRVFQPH--SGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPI 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   879 TPISQAQAKQRAGRAGRTGPGKCYRLYTERACRDEMLTTNvPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPMETLIT 958
Cdd:TIGR01967  375 EPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRD 453
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   959 AMEQLYTLGALDDE---GLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQALADQKKA 1035
Cdd:TIGR01967  454 GFRLLEELGALDDDeaePQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHA 533
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1036 KFHQTEGDHLTLLAVYNSWKN-------NKFSNpWCYENFIQARSLHRAQDICKQMLGIMDRHKLDVVSCGKSTVRVQKA 1108
Cdd:TIGR01967  534 RFKDPRSDFLSRVNLWRHIEEqrqalsaNQFRN-ACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKA 612
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521031816  1109 ICSGFFQNAAKKDPQEGYrTLIDHQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREAMGI 1170
Cdd:TIGR01967  613 LLSGLLSQIGMKDEKHEY-DGARGRKFHIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKI 673
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
565-1170 1.85e-140

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 464.53  E-value: 1.85e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  565 ESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:PRK11131   71 ENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIAEELETELGGCV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  645 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDA 724
Cdd:PRK11131  151 GYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  725 VKFSQYFYEAPIFTIPGRTYPVEILY------TKEPETDYLDASLITVMQIHlTEPPGDILVFLTGQEEI-DTAcEILYE 797
Cdd:PRK11131  231 ERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGEREIrDTA-DALNK 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  798 RmkslgpDVPELIILPVYSALPSEMQTRIFDPAppGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLV 877
Cdd:PRK11131  309 L------NLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLP 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  878 VTPISQAQAKQRAGRAGRTGPGKCYRLYTEracrDEMLT----TNvPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPM 953
Cdd:PRK11131  381 IEPISQASANQRKGRCGRVSEGICIRLYSE----DDFLSrpefTD-PEILRTNLASVILQMTALGLGDIAAFPFVEAPDK 455
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  954 ETLITAMEQLYTLGALDDEG-----LLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRPKDKQA 1028
Cdd:PRK11131  456 RNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQ 535
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1029 LADQKKAKFHQTEGDHLTLLAVYNSWK-------NNKFSNpWCYENFIQARSLHRAQDICKQMLGIMDRHKLDVVSCGKS 1101
Cdd:PRK11131  536 ASDEKHRRFADKESDFLAFVNLWNYLQeqqkalsSNQFRR-LCRTDYLNYLRVREWQDIYTQLRQVVKELGIPVNSEPAE 614
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816 1102 TVRVQKAICSGFFQNAAKKDPQEGYRTLIDHQVVYIHPSSALFNRQPEWVVYHELVLTTKEYMREAMGI 1170
Cdd:PRK11131  615 YREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARI 683
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
562-740 2.71e-126

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: 389.15  E-value: 2.71e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  562 EQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLG 641
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  642 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSAT 721
Cdd:cd17971    81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
                         170
                  ....*....|....*....
gi 521031816  722 LDAVKFSQYFYEAPIFTIP 740
Cdd:cd17971   161 LDAVKFSQYFYEAPIFTIP 179
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
567-1014 1.35e-102

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: 347.52  E-value: 1.35e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQIT-QYLAEAGYTsrGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVG 645
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGIG--GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   646 YTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKtVQK--RQDMKLIVTSATLD 723
Cdd:TIGR01970   79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALD-VQSslREDLKILAMSATLD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   724 AVKFSQYFYEAPIFTIPGRTYPVEILYTKEPETDYLDASLITVMQIHLTEPPGDILVFLTGQEEIDTACEILYERmksLG 803
Cdd:TIGR01970  158 GERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAER---LD 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   804 PDVpelIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVVTPISQ 883
Cdd:TIGR01970  235 SDV---LICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   884 AQAKQRAGRAGRTGPGKCYRLYTErACRDEMLTTNVPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPMETLITAMEQL 963
Cdd:TIGR01970  312 ASATQRAGRAGRLEPGVCYRLWSE-EQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLL 390
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 521031816   964 YTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSML 1014
Cdd:TIGR01970  391 QRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALL 441
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
567-739 4.77e-94

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: 300.53  E-value: 4.77e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVK 726
Cdd:cd17983    81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
                         170
                  ....*....|...
gi 521031816  727 FSQYFYEAPIFTI 739
Cdd:cd17983   161 FADFFGNVPIFTI 173
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
566-996 9.71e-93

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 319.18  E-value: 9.71e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  566 SLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQIT-QYLAEAGYTsrGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:PRK11664    3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGIN--GKIIMLEPRRLAARNVAQRLAEQLGEKPGETV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  645 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKtVQK--RQDMKLIVTSATL 722
Cdd:PRK11664   81 GYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLD-VQQglRDDLKLLIMSATL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  723 DAVKFSQYFYEAPIFTIPGRTYPVEILYTKEPETDYLDASLITVMQIHLTEPPGDILVFLTGQEEIDTACEILYERmksL 802
Cdd:PRK11664  160 DNDRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLASR---V 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  803 GPDVpelIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVVTPIS 882
Cdd:PRK11664  237 ASDV---LLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRIS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  883 QAQAKQRAGRAGRTGPGKCYRLYT-ERACRdeMLTTNVPEIQRTNLASTVLSLKAMGINDLLSFDFMNAPPMETLITAME 961
Cdd:PRK11664  314 QASMTQRAGRAGRLEPGICLHLYSkEQAER--AAAQSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKR 391
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 521031816  962 QLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLI 996
Cdd:PRK11664  392 LLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLV 426
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
567-739 4.80e-89

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: 286.32  E-value: 4.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRG-KIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVG 645
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGgKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  646 YTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAV 725
Cdd:cd17974    81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
                         170
                  ....*....|....
gi 521031816  726 KFSQYFYEAPIFTI 739
Cdd:cd17974   161 KFSAFFDDAPIFRI 174
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
583-739 2.59e-87

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


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 280.89  E-value: 2.59e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  583 NQILIVIGETGSGKTTQITQYLAEAGYTS--RGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGYTIRFEDCTSPETVI 660
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKggKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816  661 KYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVKFSQYFYEAPIFTI 739
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 ...
744-905 2.80e-86

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: 278.26  E-value: 2.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  744 YPVEILYTKEP-----------ETDYLDASLITVMQIHLTEPPGDILVFLTGQEEIDTACEILYERMKSlgPDVPELIIL 812
Cdd:cd18791     1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLS--PDLGKLLVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  813 PVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFVKQKVYNSKTGIDQLVVTPISQAQAKQRAGR 892
Cdd:cd18791    79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
                         170
                  ....*....|...
gi 521031816  893 AGRTGPGKCYRLY 905
Cdd:cd18791   159 AGRTRPGKCYRLY 171
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
567-739 3.72e-86

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: 278.47  E-value: 3.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKtVQKR------QDMKLIVTSA 720
Cdd:cd17978    81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKS-AQRRrkeqklSPLKVIIMSA 159
                         170
                  ....*....|....*....
gi 521031816  721 TLDAVKFSQYFYEAPIFTI 739
Cdd:cd17978   160 TLDADLFSEYFNGAPVLYI 178
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
560-739 4.62e-83

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: 270.06  E-value: 4.62e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  560 ILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGK--IGCTQPRRVAAMSVAKRVSEEFG 637
Cdd:cd17973     6 ILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKklVACTQPRRVAAMSVAQRVAEEMD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  638 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIV 717
Cdd:cd17973    86 VKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIV 165
                         170       180
                  ....*....|....*....|..
gi 521031816  718 TSATLDAVKFSQYFYEAPIFTI 739
Cdd:cd17973   166 MSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
567-731 6.61e-76

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: 249.69  E-value: 6.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGK-IGCTQPRRVAAMSVAKRVSEEFGCCLGQEVG 645
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  646 YTIRFEDCTSP-ETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDA 724
Cdd:cd17980    81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160

                  ....*..
gi 521031816  725 VKFSQYF 731
Cdd:cd17980   161 EKFRDFF 167
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
567-739 1.50e-75

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: 248.23  E-value: 1.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQ-----DMKLIVTSAT 721
Cdd:cd17984    81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpnrkeHLKVVVMSAT 160
                         170
                  ....*....|....*...
gi 521031816  722 LDAVKFSQYFYEAPIFTI 739
Cdd:cd17984   161 LELAKLSAFFGNCPVFDI 178
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
567-736 1.14e-60

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: 205.38  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVK 726
Cdd:cd17989    81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
                         170
                  ....*....|
gi 521031816  727 FSQYFYEAPI 736
Cdd:cd17989   161 FSRHFNNAPI 170
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
567-729 3.62e-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: 199.12  E-value: 3.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSR-----GKIGCTQPRRVAAMSVAKRVSEEFGCcLG 641
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  642 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDM-------- 713
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKLylqdqtvk 159
                         170
                  ....*....|....*...
gi 521031816  714 --KLIVTSATLDAVKFSQ 729
Cdd:cd17982   160 plKLVIMSATLRVEDFTE 177
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
567-736 2.09e-54

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: 187.26  E-value: 2.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSrgkIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLDAVK 726
Cdd:cd17979    78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
                         170
                  ....*....|
gi 521031816  727 FSQYFYEAPI 736
Cdd:cd17979   158 FSGYFEGAPV 167
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
567-739 8.25e-48

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: 168.87  E-value: 8.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEaGYTSRGK-----IGCTQPRRVAAMSVAKRVSEEFG--CC 639
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILD-DAIERGKgsscrIVCTQPRRISAISVAERVAAERAesCG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  640 LGQEVGYTIRFEDCTSPETV-IKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVT 718
Cdd:cd17981    80 LGNSTGYQIRLESRKPRKQGsILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILM 159
                         170       180
                  ....*....|....*....|.
gi 521031816  719 SATLDAVKFSQYFYEAPIFTI 739
Cdd:cd17981   160 SATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
567-739 8.53e-47

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: 166.24  E-value: 8.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAE-----AGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLG 641
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  642 -----QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLI 716
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                         170       180
                  ....*....|....*....|...
gi 521031816  717 VTSATLDAVKFSQYFYEAPIFTI 739
Cdd:cd17975   161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
567-739 3.25e-46

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: 164.23  E-value: 3.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRG--KIGCTQPRRVAAMSVAKRVSEEFGCCLGQEV 644
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIpcRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  645 GYTIRFEDCTSPETVIKYMTDGMLLRECLI-DPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLD 723
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
                         170
                  ....*....|....*.
gi 521031816  724 AVKFSQYFYEAPIFTI 739
Cdd:cd17987   161 VNLFIRYFGSCPVIYI 176
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
267-345 1.88e-43

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 152.39  E-value: 1.88e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLRKRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMKDVDQETG 345
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
560-739 5.96e-43

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: 156.92  E-value: 5.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  560 ILEQRESLPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAE----AGYTSRGKIGCTQPRRVAAMSVAKRVSEE 635
Cdd:cd17972    52 ILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdfiqNDRAAECNIVVTQPRRISAVSVAERVAFE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  636 FGCCLGQEVGYTIRFEDCT-SPETVIKYMTDGMLLREclIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMK 714
Cdd:cd17972   132 RGEEVGKSCGYSVRFESVLpRPHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLR 209
                         170       180
                  ....*....|....*....|....*
gi 521031816  715 LIVTSATLDAVKFSQYFYEAPIFTI 739
Cdd:cd17972   210 VILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
567-736 4.48e-42

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: 152.29  E-value: 4.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAE---AGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQE 643
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  644 VGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATLD 723
Cdd:cd17977    81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
                         170
                  ....*....|...
gi 521031816  724 AVKFSQYFYEAPI 736
Cdd:cd17977   161 SSKLLSYYGNVPL 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
567-737 7.20e-42

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


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 151.72  E-value: 7.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQEVGY 646
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  647 TIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQ-KRQDMKLIVTSATLDAV 725
Cdd:cd17990    81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDGD 160
                         170
                  ....*....|..
gi 521031816  726 KFSQYFYEAPIF 737
Cdd:cd17990   161 GLAALLPEAPVV 172
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
567-739 4.53e-41

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: 149.61  E-value: 4.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEA----GYTSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQ 642
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqgPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  643 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSATL 722
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                         170
                  ....*....|....*..
gi 521031816  723 DAVKFSQYFYEAPIFTI 739
Cdd:cd17985   161 NAELFSDYFNSCPVIHI 177
GH2-like_DHX8 cd21691
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ...
25-92 6.56e-40

GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. This model corresponds to the GH2-like domain that shows high sequence similarity with the GH2 domain found in GIPC (GAIP C-terminus-interacting protein) family of proteins, which mediate endocytosis by tethering cargo proteins to the motor myosin VI.


Pssm-ID: 409668  Cd Length: 68  Bit Score: 141.91  E-value: 6.56e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816   25 LEYLSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKTSLVKNGAEFTDSLISNLLRLIQTM 92
Cdd:cd21691     1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKENGAEFPDSFVESLLRLIQRM 68
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
567-739 9.98e-40

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: 145.72  E-value: 9.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAgYTSRGK---IGCTQPRRVAAMSVAKRVSEEFGCCLGQE 643
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDH-YYKRGKycnIVVTQPRRIAAISIARRVSQEREWTLGSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  644 VGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQ-KRQDMKLIVTSATL 722
Cdd:cd17988    80 VGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRtNSRHVKIILMSATI 159
                         170       180
                  ....*....|....*....|.
gi 521031816  723 DAVKFSQYF----YEAPIFTI 739
Cdd:cd17988   160 SCKEFADYFttpnNPAYVFEV 180
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
567-739 3.48e-39

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: 143.88  E-value: 3.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQ-ILIVIGETGSGKTTQITQYLAEAGYT---SRGKIGCTQPRRVAAMSVAKRVSEEFGCCLGQ 642
Cdd:cd17986     1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSrgfQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  643 EVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKL-IVTSAT 721
Cdd:cd17986    81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVvVVTSPA 160
                         170
                  ....*....|....*...
gi 521031816  722 LDAvKFSQYFYEAPIFTI 739
Cdd:cd17986   161 LEP-KLRAFWGNPPVVHV 177
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
567-736 4.58e-37

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: 138.00  E-value: 4.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  567 LPIYKLKEQLVQAVHDNQILIVIGETGSGKTTQITQYLAEAGYTSRGKIGC----TQPRRVAAMSVAKRVSEEFGCCLGQ 642
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCnvviTQPRRISAVSVAQRVAHELGPNLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  643 EVGYTIRFEDCTSPET-VIKYMTDGMLLRECLIDPDLTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIVTSAT 721
Cdd:cd17976    81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
                         170
                  ....*....|....*
gi 521031816  722 LDAVKFSQYFYEAPI 736
Cdd:cd17976   161 GDNQRLSRYFGGCPV 175
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
966-1048 1.37e-33

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: 124.30  E-value: 1.37e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816    966 LGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNvfYRPKDKQALADQKKAKFHQTEGDHL 1045
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 521031816   1046 TLL 1048
Cdd:smart00847   80 TLL 82
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
1197-1279 1.37e-33

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: 124.30  E-value: 1.37e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   1197 LGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNvfYRPKDKQALADQKKAKFHQTEGDHL 1276
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 521031816   1277 TLL 1279
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
1190-1278 1.89e-31

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: 119.26  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1190 AMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRP------KDKQALADQ 1263
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprSAAKAARRR 80
                           90       100
                   ....*....|....*....|....
gi 521031816  1264 KKAKFHQ---------TEGDHLTL 1278
Cdd:pfam04408   81 RRAADEKarakfarldLEGDHLTL 104
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
959-1047 1.89e-31

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: 119.26  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   959 AMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLSVQNVFYRP------KDKQALADQ 1032
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprSAAKAARRR 80
                           90       100
                   ....*....|....*....|....
gi 521031816  1033 KKAKFHQ---------TEGDHLTL 1047
Cdd:pfam04408   81 RRAADEKarakfarldLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1336-1412 2.24e-29

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: 112.35  E-value: 2.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  1336 VQKAICSGFFRNAAKKDPQE-GYRTLIDQQVVYIHPSSALFN---RQPEWVVYHELVLTTKEYMREVTTIDPRWLVEFAP 1411
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNektFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                   .
gi 521031816  1412 A 1412
Cdd:pfam07717   81 H 81
DEXDc smart00487
DEAD-like helicases superfamily;
563-748 4.99e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.89  E-value: 4.99e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816    563 QRESLPIyklkeqlvqAVHDNQILIVIGETGSGKTTQITQYLAEAGY-TSRGKIGCTQPRRVAAMSVAKRVSEEFGCCLG 641
Cdd:smart00487   13 QKEAIEA---------LLSGLRDVILAAPTGSGKTLAALLPALEALKrGKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816    642 QEVGYT------IRFEDCTSPETVIKYMTDGMLLRECLIDP-DLTQYAIIMLDEAHERT--IHTDVLFGLLKKTVQKRQd 712
Cdd:smart00487   84 KVVGLYggdskrEQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLKLLPKNVQ- 162
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 521031816    713 mkLIVTSATL--DAVKFSQYFYEAPIFTIPGRTYPVEI 748
Cdd:smart00487  163 --LLLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
GH2_like cd21690
GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) ...
28-89 2.26e-23

GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) family of proteins mediate endocytosis by tethering cargo proteins to the motor myosin VI. This model represents the C-terminal GIPC homology 2 or GH2 domain (plus the linker to the PDZ domain located N-terminally of GH2), which mediates the interaction with myosin VI and is involved in homodimerization in the autoinhibited state. The family also includes DEAH box protein 8 (DHX8) and similar proteins. DHX8 (a human homolog of yeast Prp22), also called RNA helicase HRH1, is an ATP-dependent RNA helicase involved in pre-mRNA splicing as a component of the spliceosome. It facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 contains a GH2-like domain at the N-terminus, which shows high sequence similarity with the GH2 domain found in GIPC proteins.


Pssm-ID: 409667  Cd Length: 62  Bit Score: 94.46  E-value: 2.26e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521031816   28 LSLVSKVCTELDNHLGINDKDLAEFVISLAEKNTTFDTFKTSLVKNGAEFTDSLISNLLRLI 89
Cdd:cd21690     1 LSAIEKVDDLLKNYLGIDDPELAEFVISLAKKKKNPDEFAEALDENDAAFPDEFVFDLYRAI 62
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
1167-1420 5.74e-23

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 106.32  E-value: 5.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1167 AMGINDLLSFDFMDAPPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLIMSVHLGCSEEMLTIVSMLS 1246
Cdd:COG1643   374 AWGLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLS 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1247 VQNVFYRpkdkqaladqkkakfhQTEGDHLTLLAVYNSWKNNKfsnpwcyENFIQARSLRRAQDIRKQMLGIMDRHKLDV 1326
Cdd:COG1643   454 ERDPRRG----------------AAGSDLLARLNLWRRLREQQ-------REFLSYLRLREWRDLARQLRRLLGEGANEE 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816 1327 VScgkSTVRVQKAICSGFFRNAAKKDPQEG-YRtLIDQQVVYIHPSSALFNRqpEWVVYHELVLTTKEY-MREVTTIDPR 1404
Cdd:COG1643   511 PA---DYEAIGLLLALAYPDRIARRRGEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAEArIRLAAPIDPE 584
                         250
                  ....*....|....*..
gi 521031816 1405 WLVEFAPAFFK-VSDPT 1420
Cdd:COG1643   585 WLEELAAHLIKrYSEPH 601
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
263-341 1.14e-21

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 101.66  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  263 EPAIGDIYNGKVTSIMQFGCFVQLegLRKRwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFT-GTKTSLSMKDVD 341
Cdd:PRK11824  618 EPEVGEIYEGKVVRIVDFGAFVEI--LPGK-DGLVHISEIADE-RVEKVEDVLKEGDEVKVKVLEIDkRGRIRLSRKAVL 693
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1105-1176 3.53e-21

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: 88.85  E-value: 3.53e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816  1105 VQKAICSGFFQNAAKKDPQE-GYRTLIDHQVVYIHPSSALFN---RQPEWVVYHELVLTTKEYMREAMGIND--LLSF 1176
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNektFPPEWVVYQELVETTKVYIRTVTAISPewLLLF 78
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
267-337 7.88e-21

S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo.


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 87.60  E-value: 7.88e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLRkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSF-TGTKTSLSM 337
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGK---DGLVHISELSDE-RVEKVEDVLKVGDEVKVKVIEVdDRGRISLSR 68
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
262-355 1.65e-20

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 88.70  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELrREGRVANVADVVSKGQRVKVKVLSFTGT-KTSLSMKDV 340
Cdd:COG1098     1 MSIEVGDIVEGKVTGITPFGAFVELPE---GTTGLVHISEI-ADGYVKDINDYLKVGDEVKVKVLSIDEDgKISLSIKQA 76
                          90
                  ....*....|....*
gi 521031816  341 DQETGEDLNPNRRRN 355
Cdd:COG1098    77 EEKPKRPPRPRRNSR 91
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
266-354 2.72e-19

CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator.


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 84.79  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEglrKRWEGLVHISELrREGRVANVADVVSKGQRVKVKVLS---FTGtKTSLSMKDVDQ 342
Cdd:NF040579    3 IGDIVEGKVTGIQPYGAFVALD---EHTQGLIHISEI-KHGYVKDINDFLKVGQEVKVKVLDideYTG-KISLSLRALEE 77
                          90
                  ....*....|..
gi 521031816  343 ETGEDLNPNRRR 354
Cdd:NF040579   78 APEKHRKRRKHR 89
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
262-340 8.02e-19

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 89.72  E-value: 8.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMK 338
Cdd:COG0539   270 EKYPVGDVVKGKVTRLTDFGAFVELEpGV----EGLVHISEMSWTKRVAHPSDVVKVGDEVEVKVLDIdpEERRISLSIK 345

                  ..
gi 521031816  339 DV 340
Cdd:COG0539   346 QL 347
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
266-339 5.57e-17

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 84.33  E-value: 5.57e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMKD 339
Cdd:COG0539   189 EGDVVEGTVKNITDFGAFVDLGGV----DGLLHISEISW-GRVKHPSEVLKVGDEVEVKVLKIdrEKERISLSLKQ 259
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
261-346 1.04e-16

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 85.77  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  261 PEEPAIGDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELrREGRVANVADVVSKGQRVKVKVLSFTGT--KTSLSM 337
Cdd:PRK00087  557 EEKYPVGSIVLGKVVRIAPFGAFVELEpGV----DGLVHISQI-SWKRIDKPEDVLSEGEEVKAKILEVDPEekRIRLSI 631

                  ....*....
gi 521031816  338 KDVDQETGE 346
Cdd:PRK00087  632 KEVEEEPGD 640
rpsA PRK06676
30S ribosomal protein S1; Reviewed
262-366 2.29e-15

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 79.92  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQL-EGLrkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMK 338
Cdd:PRK06676  273 EKLPEGDVIEGTVKRLTDFGAFVEVlPGV----EGLVHISQISHK-HIATPSEVLEEGQEVKVKVLEVneEEKRISLSIK 347
                          90       100
                  ....*....|....*....|....*...
gi 521031816  339 DVDQETGEDLNPNRRRNLVGETNEETSM 366
Cdd:PRK06676  348 ALEEAPAEEEDRREEYRQYELPEEETGF 375
rpsA PRK06676
30S ribosomal protein S1; Reviewed
267-340 2.50e-15

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 79.92  E-value: 2.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSF---TGtKTSLSMKDV 340
Cdd:PRK06676  193 GDVVEGTVARLTDFGAFVDIGGV----DGLVHISELSHE-RVEKPSEVVSVGQEVEVKVLSIdweTE-RISLSLKDT 263
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
267-338 5.44e-15

S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (hs4) of the H. sapiens RPS1 homolog. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 70.78  E-value: 5.44e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521031816  267 GDIYNGKVTSIMQFGCFVQL-EGLrkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFTGT-KTSLSMK 338
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELgGGI----SGLVHISQIAHK-RVKDVKDVLKEGDKVKVKVLSIDARgRISLSIK 69
HELICc smart00490
helicase superfamily c-terminal domain;
793-897 1.11e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 70.32  E-value: 1.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816    793 EILYERMKSLGpdvpeLIILPVYSALPSEMQTRIFDPAPPGSRKVVIATNIAETSLTIDGIYYVVDPGFvkqkvynsktg 872
Cdd:smart00490    1 EELAELLKELG-----IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------- 64
                            90       100
                    ....*....|....*....|....*
gi 521031816    873 idqlvvtPISQAQAKQRAGRAGRTG 897
Cdd:smart00490   65 -------PWSPASYIQRIGRAGRAG 82
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
266-338 1.42e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 69.94  E-value: 1.42e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521031816    266 IGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFTGTK--TSLSMK 338
Cdd:smart00316    2 VGDVVEGTVTEITPGGAFVDLGN---GVEGLIPISELSDK-RVKDPEEVLKVGDEVKVKVLSVDEEKgrIILSLK 72
PRK08059 PRK08059
general stress protein 13; Validated
266-369 8.60e-14

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 69.31  E-value: 8.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELrREGRVANVADVVSKGQRVKVKVLSF---TGtKTSLSMKdvdq 342
Cdd:PRK08059    7 VGSVVTGKVTGIQPYGAFVALDE---ETQGLVHISEI-THGFVKDIHDFLSVGDEVKVKVLSVdeeKG-KISLSIR---- 77
                          90       100
                  ....*....|....*....|....*..
gi 521031816  343 ETGEDLNPNRRRNLVGETNEETSMRNP 369
Cdd:PRK08059   78 ATEEAPEAKRKKGKILIPNPSEQGFNT 104
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
266-338 2.00e-13

S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 3 (ec3) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 66.50  E-value: 2.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSFTGTKTSLSMK 338
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGV----DGLLHISDMSW-GRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
763-897 1.21e-12

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: 65.69  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   763 LITVMQIHLTEPPGDILVFLTGQEEIDtaCEILYERMKslgpdvpeLIILPVYSALPSEMQTRIFDPAPPGSRKVVIATN 842
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG--------IKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 521031816   843 IAETSLTIDGIYYVVDpgfvkqkvYNSKTGIDQLVvtpisqaqakQRAGRAGRTG 897
Cdd:pfam00271   73 VAERGLDLPDVDLVIN--------YDLPWNPASYI----------QRIGRAGRAG 109
PRK08582 PRK08582
RNA-binding protein S1;
272-363 3.31e-12

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 65.44  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  272 GKVTSIMQFGCFVQLEGLRKrweGLVHISELrREGRVANVADVVSKGQRVKVKVLSFTGT-KTSLSM-KDVDQETGEDLN 349
Cdd:PRK08582   11 GKVTGITNFGAFVELPEGKT---GLVHISEV-ADNYVKDINDHLKVGDEVEVKVLNVEDDgKIGLSIkKAKDRPKRQHDR 86
                          90
                  ....*....|....
gi 521031816  350 PNRRRNLVGETNEE 363
Cdd:PRK08582   87 PRHEDNRGGGNDVA 100
rpsA PRK06299
30S ribosomal protein S1; Reviewed
266-338 4.02e-12

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 70.58  E-value: 4.02e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLS--FTGTKTSLSMK 338
Cdd:PRK06299  286 VGSKVKGKVTNITDYGAFVELEeGI----EGLVHVSEMSWTKKNKHPSKVVSVGQEVEVMVLEidEEKRRISLGLK 357
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
270-337 1.13e-11

S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 61.24  E-value: 1.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816  270 YNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFTGTKTSLSM 337
Cdd:cd00164     1 VTGKVVSITKFGVFVELED---GVEGLVHISELSDK-FVKDPSEVFKVGDEVEVKVLEVDPEKGRISL 64
rpsA PRK13806
30S ribosomal protein S1; Provisional
267-350 1.30e-11

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 68.98  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSF------TGTKTSLSMKD 339
Cdd:PRK13806  203 GDVVEGTVTRLAPFGAFVELApGV----EGMVHISELSW-SRVQKADEAVSVGDTVRVKVLGIerakkgKGLRISLSIKQ 277
                          90
                  ....*....|....*
gi 521031816  340 VD----QETGEDLNP 350
Cdd:PRK13806  278 AGgdpwDTVGDRLKA 292
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
267-340 1.45e-11

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 69.21  E-value: 1.45e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMKDV 340
Cdd:PRK00087  478 GDVVEGEVKRLTDFGAFVDIGGV----DGLLHVSEISW-GRVEKPSDVLKVGDEIKVYILDIdkENKKLSLSLKKL 548
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
264-326 4.17e-11

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 59.99  E-value: 4.17e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816   264 PAIGDIYNGKVTSIMQFGCFVQLEGLRkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVL 326
Cdd:pfam00575    1 PEKGDVVEGEVTRVTKGGAFVDLGNGV---EGFIPISELSDD-HVEDPDEVIKVGDEVKVKVL 59
PRK05807 PRK05807
RNA-binding protein S1;
267-338 4.04e-10

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 59.37  E-value: 4.04e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELrREGRVANVADVVSKGQRVKVKVLSF-TGTKTSLSMK 338
Cdd:PRK05807    6 GSILEGTVVNITNFGAFVEVEGK----TGLVHISEV-ADTYVKDIREHLKEQDKVKVKVISIdDNGKISLSIK 73
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
266-343 4.14e-10

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 58.94  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGLRKrweGLVHISELrREGRVANVADVVSKGQRVKVKVL---SFTGtKTSLSMKDVDQ 342
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTT---GLIHISEI-KTGFIDNIHQLLKVGEEVLVQVVdfdEYTG-KASLSLRTLEE 77

                  .
gi 521031816  343 E 343
Cdd:PRK07252   78 E 78
rpsA PRK07899
30S ribosomal protein S1; Reviewed
265-350 8.53e-10

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 63.14  E-value: 8.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  265 AIGDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELrREGRVANVADVVSKGQRVKVKV--LSFTGTKTSLSMKDVD 341
Cdd:PRK07899  292 AIGQIVPGKVTKLVPFGAFVRVEeGI----EGLVHISEL-AERHVEVPEQVVQVGDEVFVKVidIDLERRRISLSLKQAN 366
                          90
                  ....*....|..
gi 521031816  342 Q---ETGEDLNP 350
Cdd:PRK07899  367 EgvtPESEDFDP 378
rpsA PRK06299
30S ribosomal protein S1; Reviewed
267-338 1.21e-09

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 62.87  E-value: 1.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSFTGTKT--SLSMK 338
Cdd:PRK06299  202 GQVVEGVVKNITDYGAFVDLGGV----DGLLHITDISW-KRVNHPSEVVNVGDEVKVKVLKFDKEKKrvSLGLK 270
rpsA PRK13806
30S ribosomal protein S1; Provisional
267-339 1.48e-09

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 62.05  E-value: 1.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTK--TSLSMKD 339
Cdd:PRK13806  293 GDKVTGKVVRLAPFGAFVEILpGI----EGLVHVSEMSWTRRVNKPEDVVAPGDAVAVKIKDIDPAKrrISLSLRD 364
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
261-343 2.04e-09

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 60.22  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  261 PEEpaiGDIYNGKVTSIMQFGCFVQLE---GLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSFTGTKTS--L 335
Cdd:PRK03987    6 PEE---GELVVGTVKEVKDFGAFVTLDeypGK----EGFIHISEVAS-GWVKNIRDHVKEGQKVVCKVIRVDPRKGHidL 77

                  ....*....
gi 521031816  336 SMKDV-DQE 343
Cdd:PRK03987   78 SLKRVnEHQ 86
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
267-327 2.70e-09

S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has been characterized in Bordetella pertussis and Pseudomonas aeruginosa. The tex gene is essential in Bortella pertusis and is named for its role in toxin expression. Tex has two functional domains, an N-terminal domain homologous to the Escherichia coli maltose repression protein, which is a poorly defined transcriptional factor, and a C-terminal S1 RNA-binding domain. Tex is found in prokaryotes, eukaryotes, and archaea.


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 54.55  E-value: 2.70e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLeGLRKrwEGLVHISELRrEGRVANVADVVSKGQRVKVKVLS 327
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDI-GVKQ--DGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVIS 57
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
254-338 3.20e-09

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 61.29  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   254 KHVDRPPPEEPA----IGDIYNGKVTSIMQFGCFVQL-EGLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSF 328
Cdd:TIGR00717  256 KQLGEDPWEAIEkkfpVGDKITGRVTNLTDYGVFVEIeEGI----EGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILDI 331
                           90
                   ....*....|..
gi 521031816   329 --TGTKTSLSMK 338
Cdd:TIGR00717  332 dpERRRLSLGLK 343
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
266-346 3.43e-09

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 61.58  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFV-----QleglrkrwEGLVHISELRrEGRVANVADVVSKGQRVKVKVLSFTGTK--TSLSMK 338
Cdd:COG2183   641 PGMILEGTVTNVTDFGAFVdigvhQ--------DGLVHISQLS-DRFVKDPREVVKVGDIVKVKVLEVDLKRkrISLSMK 711

                  ....*...
gi 521031816  339 DVDQETGE 346
Cdd:COG2183   712 LDDEAGAA 719
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
264-326 6.18e-09

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 54.13  E-value: 6.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816  264 PAIGDIYNGKVTSIMQFGCFVQLEGLRKRwEGLVHISELRReGRVANVADVVSKGQRVKVKVL 326
Cdd:cd04452     1 PEEGELVVVTVKSIADMGAYVSLLEYGNI-EGMILLSELSR-RRIRSIRKLVKVGRKEVVKVI 61
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
266-346 8.73e-09

S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, which is a homolog of RNase II. RNase R degrades RNA with secondary structure having a 3' overhang of at least 7 nucleotides. RNase R and PNPase play an important role in the degradation of RNA with extensive secondary structure, such as rRNA, tRNA, and certain mRNA which contains repetitive extragenic palindromic sequences. The C-terminal S1 domain binds ssRNA.


Pssm-ID: 239917 [Multi-domain]  Cd Length: 83  Bit Score: 53.56  E-value: 8.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGLRKrwEGLVHISEL----------------RREGRVANVadvvskGQRVKVKVlsft 329
Cdd:cd04471     1 VGEEFDGVISGVTSFGLFVELDNLTV--EGLVHVSTLgddyyefdeenhalvgERTGKVFRL------GDKVKVRV---- 68
                          90
                  ....*....|....*..
gi 521031816  330 gtktslsmKDVDQETGE 346
Cdd:cd04471    69 --------VRVDLDRRK 77
rpsA PRK06299
30S ribosomal protein S1; Reviewed
266-338 1.84e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 59.02  E-value: 1.84e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMK 338
Cdd:PRK06299  373 VGDVVEGKVKNITDFGAFVGLEgGI----DGLVHLSDISWDKKGEEAVELYKKGDEVEAVVLKVdvEKERISLGIK 444
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
266-348 2.26e-08

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 58.59  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   266 IGDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRReGRVANVADVVSKGQRVKVKVLSFTGTKT--SLSMKDVDQE 343
Cdd:TIGR00717  187 EGDVVKGVVKNITDFGAFVDLGGV----DGLLHITDMSW-KRVKHPSEYVKVGQEVKVKVIKFDKEKGriSLSLKQLGED 261

                   ....*
gi 521031816   344 TGEDL 348
Cdd:TIGR00717  262 PWEAI 266
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
265-338 2.80e-08

S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 52.33  E-value: 2.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  265 AIGDIYNGKVTSIMQFGCFVQLEGlrKRWEGLVHISELRrEGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMK 338
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIDG--TNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIdaEKKRISLGLK 73
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
264-395 5.66e-08

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 57.60  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  264 PAIGDIY-NGKVTSIMQFGCFVQLEGLRkrwEGLVHISELrREGRVANVADVVSKGQRVKVKVLSFT-GTKTSLSMKDVD 341
Cdd:PLN00207  751 PTVGDIYrNCEIKSIAPYGAFVEIAPGR---EGLCHISEL-SSNWLAKPEDAFKVGDRIDVKLIEVNdKGQLRLSRRALL 826
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816  342 QETGEDLNPNRRRNlvGETNEETSMRN----PDRPTHLSLVSAPEVEDDSLERKRLTR 395
Cdd:PLN00207  827 PEANSEKSSQKQQG--GSTKDKAPQKKyvntSSRPRRAAQAEKNSAENAAVPKKKDYK 882
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
267-337 6.33e-08

S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 5 (ec5) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 50.96  E-value: 6.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSM 337
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDG---GIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
rpsA PRK06299
30S ribosomal protein S1; Reviewed
265-343 2.46e-07

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 55.17  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  265 AIGDIYNGKVTSIMQFGCFVQLEGLRkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFtGTKT---SLSMKDVD 341
Cdd:PRK06299  459 KKGSIVTGTVTEVKDKGAFVELEDGV---EGLIRASELSRD-RVEDATEVLKVGDEVEAKVINI-DRKNrriSLSIKALD 533

                  ..
gi 521031816  342 QE 343
Cdd:PRK06299  534 EA 535
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
678-906 4.03e-07

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 54.60  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  678 LTQYAIIMLDEAHERTIHTDVLFGLLKKTVQKRQDMKLIvtSATL-DAVKFSQYFYEAPIFT-IPGRT-YPVEILYTK-- 752
Cdd:PHA02653  289 LFDYGTVIIDEVHEHDQIGDIIIAVARKHIDKIRSLFLM--TATLeDDRDRIKEFFPNPAFVhIPGGTlFPISEVYVKnk 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  753 ----------EPETDYLDASLITvmqihLTEPPG-DILVFLTGQEEIDTACEILYERMkslgpdvPELIILPVYSALPS- 820
Cdd:PHA02653  367 ynpknkrayiEEEKKNIVTALKK-----YTPPKGsSGIVFVASVSQCEEYKKYLEKRL-------PIYDFYIIHGKVPNi 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  821 -EMQTRIFDPAPPgsrKVVIATNIAETSLTIDGIYYVVDPGfvkqKVYNSKT-GIDQLVvtpISQAQAKQRAGRAGRTGP 898
Cdd:PHA02653  435 dEILEKVYSSKNP---SIIISTPYLESSVTIRNATHVYDTG----RVYVPEPfGGKEMF---ISKSMRTQRKGRVGRVSP 504

                  ....*...
gi 521031816  899 GKCYRLYT 906
Cdd:PHA02653  505 GTYVYFYD 512
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
272-337 1.02e-06

S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (ec4) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 47.57  E-value: 1.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521031816  272 GKVTSIMQFGCFVQLE-GLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSFTGTKTSLSM 337
Cdd:cd05689     9 GKVTNLTDYGCFVELEeGV----EGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISL 71
VacB COG0557
Exoribonuclease R [Transcription];
266-327 2.57e-06

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 52.03  E-value: 2.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521031816  266 IGDIYNGKVTSIMQFGCFVQLEGLRKrwEGLVHISEL----------------RREGRVANVadvvskGQRVKVKVLS 327
Cdd:COG0557   622 VGEEFEGVISGVTSFGLFVELDELGV--EGLVHVSSLgddyyeyderrqalvgERTGKRYRL------GDRVEVRVVR 691
rpsA PRK07899
30S ribosomal protein S1; Reviewed
267-347 2.85e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 51.58  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  267 GDIYNGKVTSIMQFGCFVQLEGLrkrwEGLVHISELRREgRVANVADVVSKGQRVKVKVLS--FTGTKTSLSMKdvdqET 344
Cdd:PRK07899  209 GQVRKGVVSSIVNFGAFVDLGGV----DGLVHVSELSWK-HIDHPSEVVEVGQEVTVEVLDvdMDRERVSLSLK----AT 279

                  ...
gi 521031816  345 GED 347
Cdd:PRK07899  280 QED 282
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
1169-1227 7.45e-06

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 50.69  E-value: 7.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816 1169 GINDLLSFDFMDAPPMETLITAMEQLYTLGALDDEGLLTRLGRRMAEFPLEPMLCKMLI 1227
Cdd:PRK11664  368 GCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLV 426
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
586-721 1.04e-05

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: 47.01  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  586 LIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGccLGQEVGYTIRFedcTSPETV------ 659
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGG---SSAEEReknklg 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521031816  660 ---IKYMTDGMLLRECLID--PDLTQYAIIMLDEAHERTIHTDVLFgLLKKTVQKRQ--DMKLIVTSAT 721
Cdd:cd00046    79 dadIIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGAL-ILDLAVRKAGlkNAQVILLSAT 146
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
592-690 1.88e-05

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 46.39  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  592 TGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSeefgcclGQEVGY-TIRFEDCTSPETVIKYMTDGMLLR 670
Cdd:cd17931    10 PGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYrTGAVKEEHGGNEIVDYMCHGTFTC 82
                          90       100
                  ....*....|....*....|
gi 521031816  671 ECLIDPDLTQYAIIMLDEAH 690
Cdd:cd17931    83 RLLSPKRVPNYNLIIMDEAH 102
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
267-338 2.51e-05

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 48.58  E-value: 2.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521031816   267 GDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMK 338
Cdd:TIGR00717  447 GSVVKGKVTEIKDFGAFVELPG---GVEGLIRNSELSEN-RDEDKTDEIKVGDEVEAKVVDIdkKNRKVSLSVK 516
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
265-348 1.43e-04

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 46.63  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  265 AIGDIYNGKVTSIMQFGCFVQL-EGLrkrwEGLVHISELRREGRVANVADVVSKGQRVKVKVLSF--TGTKTSLSMKDVD 341
Cdd:PRK12269  577 GVNDVVKGRVTKIADFGAFIELaEGI----EGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYdiQAGRVSLGLKQVT 652

                  ....*..
gi 521031816  342 QETGEDL 348
Cdd:PRK12269  653 ANPWEEI 659
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
262-332 2.28e-04

S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay.


Pssm-ID: 239900 [Multi-domain]  Cd Length: 88  Bit Score: 41.43  E-value: 2.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521031816  262 EEPAIGDIYNGKVTSI---MQfGCFVQLeGLRKrwEGLVHISELRR--EGRVANVADVVSKGQRVKVKVL-SFTGTK 332
Cdd:cd04453     3 REPIVGNIYLGRVKKIvpgLQ-AAFVDI-GLGK--NGFLHLSDILPayFKKHKKIAKLLKEGQEILVQVVkEPIGTK 75
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
836-905 2.64e-04

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: 40.77  E-value: 2.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521031816  836 KVVIATNIAETSLTIDGIYYVVDPGFvkqkvynsktgidqlvvtPISQAQAKQRAGRAGRTG--PGKCYRLY 905
Cdd:cd18785    24 EILVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
rpsA PRK06676
30S ribosomal protein S1; Reviewed
262-343 1.29e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 42.94  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQLEGlrKRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLSFTGTKTS--LSMKD 339
Cdd:PRK06676   13 KEVEVGDVVTGEVLKVEDKQVFVNIEG--YKVEGVIPISELSND-HIEDINDVVKVGDELEVYVLKVEDGEGNllLSKRR 89

                  ....
gi 521031816  340 VDQE 343
Cdd:PRK06676   90 LEAE 93
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
266-338 2.00e-03

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 42.41  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521031816   266 IGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELR--REGRVANVadVVSKGQRVKVKVLS--FTGTKTSLSMK 338
Cdd:TIGR00717  359 VGDRVTGKIKKITDFGAFVELEG---GIDGLIHLSDISwdKDGREADH--LYKKGDEIEAVVLAvdKEKKRISLGVK 430
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
585-905 2.54e-03

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 42.03  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  585 ILIVIGETGSGKTTQITQYLAEAGYTS-RGKIGCTQPRRVAAMSVAKRVSEEFG-CCLGQEVGYTIRFEDCTSPETVIK- 661
Cdd:cd09639     1 LLVIEAPTGYGKTEAALLWALHSLKSQkADRVIIALPTRATINAMYRRAKEAFGeTGLYHSSILSSRIKEMGDSEEFEHl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  662 ---YMTDGML-----LRECLIDP------------DLTQ----YAIIMLDEAHERTIHTDVLF-GLLKktVQKRQDMKLI 716
Cdd:cd09639    81 fplYIHSNDTlfldpITVCTIDQvlksvfgefghyEFTLasiaNSLLIFDEVHFYDEYTLALIlAVLE--VLKDNDVPIL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  717 VTSATLDAVkFSQYF--YEAPIFTIPGRTYPVEILYT-KEPETDYLDASLITVMqIHLTEPPGDILVFLTgqeEIDTACE 793
Cdd:cd09639   159 LMSATLPKF-LKEYAekIGYVEENEPLDLKPNERAPFiKIESDKVGEISSLERL-LEFIKKGGSVAIIVN---TVDRAQE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816  794 IlYERMKSLGPDVPELII----LPVYSALPSEMQTRIFDPAPPGsrkVVIATNIAETSLTIDGIYYVVDPgfvkqkvyns 869
Cdd:cd09639   234 F-YQQLKEKGPEEEIMLIhsrfTEKDRAKKEAELLLEFKKSEKF---VIVATQVIEASLDISVDVMITEL---------- 299
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 521031816  870 kTGIDQLVvtpisqaqakQRAGRAGRTGPGKCYRLY 905
Cdd:cd09639   300 -APIDSLI----------QRLGRLHRYGEKNGEEVY 324
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
262-327 2.90e-03

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in S. cerevisiae Rrp5 and 14 S1 repeats in H. sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 37.95  E-value: 2.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521031816  262 EEPAIGDIYNGKVTSIMQFGCFVQLEGlrkRWEGLVHISELRREgRVANVADVVSKGQRVKVKVLS 327
Cdd:cd04461    10 SDLKPGMVVHGYVRNITPYGVFVEFLG---GLTGLAPKSYISDE-FVTDPSFGFKKGQSVTAKVTS 71
AAA_22 pfam13401
AAA domain;
584-690 3.23e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521031816   584 QILIVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVSEEFGcclgqevgytIRFEDCTSPETVIKYM 663
Cdd:pfam13401    6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALG----------LPLSGRLSKEELLAAL 75
                           90       100
                   ....*....|....*....|....*..
gi 521031816   664 TDgmLLRECLIDPdltqyaIIMLDEAH 690
Cdd:pfam13401   76 QQ--LLLALAVAV------VLIIDEAQ 94
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
267-328 7.64e-03

S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 6 (hs6) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 36.43  E-value: 7.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521031816  267 GDIYNGKVTSIMQFGCFVQ-LEGLRkrweGLVHISELrREGRVANVADVVSKGQRVKVKVLSF 328
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSfYNNVK----GFLPKSEL-SEAFIKDPEEHFRVGQVVKVKVLSC 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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