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Conserved domains on  [gi|17535281|ref|NP_495019|]
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putative pre-mRNA-splicing factor ATP-dependent RNA helicase mog-5 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
538-1157 0e+00

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: 588.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  538 ESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDV 617
Cdd:COG1643    8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  618 GYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLK-AAARKRPELKLIITSATLD 696
Cdd:COG1643   88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLdLQPALRPDLKLLVMSATLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  697 SVKFSEYFLEAPIFTIPGRTFPVEILYT--REPESDYLEAAHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLyerMKS 774
Cdd:COG1643  168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEAL---RGR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  775 MGPDVpelIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPI 854
Cdd:COG1643  244 LPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  855 SQAAAKQRSGRAGRTGPGKCYRLYTERAFRdEMLPTPVPEIQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALN 934
Cdd:COG1643  321 SQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  935 TLHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNifyrPKEKQDHADqkkakfhqpe 1014
Cdd:COG1643  400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSD---------- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281 1015 gdhltLLAVYNSWKNHHFSQPwcfeNFIQVRSMKRAQDIRKQLLGIMDRHKLLMVScgrDVSRVQKAICSGFFRNAAKRD 1094
Cdd:COG1643  466 -----LLARLNLWRRLREQQR----EFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLLALAYPDRIARRR 533
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281 1095 PQEG-YRtLTDGQNVYIHPSSACFQQqpEWVVYHELVMTTKEY-MREVTAIDPKWLVEFAPSFFK 1157
Cdd:COG1643  534 GEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAEArIRLAAPIDPEWLEELAAHLIK 595
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
234-311 1.01e-38

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: 138.53  E-value: 1.01e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGFRQKQEGLVHISQIRNE-RVQTVADVLKRGENVKVKVNKIENGKISLSMKEVDQNSG 311
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; ...
4-73 2.69e-28

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: 108.40  E-value: 2.69e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    4 LEHLSLVSKVLSEVENHFGVVEKDVAEFVIHLAQENPTFDKLKKALDSqgLGDQFDDSLTATILRIVQSM 73
Cdd:cd21691    1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKE--NGAEFPDSFVESLLRLIQRM 68
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
538-1157 0e+00

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 588.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  538 ESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDV 617
Cdd:COG1643    8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  618 GYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLK-AAARKRPELKLIITSATLD 696
Cdd:COG1643   88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLdLQPALRPDLKLLVMSATLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  697 SVKFSEYFLEAPIFTIPGRTFPVEILYT--REPESDYLEAAHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLyerMKS 774
Cdd:COG1643  168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEAL---RGR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  775 MGPDVpelIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPI 854
Cdd:COG1643  244 LPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  855 SQAAAKQRSGRAGRTGPGKCYRLYTERAFRdEMLPTPVPEIQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALN 934
Cdd:COG1643  321 SQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  935 TLHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNifyrPKEKQDHADqkkakfhqpe 1014
Cdd:COG1643  400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSD---------- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281 1015 gdhltLLAVYNSWKNHHFSQPwcfeNFIQVRSMKRAQDIRKQLLGIMDRHKLLMVScgrDVSRVQKAICSGFFRNAAKRD 1094
Cdd:COG1643  466 -----LLARLNLWRRLREQQR----EFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLLALAYPDRIARRR 533
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281 1095 PQEG-YRtLTDGQNVYIHPSSACFQQqpEWVVYHELVMTTKEY-MREVTAIDPKWLVEFAPSFFK 1157
Cdd:COG1643  534 GEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAEArIRLAAPIDPEWLEELAAHLIK 595
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
501-1157 9.61e-160

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: 510.47  E-value: 9.61e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    501 KDRNNKMKEMPEWLKHVTAGGKATYGRRTNLSMVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEA 580
Cdd:TIGR01967   27 HDQDRAIAALAKFRERIDAACDKVEARRQAVPEIRYPDNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    581 GLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLD 660
Cdd:TIGR01967  107 GRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIID 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    661 EAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVKFSEYFLEAPIFTIPGRTFPVEILY------TREPESDYLEA 734
Cdd:TIGR01967  187 EAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    735 AHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLYERmksmgpDVPELIILPVYGALPSEMQTRIFDpaPAGKRKVVIAT 814
Cdd:TIGR01967  267 ILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR------NLRHTEILPLYARLSNKEQQRVFQ--PHSGRRIVLAT 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    815 NIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPISQAAAKQRSGRAGRTGPGKCYRLYTERAFRDEMLPTPvPE 894
Cdd:TIGR01967  338 NVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PE 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    895 IQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALNTLHTLSALD---GDGLLTKLGRRMAEFPLEPSLSKLLIMS 971
Cdd:TIGR01967  417 ILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDddeAEPQLTPIGRQLAQLPVDPRLARMLLEA 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    972 VDLGCSEEVLTIVAMLNVQNIFYRPKEKQDHADQKKAKFHQPEGDHLTLLavyNSWKnhHFSQP-----------WCFEN 1040
Cdd:TIGR01967  497 HRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRV---NLWR--HIEEQrqalsanqfrnACRKQ 571
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   1041 FIQVRSMKRAQDIRKQLLGIMDRHKLLMVSCGRDVSRVQKAICSGFFRNAAKRDPQEGYrTLTDGQNVYIHPSSACFQQQ 1120
Cdd:TIGR01967  572 YLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEY-DGARGRKFHIFPGSPLFKKP 650
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 17535281   1121 PEWVVYHELVMTTKEYMREVTAIDPKWLVEFAPSFFK 1157
Cdd:TIGR01967  651 PKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK 687
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
527-1157 7.46e-144

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 468.00  E-value: 7.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   527 RRTNLSMVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVA 606
Cdd:PRK11131   60 REAARPEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   607 EEYGCKLGTDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPEL 686
Cdd:PRK11131  140 EELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDL 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   687 KLIITSATLDSVKFSEYFLEAPIFTIPGRTFPVEILY------TREPESDYLEAAHITVMQIHlTEPPGDVLVFLTGQEE 760
Cdd:PRK11131  220 KVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGERE 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   761 IDTSCEVLYERmksmgpDVPELIILPVYGALPSEMQTRIFDpaPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIY 840
Cdd:PRK11131  299 IRDTADALNKL------NLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRY 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   841 NPKSGMDSLVVTPISQAAAKQRSGRAGRTGPGKCYRLYTERAF--RDEMLPtpvPEIQRTNLASTLLQLKAMGINNLIDF 918
Cdd:PRK11131  371 SYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFlsRPEFTD---PEILRTNLASVILQMTALGLGDIAAF 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   919 DFMDAPPLDSMITALNTLHTLSALDGDG-----LLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNIF 993
Cdd:PRK11131  448 PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPR 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   994 YRPKEKQDHADQKKAKFHQPEGDHLTLLAVYN----SWKNHHFSQ--PWC---FENFIQVRSMkraQDIRKQLLGIMDRH 1064
Cdd:PRK11131  528 ERPMDKQQASDEKHRRFADKESDFLAFVNLWNylqeQQKALSSNQfrRLCrtdYLNYLRVREW---QDIYTQLRQVVKEL 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  1065 KLLMVSCGRDVSRVQKAICSGFFRNAAKRDPQEGYRTLTDGQNVYIHPSSACFQQQPEWVVYHELVMTTKEYMREVTAID 1144
Cdd:PRK11131  605 GIPVNSEPAEYREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIE 684
                         650
                  ....*....|...
gi 17535281  1145 PKWLVEFAPSFFK 1157
Cdd:PRK11131  685 PEWIEPLAQHLIK 697
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
535-713 6.85e-123

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: 375.67  E-value: 6.85e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  535 EQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLG 614
Cdd:cd17971    1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  615 TDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSAT 694
Cdd:cd17971   81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
                        170
                 ....*....|....*....
gi 17535281  695 LDSVKFSEYFLEAPIFTIP 713
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 ...
234-311 1.01e-38

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: 138.53  E-value: 1.01e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGFRQKQEGLVHISQIRNE-RVQTVADVLKRGENVKVKVNKIENGKISLSMKEVDQNSG 311
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEgRVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
939-1021 2.68e-32

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: 120.45  E-value: 2.68e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281     939 LSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNifYRPKEKQDHADQKKAKFHQPEGDHL 1018
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 17535281    1019 TLL 1021
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
932-1020 3.50e-30

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: 115.03  E-value: 3.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    932 ALNTLHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNIFYRP--------------- 996
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 17535281    997 KEKQDHADQKKAKFHQPEGDHLTL 1020
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
GH2-like_DHX8 cd21691
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ...
4-73 2.69e-28

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: 108.40  E-value: 2.69e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    4 LEHLSLVSKVLSEVENHFGVVEKDVAEFVIHLAQENPTFDKLKKALDSqgLGDQFDDSLTATILRIVQSM 73
Cdd:cd21691    1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKE--NGAEFPDSFVESLLRLIQRM 68
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
232-318 6.85e-24

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 98.33  E-value: 6.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI-ENGKISLSMKEVDQNS 310
Cdd:COG1098    4 EVGDIVEGKVTGITPFGAFVELPE---GTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIdEDGKISLSIKQAEEKP 80

                 ....*...
gi 17535281  311 GEDLNPRE 318
Cdd:COG1098   81 KRPPRPRR 88
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
231-307 1.02e-23

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 107.83  E-value: 1.02e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281   231 AEIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIEN-GKISLSMKEVD 307
Cdd:PRK11824  619 PEVGEIYEGKVVRIVDFGAFVEILP---GKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDKrGRIRLSRKAVL 693
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
232-304 1.65e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 72.25  E-value: 1.65e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281     232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:smart00316    1 EVGDVVEGTVTEITPGGAFVDLGN---GVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVdeEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
232-303 1.55e-10

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: 58.07  E-value: 1.55e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535281    232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE--NGKISLSM 303
Cdd:pfam00575    2 EKGDVVEGEVTRVTKGGAFVDLGN---GVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDkdRRRIILSI 72
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
229-314 1.62e-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: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    229 EVAEIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEV 306
Cdd:TIGR00717  183 ENLKEGDVVKGVVKNITDFGAFVDLGGV----DGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFdkEKGRISLSLKQL 258

                   ....*...
gi 17535281    307 DQNSGEDL 314
Cdd:TIGR00717  259 GEDPWEAI 266
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
538-1157 0e+00

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 588.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  538 ESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDV 617
Cdd:COG1643    8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  618 GYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLK-AAARKRPELKLIITSATLD 696
Cdd:COG1643   88 GYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLdLQPALRPDLKLLVMSATLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  697 SVKFSEYFLEAPIFTIPGRTFPVEILYT--REPESDYLEAAHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLyerMKS 774
Cdd:COG1643  168 AERFARLLGDAPVIESSGRTYPVEVRYRplPADERDLEDAVADAVREA-LAEEPGDILVFLPGEREIRRTAEAL---RGR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  775 MGPDVpelIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPI 854
Cdd:COG1643  244 LPPDT---EILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  855 SQAAAKQRSGRAGRTGPGKCYRLYTERAFRdEMLPTPVPEIQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALN 934
Cdd:COG1643  321 SQASANQRAGRAGRLAPGICYRLWSEEDFA-RRPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARAIADARA 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  935 TLHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNifyrPKEKQDHADqkkakfhqpe 1014
Cdd:COG1643  400 LLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERD----PRRGAAGSD---------- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281 1015 gdhltLLAVYNSWKNHHFSQPwcfeNFIQVRSMKRAQDIRKQLLGIMDRHKLLMVScgrDVSRVQKAICSGFFRNAAKRD 1094
Cdd:COG1643  466 -----LLARLNLWRRLREQQR----EFLSYLRLREWRDLARQLRRLLGEGANEEPA---DYEAIGLLLALAYPDRIARRR 533
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281 1095 PQEG-YRtLTDGQNVYIHPSSACFQQqpEWVVYHELVMTTKEY-MREVTAIDPKWLVEFAPSFFK 1157
Cdd:COG1643  534 GEGGrYL-LARGRGAALFPGSPLAKK--EWLVAAELVGGAAEArIRLAAPIDPEWLEELAAHLIK 595
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
501-1157 9.61e-160

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: 510.47  E-value: 9.61e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    501 KDRNNKMKEMPEWLKHVTAGGKATYGRRTNLSMVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEA 580
Cdd:TIGR01967   27 HDQDRAIAALAKFRERIDAACDKVEARRQAVPEIRYPDNLPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    581 GLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLD 660
Cdd:TIGR01967  107 GRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIID 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    661 EAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVKFSEYFLEAPIFTIPGRTFPVEILY------TREPESDYLEA 734
Cdd:TIGR01967  187 EAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrplveeQEDDDLDQLEA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    735 AHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLYERmksmgpDVPELIILPVYGALPSEMQTRIFDpaPAGKRKVVIAT 814
Cdd:TIGR01967  267 ILDAVDEL-FAEGPGDILIFLPGEREIRDAAEILRKR------NLRHTEILPLYARLSNKEQQRVFQ--PHSGRRIVLAT 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    815 NIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPISQAAAKQRSGRAGRTGPGKCYRLYTERAFRDEMLPTPvPE 894
Cdd:TIGR01967  338 NVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTD-PE 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    895 IQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALNTLHTLSALD---GDGLLTKLGRRMAEFPLEPSLSKLLIMS 971
Cdd:TIGR01967  417 ILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDddeAEPQLTPIGRQLAQLPVDPRLARMLLEA 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    972 VDLGCSEEVLTIVAMLNVQNIFYRPKEKQDHADQKKAKFHQPEGDHLTLLavyNSWKnhHFSQP-----------WCFEN 1040
Cdd:TIGR01967  497 HRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRV---NLWR--HIEEQrqalsanqfrnACRKQ 571
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   1041 FIQVRSMKRAQDIRKQLLGIMDRHKLLMVSCGRDVSRVQKAICSGFFRNAAKRDPQEGYrTLTDGQNVYIHPSSACFQQQ 1120
Cdd:TIGR01967  572 YLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEY-DGARGRKFHIFPGSPLFKKP 650
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 17535281   1121 PEWVVYHELVMTTKEYMREVTAIDPKWLVEFAPSFFK 1157
Cdd:TIGR01967  651 PKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK 687
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
527-1157 7.46e-144

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 468.00  E-value: 7.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   527 RRTNLSMVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVA 606
Cdd:PRK11131   60 REAARPEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHTQPRRLAARTVANRIA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   607 EEYGCKLGTDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPEL 686
Cdd:PRK11131  140 EELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPDL 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   687 KLIITSATLDSVKFSEYFLEAPIFTIPGRTFPVEILY------TREPESDYLEAAHITVMQIHlTEPPGDVLVFLTGQEE 760
Cdd:PRK11131  220 KVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYrpiveeADDTERDQLQAIFDAVDELG-REGPGDILIFMSGERE 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   761 IDTSCEVLYERmksmgpDVPELIILPVYGALPSEMQTRIFDpaPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIY 840
Cdd:PRK11131  299 IRDTADALNKL------NLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRY 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   841 NPKSGMDSLVVTPISQAAAKQRSGRAGRTGPGKCYRLYTERAF--RDEMLPtpvPEIQRTNLASTLLQLKAMGINNLIDF 918
Cdd:PRK11131  371 SYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFlsRPEFTD---PEILRTNLASVILQMTALGLGDIAAF 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   919 DFMDAPPLDSMITALNTLHTLSALDGDG-----LLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNIF 993
Cdd:PRK11131  448 PFVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPR 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   994 YRPKEKQDHADQKKAKFHQPEGDHLTLLAVYN----SWKNHHFSQ--PWC---FENFIQVRSMkraQDIRKQLLGIMDRH 1064
Cdd:PRK11131  528 ERPMDKQQASDEKHRRFADKESDFLAFVNLWNylqeQQKALSSNQfrRLCrtdYLNYLRVREW---QDIYTQLRQVVKEL 604
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  1065 KLLMVSCGRDVSRVQKAICSGFFRNAAKRDPQEGYRTLTDGQNVYIHPSSACFQQQPEWVVYHELVMTTKEYMREVTAID 1144
Cdd:PRK11131  605 GIPVNSEPAEYREIHTALLTGLLSHIGMKDAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIE 684
                         650
                  ....*....|...
gi 17535281  1145 PKWLVEFAPSFFK 1157
Cdd:PRK11131  685 PEWIEPLAQHLIK 697
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
535-713 6.85e-123

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: 375.67  E-value: 6.85e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  535 EQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLG 614
Cdd:cd17971    1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  615 TDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSAT 694
Cdd:cd17971   81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
                        170
                 ....*....|....*....
gi 17535281  695 LDSVKFSEYFLEAPIFTIP 713
Cdd:cd17971  161 LDAVKFSQYFYEAPIFTIP 179
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
540-1129 4.16e-110

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: 364.47  E-value: 4.16e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGlGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAP-GIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTVGY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGL-LKAAARKRPELKLIITSATLDSV 698
Cdd:TIGR01970   80 RVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALaLDVQSSLREDLKILAMSATLDGE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    699 KFSEYFLEAPIFTIPGRTFPVEILYTREPESDYLEAAHITVMQIHLTEPPGDVLVFLTGQEEIDTSCEVLYERMKsmgpd 778
Cdd:TIGR01970  160 RLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERLD----- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    779 vPELIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPISQAA 858
Cdd:TIGR01970  235 -SDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQAS 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    859 AKQRSGRAGRTGPGKCYRLYTErAFRDEMLPTPVPEIQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALNTLHT 938
Cdd:TIGR01970  314 ATQRAGRAGRLEPGVCYRLWSE-EQHQRLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    939 LSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNIfyrpkEKQDHADqkkakfhqpegdhl 1018
Cdd:TIGR01970  393 LGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL-----PRQGGAD-------------- 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   1019 tllaVYNSWK-NHHFSQPWCFENFIQVRSMKRAQDIRKQLLGIMDRHKLLMVSCGRDVSRVqkaicsgffrnaAKRDPQE 1097
Cdd:TIGR01970  454 ----LMNRLHrLQQGRQGRGQRAQQLAKKLRRRLRFSQADSGAIASHALGLLLALAFPDRI------------AKRRGQP 517
                          570       580       590
                   ....*....|....*....|....*....|..
gi 17535281   1098 GYRTLTDGQNVYIHPSSACFQQqpEWVVYHEL 1129
Cdd:TIGR01970  518 GRYQLANGRGAVLSAEDALARE--PWLVAADL 547
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
539-987 9.40e-91

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 310.70  E-value: 9.40e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   539 SLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGlGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVG 618
Cdd:PRK11664    3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLLQHG-GINGKIIMLEPRRLAARNVAQRLAEQLGEKPGETVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   619 YTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDV-LFGLLKAAARKRPELKLIITSATLDS 697
Cdd:PRK11664   82 YRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLaLALLLDVQQGLRDDLKLLIMSATLDN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   698 VKFSEYFLEAPIFTIPGRTFPVEILYTREPESDYL-EAAHITVMQIhLTEPPGDVLVFLTGQEEIDTSCEVLYERMKSmg 776
Cdd:PRK11664  162 DRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFdEAVARATAEL-LRQESGSLLLFLPGVGEIQRVQEQLASRVAS-- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   777 pDVpelIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPISQ 856
Cdd:PRK11664  239 -DV---LLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   857 AAAKQRSGRAGRTGPGKCYRLYTERAFrdEMLPT-PVPEIQRTNLASTLLQLKAMGINNLIDFDFMDAPPLDSMITALNT 935
Cdd:PRK11664  315 ASMTQRAGRAGRLEPGICLHLYSKEQA--ERAAAqSEPEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRL 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17535281   936 LHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLgcSEEVLTIVAML 987
Cdd:PRK11664  393 LQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKED--DEAALATAAKL 442
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
540-712 8.95e-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: 284.01  E-value: 8.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRG-KIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVG 618
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGgKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  619 YTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSV 698
Cdd:cd17974   81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
                        170
                 ....*....|....
gi 17535281  699 KFSEYFLEAPIFTI 712
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) ...
556-712 4.52e-88

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: 281.27  E-value: 4.52e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  556 NQILVVVGETGSGKTTQMTQYAIEAGL--GRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGYTIRFEDCTSQDTII 633
Cdd:cd17917    1 NQVVVIVGETGSGKTTQVPQFLLEDGLakGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535281  634 KYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVKFSEYFLEAPIFTI 712
Cdd:cd17917   81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
540-712 4.60e-87

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: 278.96  E-value: 4.60e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVK 699
Cdd:cd17983   81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
                        170
                 ....*....|...
gi 17535281  700 FSEYFLEAPIFTI 712
Cdd:cd17983  161 FADFFGNVPIFTI 173
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
540-712 2.42e-85

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: 274.62  E-value: 2.42e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKR-----PELKLIITSAT 694
Cdd:cd17978   81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSAT 160
                        170
                 ....*....|....*...
gi 17535281  695 LDSVKFSEYFLEAPIFTI 712
Cdd:cd17978  161 LDADLFSEYFNGAPVLYI 178
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
717-878 6.64e-85

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: 272.87  E-value: 6.64e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  717 FPVEILYTREPES-----------DYLEAAHITVMQIHLTEPPGDVLVFLTGQEEIDTSCEVLYERMKSmgPDVPELIIL 785
Cdd:cd18791    1 FPVEVYYLEDILEllgissekedpDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLS--PDLGKLLVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  786 PVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFVKQKIYNPKSGMDSLVVTPISQAAAKQRSGR 865
Cdd:cd18791   79 PLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGR 158
                        170
                 ....*....|...
gi 17535281  866 AGRTGPGKCYRLY 878
Cdd:cd18791  159 AGRTRPGKCYRLY 171
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
531-712 1.02e-80

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: 261.97  E-value: 1.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  531 LSMVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGK--IGCTQPRRVAAMSVAKRVAEE 608
Cdd:cd17973    4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKklVACTQPRRVAAMSVAQRVAEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  609 YGCKLGTDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKL 688
Cdd:cd17973   84 MDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKL 163
                        170       180
                 ....*....|....*....|....
gi 17535281  689 IITSATLDSVKFSEYFLEAPIFTI 712
Cdd:cd17973  164 IVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
540-712 2.31e-70

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: 232.82  E-value: 2.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKA-----AARKRPELKLIITSAT 694
Cdd:cd17984   81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKlfqekSPNRKEHLKVVVMSAT 160
                        170
                 ....*....|....*...
gi 17535281  695 LDSVKFSEYFLEAPIFTI 712
Cdd:cd17984  161 LELAKLSAFFGNCPVFDI 178
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
540-704 2.17e-69

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: 230.43  E-value: 2.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGK-IGCTQPRRVAAMSVAKRVAEEYGCKLGTDVG 618
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRvVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  619 YTIRFEDCTSQD-TIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDS 697
Cdd:cd17980   81 YCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160

                 ....*..
gi 17535281  698 VKFSEYF 704
Cdd:cd17980  161 EKFRDFF 167
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
540-709 5.79e-62

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: 208.85  E-value: 5.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVK 699
Cdd:cd17989   81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
                        170
                 ....*....|
gi 17535281  700 FSEYFLEAPI 709
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 ...
540-708 8.57e-55

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: 189.10  E-value: 8.57e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLG-----RRGKIGCTQPRRVAAMSVAKRVAEEYGcKLG 614
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGspesdNPGMIGITQPRRVAAVSMAKRVAEELN-VFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  615 TDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPE--------- 685
Cdd:cd17982   80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
                        170       180
                 ....*....|....*....|....*..
gi 17535281  686 -LKLIITSATLDSVKFSE---YFLEAP 708
Cdd:cd17982  160 pLKLVIMSATLRVEDFTEnklLFPRPP 186
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
540-709 1.55e-52

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: 181.87  E-value: 1.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRrgkIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLDSVK 699
Cdd:cd17979   78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
                        170
                 ....*....|
gi 17535281  700 FSEYFLEAPI 709
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 ...
540-712 4.72e-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: 169.25  E-value: 4.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQY----AIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYG--CKL 613
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFilddAIERGKGSSCRIVCTQPRRISAISVAERVAAERAesCGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  614 GTDVGYTIRFEDCTSQD-TIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITS 692
Cdd:cd17981   81 GNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
                        170       180
                 ....*....|....*....|
gi 17535281  693 ATLDSVKFSEYFLEAPIFTI 712
Cdd:cd17981  161 ATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
540-709 5.31e-46

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: 163.46  E-value: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLG---RRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTD 616
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSahyQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  617 VGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLD 696
Cdd:cd17977   81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
                        170
                 ....*....|...
gi 17535281  697 SVKFSEYFLEAPI 709
Cdd:cd17977  161 SSKLLSYYGNVPL 173
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
540-712 6.84e-46

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: 163.16  E-value: 6.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIE-----AGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLG 614
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllnGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  615 -----TDVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLI 689
Cdd:cd17975   81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
                        170       180
                 ....*....|....*....|...
gi 17535281  690 ITSATLDSVKFSEYFLEAPIFTI 712
Cdd:cd17975  161 LMSATVDCEKFSSYFTHCPILRI 183
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
540-710 1.96e-45

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: 161.73  E-value: 1.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDVGY 619
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGETVGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  620 TIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAAR-KRPELKLIITSATLDSV 698
Cdd:cd17990   81 RVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQlLRDDLRLLAMSATLDGD 160
                        170
                 ....*....|..
gi 17535281  699 KFSEYFLEAPIF 710
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 ...
540-712 3.15e-44

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: 158.08  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEA----GLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGT 615
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqgPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  616 DVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATL 695
Cdd:cd17985   81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
                        170
                 ....*....|....*..
gi 17535281  696 DSVKFSEYFLEAPIFTI 712
Cdd:cd17985  161 NAELFSDYFNSCPVIHI 177
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
540-712 3.46e-44

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 158.07  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIE--AGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGTDV 617
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDdcYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  618 GYTIRFEDCTSQDTIIKYMTDGMLLRECLI-DPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATLD 696
Cdd:cd17987   81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAgDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
                        170
                 ....*....|....*.
gi 17535281  697 SVKFSEYFLEAPIFTI 712
Cdd:cd17987  161 VNLFIRYFGSCPVIYI 176
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
533-712 6.15e-41

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: 150.75  E-value: 6.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  533 MVEQRESLPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYA----IEAGLGRRGKIGCTQPRRVAAMSVAKRVAEE 608
Cdd:cd17972   52 ILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYIlddfIQNDRAAECNIVVTQPRRISAVSVAERVAFE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  609 YGCKLGTDVGYTIRFEDCTSQD-TIIKYMTDGMLLREclIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELK 687
Cdd:cd17972  132 RGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPDLR 209
                        170       180
                 ....*....|....*....|....*
gi 17535281  688 LIITSATLDSVKFSEYFLEAPIFTI 712
Cdd:cd17972  210 VILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
540-709 1.11e-39

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: 145.32  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIE----AGLGRRGKIGCTQPRRVAAMSVAKRVAEEYGCKLGT 615
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  616 DVGYTIRFED-CTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSAT 694
Cdd:cd17976   81 NVGYQVRLESrPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
                        170
                 ....*....|....*
gi 17535281  695 LDSVKFSEYFLEAPI 709
Cdd:cd17976  161 GDNQRLSRYFGGCPV 175
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
540-712 1.66e-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: 144.66  E-value: 1.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAM-IDNQILVVVGETGSGKTTQMTQYAIEAGLGRR---GKIGCTQPRRVAAMSVAKRVAEEYGCKLGT 615
Cdd:cd17986    1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGfqkGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  616 DVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLFGLLKAAARKRPELKLIITSATL 695
Cdd:cd17986   81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
                        170
                 ....*....|....*..
gi 17535281  696 DSVKFSEYFLEAPIFTI 712
Cdd:cd17986  161 LEPKLRAFWGNPPVVHV 177
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
234-311 1.01e-38

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: 138.53  E-value: 1.01e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGFRQKQEGLVHISQIRNE-RVQTVADVLKRGENVKVKVNKIENGKISLSMKEVDQNSG 311
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLEGLKGRKEGLVHISQLSFEgRVANPSDVVKRGQKVKVKVISIQNGKISLSMKDVDQDTG 79
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
540-712 9.28e-36

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: 134.17  E-value: 9.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  540 LPIFALKKNLMEAMIDNQILVVVGETGSGKTTQMTQYAIEAGLGRrgKIGC----TQPRRVAAMSVAKRVAEEYGCKLGT 615
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKR--GKYCnivvTQPRRIAAISIARRVSQEREWTLGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  616 DVGYTIRFEDCTSQDTIIKYMTDGMLLRECLIDPDLSGYSLIMLDEAHERTIHTDVLF----GLLKAAARkrpELKLIIT 691
Cdd:cd17988   79 LVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLlvvrRLLRTNSR---HVKIILM 155
                        170       180
                 ....*....|....*....|....*
gi 17535281  692 SATLDSVKFSEYF----LEAPIFTI 712
Cdd:cd17988  156 SATISCKEFADYFttpnNPAYVFEV 180
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
939-1021 2.68e-32

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: 120.45  E-value: 2.68e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281     939 LSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNifYRPKEKQDHADQKKAKFHQPEGDHL 1018
Cdd:smart00847    2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79

                    ...
gi 17535281    1019 TLL 1021
Cdd:smart00847   80 TLL 82
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
932-1020 3.50e-30

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: 115.03  E-value: 3.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    932 ALNTLHTLSALDGDGLLTKLGRRMAEFPLEPSLSKLLIMSVDLGCSEEVLTIVAMLNVQNIFYRP--------------- 996
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 17535281    997 KEKQDHADQKKAKFHQPEGDHLTL 1020
Cdd:pfam04408   81 RRAADEKARAKFARLDLEGDHLTL 104
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1078-1154 5.90e-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: 110.81  E-value: 5.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   1078 VQKAICSGFFRNAAKRDPQE-GYRTLTDGQNVYIHPSSACFQQQ---PEWVVYHELVMTTKEYMREVTAIDPKWLVEFAP 1153
Cdd:pfam07717    1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFNEKtfpPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80

                   .
gi 17535281   1154 S 1154
Cdd:pfam07717   81 H 81
GH2-like_DHX8 cd21691
GIPC-homology 2 (GH2)-like domain found in DEAH box protein 8 (DHX8) and similar proteins; ...
4-73 2.69e-28

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: 108.40  E-value: 2.69e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    4 LEHLSLVSKVLSEVENHFGVVEKDVAEFVIHLAQENPTFDKLKKALDSqgLGDQFDDSLTATILRIVQSM 73
Cdd:cd21691    1 LEYLSLVSKVCTELENHLGISDKDLAEFIIDLAEKSKTLDEFKKALKE--NGAEFPDSFVESLLRLIQRM 68
DEXDc smart00487
DEAD-like helicases superfamily;
534-721 4.27e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.89  E-value: 4.27e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281     534 VEQRESLPIFALKKNLMEAMIDN-QILVVVGETGSGKTTQMTQYAIEAGL-GRRGKIGCTQPRRVAAMSVAKRVAEEYGC 611
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKrGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281     612 KLGTDVGYT------IRFEDCTSQDTIIKYMTDGMLLRECLIDP-DLSGYSLIMLDEAHERT--IHTDVLFGLLKaaaRK 682
Cdd:smart00487   81 LGLKVVGLYggdskrEQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLK---LL 157
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 17535281     683 RPELKLIITSATL--DSVKFSEYFLEAPIFTIPGRTFPVEI 721
Cdd:smart00487  158 PKNVQLLLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
232-318 6.85e-24

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 98.33  E-value: 6.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI-ENGKISLSMKEVDQNS 310
Cdd:COG1098    4 EVGDIVEGKVTGITPFGAFVELPE---GTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIdEDGKISLSIKQAEEKP 80

                 ....*...
gi 17535281  311 GEDLNPRE 318
Cdd:COG1098   81 KRPPRPRR 88
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
231-307 1.02e-23

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 107.83  E-value: 1.02e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281   231 AEIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIEN-GKISLSMKEVD 307
Cdd:PRK11824  619 PEVGEIYEGKVVRIVDFGAFVEILP---GKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDKrGRIRLSRKAVL 693
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
229-305 1.45e-23

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 107.40  E-value: 1.45e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281  229 EVAEIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI-ENGKISLSMKE 305
Cdd:COG1185  612 AEPEVGEIYEGKVVRIMDFGAFVEILP---GKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIdDQGRIKLSRKA 686
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
234-303 4.03e-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: 87.98  E-value: 4.03e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIEN-GKISLSM 303
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILP---GKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDDrGRISLSR 68
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
234-304 1.44e-20

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: 86.57  E-value: 1.44e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKV-NKIENGKISLSMK 304
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGG---GISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVlSIDARGRISLSIK 69
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
232-304 1.28e-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: 85.87  E-value: 1.28e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:COG0539  188 EEGDVVEGTVKNITDFGAFVDLGGV----DGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIdrEKERISLSLK 258
rpsA PRK06676
30S ribosomal protein S1; Reviewed
225-306 4.48e-17

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 84.93  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   225 ARKSEVAEI---GKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKI 299
Cdd:PRK06676  181 AKKEELLSSlkeGDVVEGTVARLTDFGAFVDIGGV----DGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIdwETERI 256

                  ....*..
gi 17535281   300 SLSMKEV 306
Cdd:PRK06676  257 SLSLKDT 263
PRK08059 PRK08059
general stress protein 13; Validated
232-306 1.59e-16

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 77.01  E-value: 1.59e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGFRQkqeGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEV 306
Cdd:PRK08059    6 EVGSVVTGKVTGIQPYGAFVALDEETQ---GLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVdeEKGKISLSIRAT 79
PRK05807 PRK05807
RNA-binding protein S1;
232-322 2.42e-16

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 76.71  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGfrqkQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE-NGKISLSMKEVDQNS 310
Cdd:PRK05807    4 KAGSILEGTVVNITNFGAFVEVEG----KTGLVHISEVADTYVKDIREHLKEQDKVKVKVISIDdNGKISLSIKQAMKQK 79
                          90
                  ....*....|..
gi 17535281   311 gEDLNPRETDLN 322
Cdd:PRK05807   80 -KSVKPAEIDWQ 90
rpsA PRK06676
30S ribosomal protein S1; Reviewed
234-319 3.52e-16

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 82.23  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   234 GKIYDGRVNSIQSFGAFITL-EGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDQNS 310
Cdd:PRK06676  278 GDVIEGTVKRLTDFGAFVEVlPGV----EGLVHISQISHKHIATPSEVLEEGQEVKVKVLEVneEEKRISLSIKALEEAP 353

                  ....*....
gi 17535281   311 GEDLNPRET 319
Cdd:PRK06676  354 AEEEDRREE 362
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
232-304 1.65e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 72.25  E-value: 1.65e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281     232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:smart00316    1 EVGDVVEGTVTEITPGGAFVDLGN---GVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVdeEKGRIILSLK 72
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
233-306 1.68e-15

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: 79.32  E-value: 1.68e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281  233 IGKIYDGRVNSIQSFGAFITLE-GFrqkqEGLVHISQI-RNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEV 306
Cdd:COG0539  274 VGDVVKGKVTRLTDFGAFVELEpGV----EGLVHISEMsWTKRVAHPSDVVKVGDEVEVKVLDIdpEERRISLSIKQL 347
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
230-312 4.30e-15

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 79.99  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   230 VAE---IGKIYDGRVNSIQSFGAFITLE-GFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSM 303
Cdd:PRK00087  556 VEEkypVGSIVLGKVVRIAPFGAFVELEpGV----DGLVHISQISWKRIDKPEDVLSEGEEVKAKILEVdpEEKRIRLSI 631

                  ....*....
gi 17535281   304 KEVDQNSGE 312
Cdd:PRK00087  632 KEVEEEPGD 640
PRK08582 PRK08582
RNA-binding protein S1;
232-342 6.40e-15

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 72.76  E-value: 6.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE-NGKISLSMKE-VDQN 309
Cdd:PRK08582    4 EVGSKLQGKVTGITNFGAFVELPE---GKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEdDGKIGLSIKKaKDRP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 17535281   310 SGEDLNPRETDLNPdaiGVRPRTPPASTSSWMN 342
Cdd:PRK08582   81 KRQHDRPRHEDNRG---GGNDVAPKEDFEQKMS 110
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
233-302 6.63e-15

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: 70.35  E-value: 6.63e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535281  233 IGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLS 302
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDLGGV----DGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIdkERKRISLG 68
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
232-304 1.95e-14

S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function with an N-terminal S1 RNA binding domain, a CCHC type zinc finger, and clusters of basic amino acids representing a potential nucleolar targeting signal. pNO40 was identified through a yeast two-hybrid interaction screen of a human kidney cDNA library using the pinin (pnn) protein as bait. pNO40 is thought to play a role in ribosome maturation and/or biogenesis.


Pssm-ID: 240191 [Multi-domain]  Cd Length: 73  Bit Score: 69.43  E-value: 1.95e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGFRQkqEGLVHISQIRNERVQTVADVLKRGENVKVKV-NKIENGKISLSMK 304
Cdd:cd05686    2 ALYQIFKGEVASVTEYGAFVKIPGCRK--QGLVHKSHMSSCRVDDPSEVVDVGEKVWVKViGREMKDKMKLSLS 73
HELICc smart00490
helicase superfamily c-terminal domain;
766-870 3.32e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 68.78  E-value: 3.32e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281     766 EVLYERMKSMGpdvpeLIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIAETSLTIDGIFYVVDPGFvkqkiynpksg 845
Cdd:smart00490    1 EELAELLKELG-----IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL----------- 64
                            90       100
                    ....*....|....*....|....*
gi 17535281     846 mdslvvtPISQAAAKQRSGRAGRTG 870
Cdd:smart00490   65 -------PWSPASYIQRIGRAGRAG 82
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
232-306 4.94e-14

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 76.52  E-value: 4.94e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEV 306
Cdd:PRK00087  476 EEGDVVEGEVKRLTDFGAFVDIGGV----DGLLHVSEISWGRVEKPSDVLKVGDEIKVYILDIdkENKKLSLSLKKL 548
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
738-870 6.04e-14

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: 69.16  E-value: 6.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    738 TVMQIHLTEPPGDVLVFLTGQEEIDtsCEVLYERMKsmgpdvpeLIILPVYGALPSEMQTRIFDPAPAGKRKVVIATNIA 817
Cdd:pfam00271    5 ALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEG--------IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17535281    818 ETSLTIDGIFYVVdpgfvkqkIYNPKSGMDSLVvtpisqaaakQRSGRAGRTG 870
Cdd:pfam00271   75 ERGLDLPDVDLVI--------NYDLPWNPASYI----------QRIGRAGRAG 109
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
234-302 2.51e-11

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: 60.32  E-value: 2.51e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535281  234 GKIYDGRVNSIQSFGAFITLeGFrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLS 302
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDI-GV--KQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIdeERGRISLS 68
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
232-304 8.52e-11

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: 58.88  E-value: 8.52e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGfrQKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:cd05708    1 KVGQKIDGTVRRVEDYGVFIDIDG--TNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIdaEKKRISLGLK 73
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
232-303 1.55e-10

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: 58.07  E-value: 1.55e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535281    232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE--NGKISLSM 303
Cdd:pfam00575    2 EKGDVVEGEVTRVTKGGAFVDLGN---GVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDkdRRRIILSI 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
237-302 1.81e-10

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: 57.78  E-value: 1.81e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281  237 YDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLS 302
Cdd:cd00164    1 VTGKVVSITKFGVFVELED---GVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVdpEKGRISLS 65
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
232-308 1.90e-10

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 65.05  E-value: 1.90e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLeGFrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDQ 308
Cdd:COG2183  640 KPGMILEGTVTNVTDFGAFVDI-GV--HQDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVdlKRKRISLSMKLDDE 715
rpsA PRK07899
30S ribosomal protein S1; Reviewed
233-323 1.06e-09

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 62.37  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   233 IGKIYDGRVNSIQSFGAFITLEgfrQKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDqns 310
Cdd:PRK07899  293 IGQIVPGKVTKLVPFGAFVRVE---EGIEGLVHISELAERHVEVPEQVVQVGDEVFVKVIDIdlERRRISLSLKQAN--- 366
                          90
                  ....*....|...
gi 17535281   311 gEDLNPRETDLNP 323
Cdd:PRK07899  367 -EGVTPESEDFDP 378
GH2_like cd21690
GIPC homology 2 (GH2) domain-like family; The GIPC (GAIP C-terminus-interacting protein) ...
7-70 1.32e-09

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: 55.17  E-value: 1.32e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535281    7 LSLVSKVLSEVENHFGVVEKDVAEFVIHLAQENPTFDKLKKALDSQGLGdqFDDSLTATILRIV 70
Cdd:cd21690    1 LSAIEKVDDLLKNYLGIDDPELAEFVISLAKKKKNPDEFAEALDENDAA--FPDEFVFDLYRAI 62
rpsA PRK06299
30S ribosomal protein S1; Reviewed
225-304 2.13e-09

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 61.72  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   225 ARKSEVAEI---GKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKI 299
Cdd:PRK06299  190 EEREELLENleeGQVVEGVVKNITDYGAFVDLGGV----DGLLHITDISWKRVNHPSEVVNVGDEVKVKVLKFdkEKKRV 265

                  ....*
gi 17535281   300 SLSMK 304
Cdd:PRK06299  266 SLGLK 270
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
232-304 4.89e-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: 4.89e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGFRQKqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:cd04452    2 EEGELVVVTVKSIADMGAYVSLLEYGNI-EGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVdkEKGYIDLSKK 75
rpsA PRK06299
30S ribosomal protein S1; Reviewed
234-308 5.20e-09

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 60.18  E-value: 5.20e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17535281   234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDQ 308
Cdd:PRK06299  461 GSIVTGTVTEVKDKGAFVELED---GVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIdrKNRRISLSIKALDE 534
rpsA PRK13806
30S ribosomal protein S1; Provisional
229-306 6.86e-09

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 59.74  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   229 EVAEIGKIYDGRVNSIQSFGAFITLE-GFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIENG------KISL 301
Cdd:PRK13806  198 ETVKEGDVVEGTVTRLAPFGAFVELApGV----EGMVHISELSWSRVQKADEAVSVGDTVRVKVLGIERAkkgkglRISL 273

                  ....*
gi 17535281   302 SMKEV 306
Cdd:PRK13806  274 SIKQA 278
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
651-879 7.44e-09

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 59.99  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   651 LSGYSLIMLDEAHERTIHTDVLFgllkAAARKRPEL--KLIITSATL-DSVKFSEYFLEAPIFT-IPGRT-FPVEILYTR 725
Cdd:PHA02653  289 LFDYGTVIIDEVHEHDQIGDIII----AVARKHIDKirSLFLMTATLeDDRDRIKEFFPNPAFVhIPGGTlFPISEVYVK 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   726 EPESDYLEAAHI-----TVMQIHLTEPPGD---VLVFLTGQEEIDTSCEVLYERMksmgpdvPELIILPVYGALPS--EM 795
Cdd:PHA02653  365 NKYNPKNKRAYIeeekkNIVTALKKYTPPKgssGIVFVASVSQCEEYKKYLEKRL-------PIYDFYIIHGKVPNidEI 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   796 QTRIFD-PAPAgkrkVVIATNIAETSLTIDGIFYVVDPGfvkqKIYNPK--SGMDSLvvtpISQAAAKQRSGRAGRTGPG 872
Cdd:PHA02653  438 LEKVYSsKNPS----IIISTPYLESSVTIRNATHVYDTG----RVYVPEpfGGKEMF----ISKSMRTQRKGRVGRVSPG 505

                  ....*..
gi 17535281   873 KCYRLYT 879
Cdd:PHA02653  506 TYVYFYD 512
rpsA PRK06299
30S ribosomal protein S1; Reviewed
233-309 1.48e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 59.02  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   233 IGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIR-NERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDQN 309
Cdd:PRK06299  373 VGDVVEGKVKNITDFGAFVGLEG---GIDGLVHLSDISwDKKGEEAVELYKKGDEVEAVVLKVdvEKERISLGIKQLEED 449
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
559-694 1.52e-08

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: 54.72  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  559 LVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEYgcKLGTDVGYTIRFED------CTSQDTI 632
Cdd:cd00046    4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELF--GPGIRVAVLVGGSSaeerekNKLGDAD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535281  633 IKYMTDGMLLRECLID--PDLSGYSLIMLDEAHERTIHTDVLFGLLKAA-ARKRPELKLIITSAT 694
Cdd:cd00046   82 IIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVrKAGLKNAQVILLSAT 146
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
229-314 1.62e-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: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    229 EVAEIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEV 306
Cdd:TIGR00717  183 ENLKEGDVVKGVVKNITDFGAFVDLGGV----DGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFdkEKGRISLSLKQL 258

                   ....*...
gi 17535281    307 DQNSGEDL 314
Cdd:TIGR00717  259 GEDPWEAI 266
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
226-318 2.20e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 57.12  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   226 RKSEVAEIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSM 303
Cdd:PRK07400  189 RKMNRLEVGEVVVGTVRGIKPYGAFIDIGGV----SGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLdaERGRISLST 264
                          90
                  ....*....|....*
gi 17535281   304 KEVDQNSGEDLNPRE 318
Cdd:PRK07400  265 KQLEPEPGDMLKDPQ 279
rpsA PRK06299
30S ribosomal protein S1; Reviewed
232-309 4.08e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 57.48  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLE-GFrqkqEGLVHISQI----RNERVQtvaDVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:PRK06299  285 PVGSKVKGKVTNITDYGAFVELEeGI----EGLVHVSEMswtkKNKHPS---KVVSVGQEVEVMVLEIdeEKRRISLGLK 357

                  ....*
gi 17535281   305 EVDQN 309
Cdd:PRK06299  358 QCKEN 362
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
233-304 5.19e-08

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 52.40  E-value: 5.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535281   233 IGKIYDGRVNSIQSFGAFITLEgfrQKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE--NGKISLSMK 304
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALE---NGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDeyTGKASLSLR 73
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
234-303 8.67e-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: 50.18  E-value: 8.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIR-NERVQTVADVLKRGENVKVKVNKIENGKISLSM 303
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDG---GIDGLVHISDISwTQRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
233-303 2.42e-07

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: 49.32  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  233 IGKIYDGRVNSIQSFGAFITLEGFrqKQEGLVHISQIRNERVQTVADVLK-RGEN----------VKVKVNK--IENGKI 299
Cdd:cd04471    1 VGEEFDGVISGVTSFGLFVELDNL--TVEGLVHVSTLGDDYYEFDEENHAlVGERtgkvfrlgdkVKVRVVRvdLDRRKI 78

                 ....
gi 17535281  300 SLSM 303
Cdd:cd04471   79 DFEL 82
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
226-309 1.25e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 51.36  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   226 RKSEVAEIGKIYDGRVNSIQSFGAFITLEGFRQKqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSM 303
Cdd:PRK03987    1 KRKEWPEEGELVVGTVKEVKDFGAFVTLDEYPGK-EGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVdpRKGHIDLSL 79

                  ....*.
gi 17535281   304 KEVDQN 309
Cdd:PRK03987   80 KRVNEH 85
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
234-309 1.37e-06

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: 52.43  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    234 GKIYDGRVNSIQSFGAFITL-EGFrqkqEGLVHISQIR-NERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKEVDQN 309
Cdd:TIGR00717  273 GDKITGRVTNLTDYGVFVEIeEGI----EGLVHVSEMSwVKKNSHPSKVVKKGDEVEVMILDIdpERRRLSLGLKQCKAN 348
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
557-663 4.26e-06

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: 47.93  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  557 QILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAeeygcklGTDVGY-TIRFEDCTSQDTIIKY 635
Cdd:cd17931    2 QLTVLDLHPGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYrTGAVKEEHGGNEIVDY 74
                         90       100
                 ....*....|....*....|....*...
gi 17535281  636 MTDGMLLRECLIDPDLSGYSLIMLDEAH 663
Cdd:cd17931   75 MCHGTFTCRLLSPKRVPNYNLIIMDEAH 102
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
234-304 4.76e-06

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: 50.50  E-value: 4.76e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535281    234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIE--NGKISLSMK 304
Cdd:TIGR00717  447 GSVVKGKVTEIKDFGAFVELPG---GVEGLIRNSELSENRDEDKTDEIKVGDEVEAKVVDIDkkNRKVSLSVK 516
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
233-309 6.37e-06

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: 50.12  E-value: 6.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    233 IGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGEN-VKVKVNKI--ENGKISLSMKEVDQN 309
Cdd:TIGR00717  359 VGDRVTGKIKKITDFGAFVELEG---GIDGLIHLSDISWDKDGREADHLYKKGDeIEAVVLAVdkEKKRISLGVKQLTEN 435
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
230-352 9.69e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 49.89  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   230 VAEIGKIY-DGRVNSIQSFGAFITLEGFRqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI-ENGKISLSMK--- 304
Cdd:PLN00207  750 VPTVGDIYrNCEIKSIAPYGAFVEIAPGR---EGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVnDKGQLRLSRRall 826
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17535281   305 ---EVDQNSGEDLNPRETDLNPDAIGVRPRTPPASTSSwmnPEASGVGQGP 352
Cdd:PLN00207  827 peaNSEKSSQKQQGGSTKDKAPQKKYVNTSSRPRRAAQ---AEKNSAENAA 874
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
232-302 1.10e-05

S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of this family is not fully understood. In Escherichia coli, RecJ degrades single-stranded DNA in the 5'-3' direction and participates in homologous recombination and mismatch repair.


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 44.52  E-value: 1.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535281  232 EIGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNErvqtvadvLKRGENVKVKVNKI-ENGKISLS 302
Cdd:cd04473   15 EVGKLYKGKVNGVAKYGVFVDLND---HVRGLIHRSNLLRD--------YEVGDEVIVQVTDIpENGNIDLI 75
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
536-698 1.37e-05

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 46.47  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    536 QRESLPIFALKKNLmeamidnqilVVVGETGSGKTTQMTQYAIEAGLGRRGKIGC--TQPRRVAA---MSVAKRVAEEYG 610
Cdd:pfam00270    4 QAEAIPAILEGRDV----------LVQAPTGSGKTLAFLLPALEALDKLDNGPQAlvLAPTRELAeqiYEELKKLGKGLG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    611 CKLGTDVGYTIRFEDCTSQDTI-IKYMTDGMLLRECLIDPDLSGYSLIMLDEAHErtiHTDVLFG--LLKAAARKRPELK 687
Cdd:pfam00270   74 LKVASLLGGDSRKEQLEKLKGPdILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR---LLDMGFGpdLEEILRRLPKKRQ 150
                          170
                   ....*....|.
gi 17535281    688 LIITSATLDSV 698
Cdd:pfam00270  151 ILLLSATLPRN 161
VacB COG0557
Exoribonuclease R [Transcription];
233-303 1.60e-05

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 49.33  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  233 IGKIYDGRVNSIQSFGAFITLEGFrqKQEGLVHISQIRN------ERVQTVadVLKR-------GENVKVKVNK--IENG 297
Cdd:COG0557  622 VGEEFEGVISGVTSFGLFVELDEL--GVEGLVHVSSLGDdyyeydERRQAL--VGERtgkryrlGDRVEVRVVRvdLDRR 697

                 ....*.
gi 17535281  298 KISLSM 303
Cdd:COG0557  698 QIDFEL 703
rpsA PRK13806
30S ribosomal protein S1; Provisional
232-305 2.68e-05

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 48.18  E-value: 2.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281   232 EIGKIYDGRVNSIQSFGAFI-TLEGFrqkqEGLVHISQIR-NERVQTVADVLKRGENVKVKVNKI--ENGKISLSMKE 305
Cdd:PRK13806  291 KAGDKVTGKVVRLAPFGAFVeILPGI----EGLVHVSEMSwTRRVNKPEDVVAPGDAVAVKIKDIdpAKRRISLSLRD 364
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
558-898 4.70e-05

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: 47.04  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  558 ILVVVGETGSGKTTQMTQYAIEA-GLGRRGKIGCTQPRRVAAMSVAKRVAEEYG-CKLGTDVGYTIRFEDCTSQDTIIK- 634
Cdd:cd09639    1 LLVIEAPTGYGKTEAALLWALHSlKSQKADRVIIALPTRATINAMYRRAKEAFGeTGLYHSSILSSRIKEMGDSEEFEHl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  635 ---YMTDGML-----LRECLID-------PDLSGY---------SLIMLDEAHERTIHTDVLF-GLLKAAARKRpeLKLI 689
Cdd:cd09639   81 fplYIHSNDTlfldpITVCTIDqvlksvfGEFGHYeftlasianSLLIFDEVHFYDEYTLALIlAVLEVLKDND--VPIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  690 ITSATLdSVKFSEYFL--EAPIFTIPGRTFPVEILYTREPESDYLEAAHITVMQIHLTEPPGDVLVFLTgqeEIDTSCEV 767
Cdd:cd09639  159 LMSATL-PKFLKEYAEkiGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAIIVN---TVDRAQEF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  768 lYERMKSMGPDVPELII----LPVYGALPSEMQTRIFdpapagKRK---VVIATNIAETSLTIDGIFYVVDPgfvkqkiy 840
Cdd:cd09639  235 -YQQLKEKGPEEEIMLIhsrfTEKDRAKKEAELLLEF------KKSekfVIVATQVIEASLDISVDVMITEL-------- 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  841 npkSGMDSLVvtpisqaaakQRSGRAGRTGPGKCYRLYTERAFRD--EMLPTPVPEIQRT 898
Cdd:cd09639  300 ---APIDSLI----------QRLGRLHRYGEKNGEEVYIITDAPDgkGQKPYPYDLVERT 346
rpsA PRK07899
30S ribosomal protein S1; Reviewed
234-304 5.63e-05

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 47.35  E-value: 5.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535281   234 GKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSMK 304
Cdd:PRK07899  209 GQVRKGVVSSIVNFGAFVDLGGV----DGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVdmDRERVSLSLK 277
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
232-304 5.74e-05

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 45.20  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVAD-----------VLKRGENVKVKV-------NK 293
Cdd:PRK08563   80 ELQEVVEGEVVEVVEFGAFVRIGPV----DGLLHISQIMDDYISYDPKngrligkeskrVLKVGDVVRARIvavslkeRR 155
                          90
                  ....*....|.
gi 17535281   294 IENGKISLSMK 304
Cdd:PRK08563  156 PRGSKIGLTMR 166
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
233-317 5.77e-05

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 47.40  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281   233 IGKIYDGRVNSIQSFGAFITL-EGFrqkqEGLVHISQIR-NERVQTVADVLKRGENVKVKV--NKIENGKISLSMKEVDQ 308
Cdd:PRK12269  578 VNDVVKGRVTKIADFGAFIELaEGI----EGLAHISEFSwVKKTSKPSDMVKIGDEVECMIlgYDIQAGRVSLGLKQVTA 653

                  ....*....
gi 17535281   309 NSGEDLNPR 317
Cdd:PRK12269  654 NPWEEIEAR 662
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
236-305 1.47e-04

S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. RpoE is subunit E of archaeal RNA polymerase. Archaeal cells contain a single RNA polymerase made up of 12 subunits, which are homologous to the 12 subunits (RPB1-12) of eukaryotic RNA polymerase II. RpoE is homologous to Rpa43 of eukaryotic RNA polymerase I, RPB7 of eukaryotic RNA polymerase II, and Rpc25 of eukaryotic RNA polymerase III. RpoE is composed of two domains, the N-terminal RNP (ribonucleoprotein) domain and the C-terminal S1 domain. This S1 domain binds ssRNA and ssDNA. This family is classified based on the C-terminal S1 domain. The function of RpoE is not fully understood. In eukaryotes, RPB7 and RPB4 form a heterodimer that reversibly associates with the RNA polymerase II core.


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 41.89  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281  236 IYDGRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVAD-----------VLKRGENVKVKV-------NKIENG 297
Cdd:cd04460    2 VVEGEVVEVVDFGAFVRIGPV----DGLLHISQIMDDYISYDPKnkrligeetkrVLKVGDVVRARIvavslkeRRPRES 77

                 ....*...
gi 17535281  298 KISLSMKE 305
Cdd:cd04460   78 KIGLTMRQ 85
rpsA PRK06676
30S ribosomal protein S1; Reviewed
232-307 1.75e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 45.25  E-value: 1.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281   232 EIGKIYDGRVNSIQSFGAFITLEGfrQKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIENGKIS--LSMKEVD 307
Cdd:PRK06676   16 EVGDVVTGEVLKVEDKQVFVNIEG--YKVEGVIPISELSNDHIEDINDVVKVGDELEVYVLKVEDGEGNllLSKRRLE 91
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
234-304 2.07e-04

S1_RPS1_repeat_ec1_hs1: 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 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 40.59  E-value: 2.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535281  234 GKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIEN--GKISLSMK 304
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGY---KSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDeeGNVVLSKR 70
AAA_22 pfam13401
AAA domain;
557-663 7.65e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 7.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535281    557 QILVVVGETGSGKTTQMTQYAIEAGLGRRGKIGCTQPRRVAAMSVAKRVAEEygckLGTDVGYTIRFEDCTSqdtiikym 636
Cdd:pfam13401    6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRA----LGLPLSGRLSKEELLA-------- 73
                           90       100
                   ....*....|....*....|....*..
gi 17535281    637 tdgMLLRECLidpDLSGYSLIMLDEAH 663
Cdd:pfam13401   74 ---ALQQLLL---ALAVAVVLIIDEAQ 94
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
809-878 9.28e-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: 39.22  E-value: 9.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535281  809 KVVIATNIAETSLTIDGIFYVVDPGFvkqkiynpksgmdslvvtPISQAAAKQRSGRAGRTG--PGKCYRLY 878
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
239-304 2.33e-03

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 42.39  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281   239 GRVNSIQSFGAFITLEGFrqkqEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIENG--KISLSMK 304
Cdd:PRK12269  499 GVVKSFTSFGAFIDLGGF----DGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAekRINLSLK 562
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
228-303 5.88e-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: 37.18  E-value: 5.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535281  228 SEVAEiGKIYDGRVNSIQSFGAFITlegFRQKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKI--ENGKISLSM 303
Cdd:cd04461   10 SDLKP-GMVVHGYVRNITPYGVFVE---FLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVdeEKQRFLLSL 83
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
233-307 7.34e-03

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 40.32  E-value: 7.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17535281   233 IGKIYDGRVNSIQSFGAFITLEGfrqKQEGLVHISQIRNERVQTVADVLKRGENVKVKVNKIEN--GKISLSMKEVD 307
Cdd:PRK00087  302 RGDIVKGTVVSVNENEVFVDVGY---KSEGVIPLRELTLDEISSLKESVKVGDEIEVKVLKLEDedGYVVLSKKEAD 375
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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