|
Name |
Accession |
Description |
Interval |
E-value |
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1-1058 |
0e+00 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 1684.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPS 80
Cdd:PRK10811 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 81 SYHAHGRPNIKDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRIELKEALSSLEL 160
Cdd:PRK10811 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 161 PEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLA 240
Cdd:PRK10811 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 241 RQHITALGRPDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAF 320
Cdd:PRK10811 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGESS 400
Cdd:PRK10811 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 401 HHVCPRCSGTGTIRDNESLSLSILRLIEEEALKENTHQVHAIVPVQIASYLLNEKRKAVSAIEHRQGDVGVVIVPNDQMQ 480
Cdd:PRK10811 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQGGVRCVIVPNDQMQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 481 TPHFSVLRVRKGEEISTLSYLLPQLHEAEMTNAQDDGQHERKRPEQPAISTFDLPA-----ETVAPVAAKTKEKKVVVSN 555
Cdd:PRK10811 481 TPHYSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDvppapTPAEPAAPVVAAAPKAAAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 556 NqQIEQPGLFSRFLCALKKIFNGEEEKQEQEKSNKSSSNDNRRSPERRNSRRQNQRRERNENDTRNNH----NRERGDEQ 631
Cdd:PRK10811 561 T-PPAQPGLLSRFFGALKALFSGGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRDNRtrreGRENREEN 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 632 RKGRNVQQKNNAPDN-IAVDIDNEAREAQQQQRREQRAERQRRRQEEKRQQQLETKVQQTSRPEITEEEVE-EHQPVMPR 709
Cdd:PRK10811 640 RRNRRQAQQQTAETReSQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEeRVQQVQPR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 710 RQRRQLEQKIRITDNVKEEVV-------VASLPVVTKAiiPAITEEEKKVSVPAIIDTNVEAANQpsipqgsiaQNNEQQ 782
Cdd:PRK10811 720 RKQRQLNQKVRIEQSVAEEAVapvveetVAAEPVVQEV--PAPRTELVKVPLPVVAQTAPEQDEE---------NNAENR 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 783 D-NIMPRRSRRSPRHLRVSGQRRRRYRDERNLTQSPVPLVMAVASPELASGKVWVRYPVTPV----TQPAEPEVSTVEET 857
Cdd:PRK10811 789 DnNGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPqdvqVEEQREAEEVQVQP 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 858 VIGAEQKESVMPIPAVAESVSVSVSTVADTQVAEQNAVTHDDIKSATNGDPLVEPVPEKPEVlVSENLEPVVNHDTQY-- 935
Cdd:PRK10811 869 VVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV-ITESDVAVAQEVAEHae 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 936 --QPEALHDMLVHDTEETRHT--AEPIIVTSIAEQEQHEEQPTVTTEIYAKAEEVKAEETkiaespIIVEKNHHASSPMT 1011
Cdd:PRK10811 948 pvVEPQDETADIEEAAETAEVvvAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP------EATVEHNHATAPMT 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 502754280 1012 KAPAPDLAAQPVIINEWQRPAYPFAGKGGAGGHSATNIATSAMSKPQ 1058
Cdd:PRK10811 1022 RAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHSATHHASAPATRPQ 1068
|
|
| CafA |
COG1530 |
Ribonuclease G or E [Translation, ribosomal structure and biogenesis]; |
2-493 |
0e+00 |
|
Ribonuclease G or E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441139 [Multi-domain] Cd Length: 490 Bit Score: 869.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 2 KRMLINATQQEeLRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPSS 81
Cdd:COG1530 1 KEILINATPQE-TRVALVEGGRLVELDIERPGREQLVGNIYKGKVTRVLPGLQAAFVDIGLERHGFLHVKDISPEYFSLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 82 YHAHG-RPNIKDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNpRAGGISRRIEG-DDRIELKEALSSLE 159
Cdd:COG1530 80 KEDSGkRPNIQDVLKEGQEVLVQVVKEPRGTKGARLTTFISLAGRYLVLMPNN-RHVGVSRRIEGeEERERLKELLSELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 160 LPEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDL 239
Cdd:COG1530 159 VPEGMGLIVRTAAEGASEEELQWDLDYLLKLWEAIQEAAKSAKAPFLIYQELDLIIRALRDYFRPDIGEILVDSREAYEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 240 ARQHITALgRPDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETA 319
Cdd:COG1530 239 AKDFISLV-MPDLADRVKLYTGERPLFDRYQIESQIESALERRVWLKSGGYLVIDQTEALTTIDVNSGRFTGGRNIEETA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 320 FNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGES 399
Cdd:COG1530 318 FKTNLEAADEIARQLRLRDLGGIIVIDFIDMEDEEHQREVENRLKEALKKDRARTQIGGISRFGLVEMTRQRLRPSLGES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 400 SHHVCPRCSGTGTIRDNESLSLSILRLIEEEALKENTHQVHAIVPVQIASYLLNEKRKAVSAIEHRQGdVGVVIVPNDQM 479
Cdd:COG1530 398 LCEPCPRCEGRGTIKSVETVALEILREIEREARKENTREVLVQAPPEVAAYLLNEKRQELAELEKRYG-VSIKLIPNPSL 476
|
490
....*....|....
gi 502754280 480 QTPHFSVLRVRKGE 493
Cdd:COG1530 477 ETEQYDIVRLRDDE 490
|
|
| RNaseEG |
TIGR00757 |
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic ... |
14-425 |
0e+00 |
|
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome. [Transcription, Degradation of RNA]
Pssm-ID: 273254 [Multi-domain] Cd Length: 414 Bit Score: 632.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 14 LRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYF---PSSYHAHGRPNI 90
Cdd:TIGR00757 1 TRVALVEGGRLFDLIIERPKSRQLKGNIYKGRVTRILPSLQAAFVDIGLEKNGFLHASDIGPNYEclaPAEAKREAGPSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 91 KDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRaGGISRRIE-GDDRIELKEALSSLELPEGMGLIVR 169
Cdd:TIGR00757 81 SELLRPGQSVLVQVVKEPRGNKGARLTTDISLPGRYLVLMPNNSH-VGVSRRIEsGEERERLKKLLRSEELPEGMGLIIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 170 TAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLARQHItALGR 249
Cdd:TIGR00757 160 TAAEGASEEALIKDLEFLLRKWEKIKEKAQKRPAPCLIYGEPDIIKRVIRDYLDTDVKEILIDSKEIYEEAKEFI-QLYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 250 PDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAFNTNLEAADE 329
Cdd:TIGR00757 239 PELVSKLKLYRGSDPLFEGFQIEKQIDKATQRKVWLPSGGYIVIDQTEALTTIDVNSGRFTGGGNLEETALNTNLEAAKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 330 IARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGESSHHVCPRCSG 409
Cdd:TIGR00757 319 IARQLRLRNLGGIIIIDFIDMKSEKNQRRVLERLKEALRRDRARIQISGISEFGLVEMTRKRLRESLMEVLGTVCPHCSG 398
|
410
....*....|....*.
gi 502754280 410 TGTIRDNESLSLSILR 425
Cdd:TIGR00757 399 TGIVKTSESVLLEIER 414
|
|
| RNase_E_G |
pfam10150 |
Ribonuclease E/G family; Ribonuclease E and Ribonuclease G are related enzymes that cleave a ... |
122-390 |
1.44e-133 |
|
Ribonuclease E/G family; Ribonuclease E and Ribonuclease G are related enzymes that cleave a wide variety of RNAs.
Pssm-ID: 462965 Cd Length: 267 Bit Score: 404.46 E-value: 1.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 122 LAGSYLVLMPNNpRAGGISRRIEGD-DRIELKEALSSLeLPEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADN 200
Cdd:pfam10150 1 LPGRYLVLMPFG-KIVGVSRKIEDEeERERLKEILESL-KPEGMGVIVRTAAEGASEEELQADLEYLLKLWEEILKKAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 201 HPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLARQHITALGrPDFASKIKLYSGEVPLFSHYQIESQIESAFQ 280
Cdd:pfam10150 79 AKAPSLLYEELDLILRVLRDLLNDDIDEIIVDDEEVYEEIKEFLEEIA-PDLKKRVELYEGERPLFDLYGIEKQIEKALS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 281 REVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVE 360
Cdd:pfam10150 158 RKVWLKSGGYLVIDQTEALTVIDVNSGKFTGKKNLEETALKTNLEAAKEIARQLRLRNLGGIIVIDFIDMKDEENREKVL 237
|
250 260 270
....*....|....*....|....*....|
gi 502754280 361 NRLRDAVRQDRARIQIGRISRFGLLEMSRQ 390
Cdd:pfam10150 238 EALKEALKKDRAKTQVLGITKLGLVEMTRK 267
|
|
| S1_RNase_E |
cd04453 |
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ... |
32-124 |
8.34e-35 |
|
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay.
Pssm-ID: 239900 [Multi-domain] Cd Length: 88 Bit Score: 127.71 E-value: 8.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 32 PGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPssyhahGRPNIKDILKEGQEVIVQVDKEERGN 111
Cdd:cd04453 1 PNREPIVGNIYLGRVKKIVPGLQAAFVDIGLGKNGFLHLSDILPAYFK------KHKKIAKLLKEGQEILVQVVKEPIGT 74
|
90
....*....|...
gi 502754280 112 KGAALTTFISLAG 124
Cdd:cd04453 75 KGPRLTTNISLPG 87
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
37-118 |
1.61e-08 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 52.22 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 37 KKANIYKGKITRIEPSleAAFVDYGAERHGFLPIKEIAREYfpssyhahgRPNIKDILKEGQEVIVQVDKEERGNKGAAL 116
Cdd:smart00316 1 EVGDVVEGTVTEITPG--GAFVDLGNGVEGLIPISELSDKR---------VKDPEEVLKVGDEVKVKVLSVDEEKGRIIL 69
|
..
gi 502754280 117 TT 118
Cdd:smart00316 70 SL 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1-1058 |
0e+00 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 1684.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPS 80
Cdd:PRK10811 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 81 SYHAHGRPNIKDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRIELKEALSSLEL 160
Cdd:PRK10811 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 161 PEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLA 240
Cdd:PRK10811 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 241 RQHITALGRPDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAF 320
Cdd:PRK10811 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGESS 400
Cdd:PRK10811 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 401 HHVCPRCSGTGTIRDNESLSLSILRLIEEEALKENTHQVHAIVPVQIASYLLNEKRKAVSAIEHRQGDVGVVIVPNDQMQ 480
Cdd:PRK10811 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQGGVRCVIVPNDQMQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 481 TPHFSVLRVRKGEEISTLSYLLPQLHEAEMTNAQDDGQHERKRPEQPAISTFDLPA-----ETVAPVAAKTKEKKVVVSN 555
Cdd:PRK10811 481 TPHYSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDvppapTPAEPAAPVVAAAPKAAAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 556 NqQIEQPGLFSRFLCALKKIFNGEEEKQEQEKSNKSSSNDNRRSPERRNSRRQNQRRERNENDTRNNH----NRERGDEQ 631
Cdd:PRK10811 561 T-PPAQPGLLSRFFGALKALFSGGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRDNRtrreGRENREEN 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 632 RKGRNVQQKNNAPDN-IAVDIDNEAREAQQQQRREQRAERQRRRQEEKRQQQLETKVQQTSRPEITEEEVE-EHQPVMPR 709
Cdd:PRK10811 640 RRNRRQAQQQTAETReSQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEeRVQQVQPR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 710 RQRRQLEQKIRITDNVKEEVV-------VASLPVVTKAiiPAITEEEKKVSVPAIIDTNVEAANQpsipqgsiaQNNEQQ 782
Cdd:PRK10811 720 RKQRQLNQKVRIEQSVAEEAVapvveetVAAEPVVQEV--PAPRTELVKVPLPVVAQTAPEQDEE---------NNAENR 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 783 D-NIMPRRSRRSPRHLRVSGQRRRRYRDERNLTQSPVPLVMAVASPELASGKVWVRYPVTPV----TQPAEPEVSTVEET 857
Cdd:PRK10811 789 DnNGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPqdvqVEEQREAEEVQVQP 868
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 858 VIGAEQKESVMPIPAVAESVSVSVSTVADTQVAEQNAVTHDDIKSATNGDPLVEPVPEKPEVlVSENLEPVVNHDTQY-- 935
Cdd:PRK10811 869 VVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV-ITESDVAVAQEVAEHae 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 936 --QPEALHDMLVHDTEETRHT--AEPIIVTSIAEQEQHEEQPTVTTEIYAKAEEVKAEETkiaespIIVEKNHHASSPMT 1011
Cdd:PRK10811 948 pvVEPQDETADIEEAAETAEVvvAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP------EATVEHNHATAPMT 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 502754280 1012 KAPAPDLAAQPVIINEWQRPAYPFAGKGGAGGHSATNIATSAMSKPQ 1058
Cdd:PRK10811 1022 RAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHSATHHASAPATRPQ 1068
|
|
| CafA |
COG1530 |
Ribonuclease G or E [Translation, ribosomal structure and biogenesis]; |
2-493 |
0e+00 |
|
Ribonuclease G or E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441139 [Multi-domain] Cd Length: 490 Bit Score: 869.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 2 KRMLINATQQEeLRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPSS 81
Cdd:COG1530 1 KEILINATPQE-TRVALVEGGRLVELDIERPGREQLVGNIYKGKVTRVLPGLQAAFVDIGLERHGFLHVKDISPEYFSLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 82 YHAHG-RPNIKDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNpRAGGISRRIEG-DDRIELKEALSSLE 159
Cdd:COG1530 80 KEDSGkRPNIQDVLKEGQEVLVQVVKEPRGTKGARLTTFISLAGRYLVLMPNN-RHVGVSRRIEGeEERERLKELLSELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 160 LPEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDL 239
Cdd:COG1530 159 VPEGMGLIVRTAAEGASEEELQWDLDYLLKLWEAIQEAAKSAKAPFLIYQELDLIIRALRDYFRPDIGEILVDSREAYEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 240 ARQHITALgRPDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETA 319
Cdd:COG1530 239 AKDFISLV-MPDLADRVKLYTGERPLFDRYQIESQIESALERRVWLKSGGYLVIDQTEALTTIDVNSGRFTGGRNIEETA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 320 FNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGES 399
Cdd:COG1530 318 FKTNLEAADEIARQLRLRDLGGIIVIDFIDMEDEEHQREVENRLKEALKKDRARTQIGGISRFGLVEMTRQRLRPSLGES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 400 SHHVCPRCSGTGTIRDNESLSLSILRLIEEEALKENTHQVHAIVPVQIASYLLNEKRKAVSAIEHRQGdVGVVIVPNDQM 479
Cdd:COG1530 398 LCEPCPRCEGRGTIKSVETVALEILREIEREARKENTREVLVQAPPEVAAYLLNEKRQELAELEKRYG-VSIKLIPNPSL 476
|
490
....*....|....
gi 502754280 480 QTPHFSVLRVRKGE 493
Cdd:COG1530 477 ETEQYDIVRLRDDE 490
|
|
| RNaseEG |
TIGR00757 |
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic ... |
14-425 |
0e+00 |
|
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome. [Transcription, Degradation of RNA]
Pssm-ID: 273254 [Multi-domain] Cd Length: 414 Bit Score: 632.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 14 LRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYF---PSSYHAHGRPNI 90
Cdd:TIGR00757 1 TRVALVEGGRLFDLIIERPKSRQLKGNIYKGRVTRILPSLQAAFVDIGLEKNGFLHASDIGPNYEclaPAEAKREAGPSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 91 KDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRaGGISRRIE-GDDRIELKEALSSLELPEGMGLIVR 169
Cdd:TIGR00757 81 SELLRPGQSVLVQVVKEPRGNKGARLTTDISLPGRYLVLMPNNSH-VGVSRRIEsGEERERLKKLLRSEELPEGMGLIIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 170 TAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLARQHItALGR 249
Cdd:TIGR00757 160 TAAEGASEEALIKDLEFLLRKWEKIKEKAQKRPAPCLIYGEPDIIKRVIRDYLDTDVKEILIDSKEIYEEAKEFI-QLYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 250 PDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAFNTNLEAADE 329
Cdd:TIGR00757 239 PELVSKLKLYRGSDPLFEGFQIEKQIDKATQRKVWLPSGGYIVIDQTEALTTIDVNSGRFTGGGNLEETALNTNLEAAKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 330 IARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSPSLGESSHHVCPRCSG 409
Cdd:TIGR00757 319 IARQLRLRNLGGIIIIDFIDMKSEKNQRRVLERLKEALRRDRARIQISGISEFGLVEMTRKRLRESLMEVLGTVCPHCSG 398
|
410
....*....|....*.
gi 502754280 410 TGTIRDNESLSLSILR 425
Cdd:TIGR00757 399 TGIVKTSESVLLEIER 414
|
|
| RNase_E_G |
pfam10150 |
Ribonuclease E/G family; Ribonuclease E and Ribonuclease G are related enzymes that cleave a ... |
122-390 |
1.44e-133 |
|
Ribonuclease E/G family; Ribonuclease E and Ribonuclease G are related enzymes that cleave a wide variety of RNAs.
Pssm-ID: 462965 Cd Length: 267 Bit Score: 404.46 E-value: 1.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 122 LAGSYLVLMPNNpRAGGISRRIEGD-DRIELKEALSSLeLPEGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADN 200
Cdd:pfam10150 1 LPGRYLVLMPFG-KIVGVSRKIEDEeERERLKEILESL-KPEGMGVIVRTAAEGASEEELQADLEYLLKLWEEILKKAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 201 HPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNPKILDLARQHITALGrPDFASKIKLYSGEVPLFSHYQIESQIESAFQ 280
Cdd:pfam10150 79 AKAPSLLYEELDLILRVLRDLLNDDIDEIIVDDEEVYEEIKEFLEEIA-PDLKKRVELYEGERPLFDLYGIEKQIEKALS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 281 REVRLPSGGSVVIDTTEALTAIDINSSRATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVE 360
Cdd:pfam10150 158 RKVWLKSGGYLVIDQTEALTVIDVNSGKFTGKKNLEETALKTNLEAAKEIARQLRLRNLGGIIVIDFIDMKDEENREKVL 237
|
250 260 270
....*....|....*....|....*....|
gi 502754280 361 NRLRDAVRQDRARIQIGRISRFGLLEMSRQ 390
Cdd:pfam10150 238 EALKEALKKDRAKTQVLGITKLGLVEMTRK 267
|
|
| PRK11712 |
PRK11712 |
ribonuclease G; Provisional |
4-463 |
1.37e-97 |
|
ribonuclease G; Provisional
Pssm-ID: 183285 [Multi-domain] Cd Length: 489 Bit Score: 317.72 E-value: 1.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 4 MLINATQQEElRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFL------PIKEIAREY 77
Cdd:PRK11712 5 LLVNVTPSET-RVALIEGGILQEIHIEREAKRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLhasdivPHTECVAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 78 FPSSYHAhgrPNIKDILKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGgISRRIEGDdriELKEALSS 157
Cdd:PRK11712 84 EQKQFVV---RDISELVRQGQDIMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVG-VSQRIESE---EERERLKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 158 LELP---EGMGLIVRTAGVGKSAEALQGDLNFRLKHWEAIKKAADNHPAPFLIHQESNVIVRAFRDYLRPDIGEILIDNP 234
Cdd:PRK11712 157 IVAPycdEQGGFIIRTAAEGVGEEELAQDAAFLKRLWTKVMERKKRYQTRYQLYGELALAQRVLRDFVGAELDRIRVDSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 235 KILDLArQHITALGRPDFASKIKLYSGEVPLFSHYQIESQIESAFQREVRLPSGGSVVIDTTEALTAIDINSSRATRGGD 314
Cdd:PRK11712 237 LTYEEL-KEFTSEYIPEMTDKLEHYSGRQPIFDLYDVENEIQRALERKVELKSGGYLIIDQTEAMTTVDINTGAFVGHRN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 315 IEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQREVENRLRDAVRQDRARIQIGRISRFGLLEMSRQRLSP 394
Cdd:PRK11712 316 LEETIFNTNIEATQAIARQLRLRNLGGIIIIDFIDMNNEDHRRRVLHSLEQALSKDRVKTNINGFSQLGLVEMTRKRTRE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754280 395 SLGESSHHVCPRCSGTGTIRDNESLSLSILRLIE--EEALKENTHQVHAIVPVqiASYLLNEKRKAVSAIE 463
Cdd:PRK11712 396 SLEHVLCGECPTCHGRGTVKTVETVCYEIMREIVrvHHAYDSDRFLVYASPAV--AEALKGEESHALAELE 464
|
|
| S1_RNase_E |
cd04453 |
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ... |
32-124 |
8.34e-35 |
|
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay.
Pssm-ID: 239900 [Multi-domain] Cd Length: 88 Bit Score: 127.71 E-value: 8.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 32 PGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPIKEIAREYFPssyhahGRPNIKDILKEGQEVIVQVDKEERGN 111
Cdd:cd04453 1 PNREPIVGNIYLGRVKKIVPGLQAAFVDIGLGKNGFLHLSDILPAYFK------KHKKIAKLLKEGQEILVQVVKEPIGT 74
|
90
....*....|...
gi 502754280 112 KGAALTTFISLAG 124
Cdd:cd04453 75 KGPRLTTNISLPG 87
|
|
| PNPase_C |
pfam12111 |
Polyribonucleotide phosphorylase C terminal; PNPase regulates the expression of small ... |
1022-1058 |
5.76e-13 |
|
Polyribonucleotide phosphorylase C terminal; PNPase regulates the expression of small non-coding RNAs that control expression of outer-membrane proteins. The enzyme also affects complex processes, such as the tissue-invasive virulence of Salmonella enterica and the regulation of a virulence-factor secretion system in Yersinia. In Escherichia coli, PNPase is involved in the quality control of ribosomal RNA precursors and is required for growth following cold shock. This family contains the C terminal protomer domain of the PNPase core. The function of the C terminal protomer is to catalyze phosphorolysis through its two active sites.
Pssm-ID: 432339 [Multi-domain] Cd Length: 37 Bit Score: 63.92 E-value: 5.76e-13
10 20 30
....*....|....*....|....*....|....*..
gi 502754280 1022 PVIINEWQRPAYPFAGKGGAGGHSATNIATSAMSKPQ 1058
Cdd:pfam12111 1 PPRISDWQRPRYYFEGKGSAGGHSATSHATAPATKPE 37
|
|
| S1 |
pfam00575 |
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ... |
37-118 |
1.27e-09 |
|
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: 55.37 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 37 KKANIYKGKITRIEPslEAAFVDYGAERHGFLPIKEIareyfpssyHAHGRPNIKDILKEGQEVIVQVDKEERGNKGAAL 116
Cdd:pfam00575 2 EKGDVVEGEVTRVTK--GGAFVDLGNGVEGFIPISEL---------SDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIIL 70
|
..
gi 502754280 117 TT 118
Cdd:pfam00575 71 SI 72
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
37-118 |
1.61e-08 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 52.22 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 37 KKANIYKGKITRIEPSleAAFVDYGAERHGFLPIKEIAREYfpssyhahgRPNIKDILKEGQEVIVQVDKEERGNKGAAL 116
Cdd:smart00316 1 EVGDVVEGTVTEITPG--GAFVDLGNGVEGLIPISELSDKR---------VKDPEEVLKVGDEVKVKVLSVDEEKGRIIL 69
|
..
gi 502754280 117 TT 118
Cdd:smart00316 70 SL 71
|
|
| S1_like |
cd00164 |
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ... |
42-117 |
7.24e-06 |
|
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: 44.68 E-value: 7.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502754280 42 YKGKITRIEPslEAAFVDYGAERHGFLPIKEIAREYfpssyhahgRPNIKDILKEGQEVIVQVDKEERGNKGAALT 117
Cdd:cd00164 1 VTGKVVSITK--FGVFVELEDGVEGLVHISELSDKF---------VKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
|
|
| YabR |
COG1098 |
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ... |
40-110 |
1.01e-05 |
|
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];
Pssm-ID: 440715 [Multi-domain] Cd Length: 130 Bit Score: 45.94 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502754280 40 NIYKGKITRIEPSleAAFVDYGAERHGFLPIKEIAREYFpssyhahgrPNIKDILKEGQEVIVQV-DKEERG 110
Cdd:COG1098 7 DIVEGKVTGITPF--GAFVELPEGTTGLVHISEIADGYV---------KDINDYLKVGDEVKVKVlSIDEDG 67
|
|
| S1_RPS1_repeat_hs4 |
cd05692 |
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
44-110 |
9.32e-05 |
|
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: 41.50 E-value: 9.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502754280 44 GKITRIEPSleAAFVDYGAERHGFLPIKEIAREYFPssyhahgrpNIKDILKEGQEVIVQV-DKEERG 110
Cdd:cd05692 6 GTVTRLKPF--GAFVELGGGISGLVHISQIAHKRVK---------DVKDVLKEGDKVKVKVlSIDARG 62
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
41-110 |
1.48e-04 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 45.81 E-value: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754280 41 IYKGKITRIEPSleAAFVDYGAERHGFLPIKEIAREYFPssyhahgrpNIKDILKEGQEVIVQV-DKEERG 110
Cdd:PRK11824 624 IYEGKVVRIVDF--GAFVEILPGKDGLVHISEIADERVE---------KVEDVLKEGDEVKVKVlEIDKRG 683
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
37-132 |
5.61e-04 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 43.78 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 37 KKANIYKGKITRIEPSleAAFVDYGAeRHGFLPIKEIareyfpsSYHAHGRPniKDILKEGQEVIVQVDKEERGNKGaal 116
Cdd:PRK00087 476 EEGDVVEGEVKRLTDF--GAFVDIGG-VDGLLHVSEI-------SWGRVEKP--SDVLKVGDEIKVYILDIDKENKK--- 540
|
90
....*....|....*.
gi 502754280 117 ttfISLagSYLVLMPN 132
Cdd:PRK00087 541 ---LSL--SLKKLLPD 551
|
|
| PRK08059 |
PRK08059 |
general stress protein 13; Validated |
41-112 |
1.29e-03 |
|
general stress protein 13; Validated
Pssm-ID: 181215 [Multi-domain] Cd Length: 123 Bit Score: 39.64 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502754280 41 IYKGKITRIEPSleAAFVDYGAERHGFLPIKEIAREYFPssyhahgrpNIKDILKEGQEVIVQV-DKEERGNK 112
Cdd:PRK08059 10 VVTGKVTGIQPY--GAFVALDEETQGLVHISEITHGFVK---------DIHDFLSVGDEVKVKVlSVDEEKGK 71
|
|
| S1_RPS1_repeat_ec1_hs1 |
cd05687 |
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
41-111 |
3.07e-03 |
|
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: 37.12 E-value: 3.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502754280 41 IYKGKITRIEPslEAAFVDYGAERHGFLPIKEIareyfpSSYHahgRPNIKDILKEGQEVIVQVDKEERGN 111
Cdd:cd05687 3 IVKGTVVSVDD--DEVLVDIGYKSEGIIPISEF------SDDP---IENGEDEVKVGDEVEVYVLRVEDEE 62
|
|
| RpsA |
COG0539 |
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ... |
41-109 |
4.12e-03 |
|
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: 40.80 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502754280 41 IYKGKITRIepsleaafVDYGA--------ErhGFLPIKEIareyfpsSYHAHGRpNIKDILKEGQEV---IVQVDKEER 109
Cdd:COG0539 277 VVKGKVTRL--------TDFGAfvelepgvE--GLVHISEM-------SWTKRVA-HPSDVVKVGDEVevkVLDIDPEER 338
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