|
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: 1818.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
Cdd:PRK10811 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
Cdd:PRK10811 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
Cdd:PRK10811 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
Cdd:PRK10811 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
Cdd:PRK10811 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQDGVRCVIVPNDQME 480
Cdd:PRK10811 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQGGVRCVIVPNDQMQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 481 TPHYHVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVppAPTPAEPAAPVVAPAPKAAPA 560
Cdd:PRK10811 481 TPHYSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDV--PPAPTPAEPAAPVVAAAPKAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 561 TPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERT--EGSDNREE 638
Cdd:PRK10811 559 AATPPAQPGLLSRFFGALKALFSGGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRDNRTrrEGRENREE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 639 NRRNRRQAQQQTAETREsRQQAEVTEKARTADEQQ-APRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQ 717
Cdd:PRK10811 639 NRRNRRQAQQQTAETRE-SQQAEVTEKARTQDEQQqAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQ 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 718 PRRKQRQLNQKVRYEQSVAEEAvVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRR 797
Cdd:PRK10811 718 PRRKQRQLNQKVRIEQSVAEEA-VAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNNGMPRR 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 798 SRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVA 877
Cdd:PRK10811 797 SRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVA 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 878 AAIEPVVSAPVVEEVAGVVEAPVQVAEPQPE---VVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEET 954
Cdd:PRK10811 877 AAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEevvVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDET 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 955 ADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEV--------TVEHNHATAPMTRAPAPEYVPEAPRHS 1026
Cdd:PRK10811 957 ADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVapaqvpeaTVEHNHATAPMTRAPAPEYVPEAPRHS 1036
|
1050 1060 1070
....*....|....*....|....*....|..
gi 16129047 1027 DWQRPTFAFEGKGAAGGHTATHHASAAPARPQ 1058
Cdd:PRK10811 1037 DWQRPTFAFEGKGAAGGHSATHHASAPATRPQ 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: 872.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 2 KRMLINATQQEeLRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPAN 81
Cdd:COG1530 1 KEILINATPQE-TRVALVEGGRLVELDIERPGREQLVGNIYKGKVTRVLPGLQAAFVDIGLERHGFLHVKDISPEYFSLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 82 YSAHG-RPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNpRAGGISRRIEG-DDRTELKEALASLE 159
Cdd:COG1530 80 KEDSGkRPNIQDVLKEGQEVLVQVVKEPRGTKGARLTTFISLAGRYLVLMPNN-RHVGVSRRIEGeEERERLKELLSELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 160 LPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLEL 239
Cdd:COG1530 159 VPEGMGLIVRTAAEGASEEELQWDLDYLLKLWEAIQEAAKSAKAPFLIYQELDLIIRALRDYFRPDIGEILVDSREAYEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 240 ARQHIAALgRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETA 319
Cdd:COG1530 239 AKDFISLV-MPDLADRVKLYTGERPLFDRYQIESQIESALERRVWLKSGGYLVIDQTEALTTIDVNSGRFTGGRNIEETA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 320 FNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGES 399
Cdd:COG1530 318 FKTNLEAADEIARQLRLRDLGGIIVIDFIDMEDEEHQREVENRLKEALKKDRARTQIGGISRFGLVEMTRQRLRPSLGES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 400 SHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQdGVRCVIVPNDQM 479
Cdd:COG1530 398 LCEPCPRCEGRGTIKSVETVALEILREIEREARKENTREVLVQAPPEVAAYLLNEKRQELAELEKRY-GVSIKLIPNPSL 476
|
490
....*....|....
gi 16129047 480 ETPHYHVLRVRKGE 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: 660.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 14 LRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYF---PANYSAHGRPNI 90
Cdd:TIGR00757 1 TRVALVEGGRLFDLIIERPKSRQLKGNIYKGRVTRILPSLQAAFVDIGLEKNGFLHASDIGPNYEclaPAEAKREAGPSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 91 KDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRaGGISRRIE-GDDRTELKEALASLELPEGMGLIVR 169
Cdd:TIGR00757 81 SELLRPGQSVLVQVVKEPRGNKGARLTTDISLPGRYLVLMPNNSH-VGVSRRIEsGEERERLKKLLRSEELPEGMGLIIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 170 TAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAaLGR 249
Cdd:TIGR00757 160 TAAEGASEEALIKDLEFLLRKWEKIKEKAQKRPAPCLIYGEPDIIKRVIRDYLDTDVKEILIDSKEIYEEAKEFIQ-LYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 250 PDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADE 329
Cdd:TIGR00757 239 PELVSKLKLYRGSDPLFEGFQIEKQIDKATQRKVWLPSGGYIVIDQTEALTTIDVNSGRFTGGGNLEETALNTNLEAAKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 330 IARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSG 409
Cdd:TIGR00757 319 IARQLRLRNLGGIIIIDFIDMKSEKNQRRVLERLKEALRRDRARIQISGISEFGLVEMTRKRLRESLMEVLGTVCPHCSG 398
|
410
....*....|....*.
gi 16129047 410 TGTVRDNESLSLSILR 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 |
9.28e-138 |
|
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: 415.25 E-value: 9.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 122 LAGSYLVLMPNNpRAGGISRRIEGD-DRTELKEALASLeLPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAES 200
Cdd:pfam10150 1 LPGRYLVLMPFG-KIVGVSRKIEDEeERERLKEILESL-KPEGMGVIVRTAAEGASEEELQADLEYLLKLWEEILKKAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 201 RPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGrPDFSSKIKLYTGEIPLFSHYQIESQIESAFQ 280
Cdd:pfam10150 79 AKAPSLLYEELDLILRVLRDLLNDDIDEIIVDDEEVYEEIKEFLEEIA-PDLKKRVELYEGERPLFDLYGIEKQIEKALS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 281 REVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVE 360
Cdd:pfam10150 158 RKVWLKSGGYLVIDQTEALTVIDVNSGKFTGKKNLEETALKTNLEAAKEIARQLRLRNLGGIIVIDFIDMKDEENREKVL 237
|
250 260 270
....*....|....*....|....*....|
gi 16129047 361 NRLREAVRQDRARIQISHISRFGLLEMSRQ 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 |
5.18e-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: 128.10 E-value: 5.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 32 PGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPanysahGRPNIKDVLREGQEVIVQIDKEERGN 111
Cdd:cd04453 1 PNREPIVGNIYLGRVKKIVPGLQAAFVDIGLGKNGFLHLSDILPAYFK------KHKKIAKLLKEGQEILVQVVKEPIGT 74
|
90
....*....|...
gi 16129047 112 KGAALTTFISLAG 124
Cdd:cd04453 75 KGPRLTTNISLPG 87
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
37-118 |
4.47e-09 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 53.76 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 37 KKANIYKGKITRIEPSleAAFVDYGAERHGFLPLKEIAREYfpanysahgRPNIKDVLREGQEVIVQIDKEERGNKGAAL 116
Cdd:smart00316 1 EVGDVVEGTVTEITPG--GAFVDLGNGVEGLIPISELSDKR---------VKDPEEVLKVGDEVKVKVLSVDEEKGRIIL 69
|
..
gi 16129047 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: 1818.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
Cdd:PRK10811 1 MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
Cdd:PRK10811 81 NYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
Cdd:PRK10811 161 PEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
Cdd:PRK10811 241 RQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
Cdd:PRK10811 321 NTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQDGVRCVIVPNDQME 480
Cdd:PRK10811 401 HHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQGGVRCVIVPNDQMQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 481 TPHYHVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVppAPTPAEPAAPVVAPAPKAAPA 560
Cdd:PRK10811 481 TPHYSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDV--PPAPTPAEPAAPVVAAAPKAA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 561 TPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERT--EGSDNREE 638
Cdd:PRK10811 559 AATPPAQPGLLSRFFGALKALFSGGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRDNRTrrEGRENREE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 639 NRRNRRQAQQQTAETREsRQQAEVTEKARTADEQQ-APRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQ 717
Cdd:PRK10811 639 NRRNRRQAQQQTAETRE-SQQAEVTEKARTQDEQQqAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQ 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 718 PRRKQRQLNQKVRYEQSVAEEAvVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRR 797
Cdd:PRK10811 718 PRRKQRQLNQKVRIEQSVAEEA-VAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNNGMPRR 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 798 SRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVA 877
Cdd:PRK10811 797 SRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPEMASGKVWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVA 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 878 AAIEPVVSAPVVEEVAGVVEAPVQVAEPQPE---VVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEET 954
Cdd:PRK10811 877 AAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEevvVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDET 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 955 ADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEV--------TVEHNHATAPMTRAPAPEYVPEAPRHS 1026
Cdd:PRK10811 957 ADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVapaqvpeaTVEHNHATAPMTRAPAPEYVPEAPRHS 1036
|
1050 1060 1070
....*....|....*....|....*....|..
gi 16129047 1027 DWQRPTFAFEGKGAAGGHTATHHASAAPARPQ 1058
Cdd:PRK10811 1037 DWQRPTFAFEGKGAAGGHSATHHASAPATRPQ 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: 872.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 2 KRMLINATQQEeLRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPAN 81
Cdd:COG1530 1 KEILINATPQE-TRVALVEGGRLVELDIERPGREQLVGNIYKGKVTRVLPGLQAAFVDIGLERHGFLHVKDISPEYFSLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 82 YSAHG-RPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNpRAGGISRRIEG-DDRTELKEALASLE 159
Cdd:COG1530 80 KEDSGkRPNIQDVLKEGQEVLVQVVKEPRGTKGARLTTFISLAGRYLVLMPNN-RHVGVSRRIEGeEERERLKELLSELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 160 LPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLEL 239
Cdd:COG1530 159 VPEGMGLIVRTAAEGASEEELQWDLDYLLKLWEAIQEAAKSAKAPFLIYQELDLIIRALRDYFRPDIGEILVDSREAYEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 240 ARQHIAALgRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETA 319
Cdd:COG1530 239 AKDFISLV-MPDLADRVKLYTGERPLFDRYQIESQIESALERRVWLKSGGYLVIDQTEALTTIDVNSGRFTGGRNIEETA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 320 FNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGES 399
Cdd:COG1530 318 FKTNLEAADEIARQLRLRDLGGIIVIDFIDMEDEEHQREVENRLKEALKKDRARTQIGGISRFGLVEMTRQRLRPSLGES 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 400 SHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQdGVRCVIVPNDQM 479
Cdd:COG1530 398 LCEPCPRCEGRGTIKSVETVALEILREIEREARKENTREVLVQAPPEVAAYLLNEKRQELAELEKRY-GVSIKLIPNPSL 476
|
490
....*....|....
gi 16129047 480 ETPHYHVLRVRKGE 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: 660.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 14 LRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYF---PANYSAHGRPNI 90
Cdd:TIGR00757 1 TRVALVEGGRLFDLIIERPKSRQLKGNIYKGRVTRILPSLQAAFVDIGLEKNGFLHASDIGPNYEclaPAEAKREAGPSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 91 KDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRaGGISRRIE-GDDRTELKEALASLELPEGMGLIVR 169
Cdd:TIGR00757 81 SELLRPGQSVLVQVVKEPRGNKGARLTTDISLPGRYLVLMPNNSH-VGVSRRIEsGEERERLKKLLRSEELPEGMGLIIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 170 TAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAaLGR 249
Cdd:TIGR00757 160 TAAEGASEEALIKDLEFLLRKWEKIKEKAQKRPAPCLIYGEPDIIKRVIRDYLDTDVKEILIDSKEIYEEAKEFIQ-LYA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 250 PDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADE 329
Cdd:TIGR00757 239 PELVSKLKLYRGSDPLFEGFQIEKQIDKATQRKVWLPSGGYIVIDQTEALTTIDVNSGRFTGGGNLEETALNTNLEAAKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 330 IARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSG 409
Cdd:TIGR00757 319 IARQLRLRNLGGIIIIDFIDMKSEKNQRRVLERLKEALRRDRARIQISGISEFGLVEMTRKRLRESLMEVLGTVCPHCSG 398
|
410
....*....|....*.
gi 16129047 410 TGTVRDNESLSLSILR 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 |
9.28e-138 |
|
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: 415.25 E-value: 9.28e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 122 LAGSYLVLMPNNpRAGGISRRIEGD-DRTELKEALASLeLPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAES 200
Cdd:pfam10150 1 LPGRYLVLMPFG-KIVGVSRKIEDEeERERLKEILESL-KPEGMGVIVRTAAEGASEEELQADLEYLLKLWEEILKKAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 201 RPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGrPDFSSKIKLYTGEIPLFSHYQIESQIESAFQ 280
Cdd:pfam10150 79 AKAPSLLYEELDLILRVLRDLLNDDIDEIIVDDEEVYEEIKEFLEEIA-PDLKKRVELYEGERPLFDLYGIEKQIEKALS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 281 REVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVE 360
Cdd:pfam10150 158 RKVWLKSGGYLVIDQTEALTVIDVNSGKFTGKKNLEETALKTNLEAAKEIARQLRLRNLGGIIVIDFIDMKDEENREKVL 237
|
250 260 270
....*....|....*....|....*....|
gi 16129047 361 NRLREAVRQDRARIQISHISRFGLLEMSRQ 390
Cdd:pfam10150 238 EALKEALKKDRAKTQVLGITKLGLVEMTRK 267
|
|
| PRK11712 |
PRK11712 |
ribonuclease G; Provisional |
4-427 |
5.37e-99 |
|
ribonuclease G; Provisional
Pssm-ID: 183285 [Multi-domain] Cd Length: 489 Bit Score: 321.58 E-value: 5.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 4 MLINATQQEElRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFL------PLKEIAREY 77
Cdd:PRK11712 5 LLVNVTPSET-RVALIEGGILQEIHIEREAKRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLhasdivPHTECVAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 78 FPANYSAhgrPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGgISRRIE-GDDRTELKEALA 156
Cdd:PRK11712 84 EQKQFVV---RDISELVRQGQDIMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVG-VSQRIEsEEERERLKKIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 157 SLeLPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDN--- 233
Cdd:PRK11712 160 PY-CDEQGGFIIRTAAEGVGEEELAQDAAFLKRLWTKVMERKKRYQTRYQLYGELALAQRVLRDFVGAELDRIRVDSrlt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 234 -PKVLELARQHIaalgrPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRG 312
Cdd:PRK11712 239 yEELKEFTSEYI-----PEMTDKLEHYSGRQPIFDLYDVENEIQRALERKVELKSGGYLIIDQTEAMTTVDINTGAFVGH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 313 GDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRL 392
Cdd:PRK11712 314 RNLEETIFNTNIEATQAIARQLRLRNLGGIIIIDFIDMNNEDHRRRVLHSLEQALSKDRVKTNINGFSQLGLVEMTRKRT 393
|
410 420 430
....*....|....*....|....*....|....*
gi 16129047 393 SPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLI 427
Cdd:PRK11712 394 RESLEHVLCGECPTCHGRGTVKTVETVCYEIMREI 428
|
|
| S1_RNase_E |
cd04453 |
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ... |
32-124 |
5.18e-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: 128.10 E-value: 5.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 32 PGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPanysahGRPNIKDVLREGQEVIVQIDKEERGN 111
Cdd:cd04453 1 PNREPIVGNIYLGRVKKIVPGLQAAFVDIGLGKNGFLHLSDILPAYFK------KHKKIAKLLKEGQEILVQVVKEPIGT 74
|
90
....*....|...
gi 16129047 112 KGAALTTFISLAG 124
Cdd:cd04453 75 KGPRLTTNISLPG 87
|
|
| PNPase_C |
pfam12111 |
Polyribonucleotide phosphorylase C terminal; PNPase regulates the expression of small ... |
1022-1058 |
1.91e-16 |
|
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: 73.55 E-value: 1.91e-16
10 20 30
....*....|....*....|....*....|....*..
gi 16129047 1022 APRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQ 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 |
3.81e-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: 56.91 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 37 KKANIYKGKITRIEPslEAAFVDYGAERHGFLPLKEIareyfpanySAHGRPNIKDVLREGQEVIVQIDKEERGNKGAAL 116
Cdd:pfam00575 2 EKGDVVEGEVTRVTK--GGAFVDLGNGVEGFIPISEL---------SDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIIL 70
|
..
gi 16129047 117 TT 118
Cdd:pfam00575 71 SI 72
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
37-118 |
4.47e-09 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 53.76 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 37 KKANIYKGKITRIEPSleAAFVDYGAERHGFLPLKEIAREYfpanysahgRPNIKDVLREGQEVIVQIDKEERGNKGAAL 116
Cdd:smart00316 1 EVGDVVEGTVTEITPG--GAFVDLGNGVEGLIPISELSDKR---------VKDPEEVLKVGDEVKVKVLSVDEEKGRIIL 69
|
..
gi 16129047 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 |
7.03e-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: 7.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129047 42 YKGKITRIEPslEAAFVDYGAERHGFLPLKEIAREYfpanysahgRPNIKDVLREGQEVIVQIDKEERGNKGAALT 117
Cdd:cd00164 1 VTGKVVSITK--FGVFVELEDGVEGLVHISELSDKF---------VKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
|
|
| S1_RPS1_repeat_hs4 |
cd05692 |
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
44-110 |
1.85e-04 |
|
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: 40.73 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129047 44 GKITRIEPSleAAFVDYGAERHGFLPLKEIAREYFPanysahgrpNIKDVLREGQEVIVQI-DKEERG 110
Cdd:cd05692 6 GTVTRLKPF--GAFVELGGGISGLVHISQIAHKRVK---------DVKDVLKEGDKVKVKVlSIDARG 62
|
|
| S1_PNPase |
cd04472 |
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ... |
41-111 |
3.10e-04 |
|
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: 39.83 E-value: 3.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129047 41 IYKGKITRIEPSleAAFVDYGAERHGFLPLKEIAREYFPanysahgrpNIKDVLREGQEVIVQ-IDKEERGN 111
Cdd:cd04472 3 IYEGKVVKIKDF--GAFVEILPGKDGLVHISELSDERVE---------KVEDVLKVGDEVKVKvIEVDDRGR 63
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
586-783 |
6.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 586 EETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRnrrqaqqqtaETRESRQQAEVTEK 665
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE----------EAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 666 ARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVqprrKQRQLNQKVRYEQSVAEEAVVAPvv 745
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI----KAEEAKKEAEEDKKKAEEAKKDE-- 1753
|
170 180 190
....*....|....*....|....*....|....*...
gi 16129047 746 EETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEE 783
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
37-132 |
2.98e-03 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 41.47 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129047 37 KKANIYKGKITRIEPSleAAFVDYGAeRHGFLPLKEIAreyfpanysaHGRPN-IKDVLREGQEVIVQIDKEERGNKGaa 115
Cdd:PRK00087 476 EEGDVVEGEVKRLTDF--GAFVDIGG-VDGLLHVSEIS----------WGRVEkPSDVLKVGDEIKVYILDIDKENKK-- 540
|
90
....*....|....*..
gi 16129047 116 lttfISLagSYLVLMPN 132
Cdd:PRK00087 541 ----LSL--SLKKLLPD 551
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
41-110 |
5.82e-03 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 40.80 E-value: 5.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129047 41 IYKGKITRIEPSleAAFVDYGAERHGFLPLKEIAREYFPanysahgrpNIKDVLREGQEVIVQ-IDKEERG 110
Cdd:PRK11824 624 IYEGKVVRIVDF--GAFVEILPGKDGLVHISEIADERVE---------KVEDVLKEGDEVKVKvLEIDKRG 683
|
|
| PRK08059 |
PRK08059 |
general stress protein 13; Validated |
41-112 |
6.27e-03 |
|
general stress protein 13; Validated
Pssm-ID: 181215 [Multi-domain] Cd Length: 123 Bit Score: 37.72 E-value: 6.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129047 41 IYKGKITRIEPSleAAFVDYGAERHGFLPLKEIAREYFPanysahgrpNIKDVLREGQEVIVQI-DKEERGNK 112
Cdd:PRK08059 10 VVTGKVTGIQPY--GAFVALDEETQGLVHISEITHGFVK---------DIHDFLSVGDEVKVKVlSVDEEKGK 71
|
|
| |
