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Conserved domains on  [gi|1083809137|gb|OGI87149|]
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polyribonucleotide nucleotidyltransferase [Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_36_16]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pnp super family cl34166
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
5-702 0e+00

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


The actual alignment was detected with superfamily member COG1185:

Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 848.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   5 EYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKP 84
Cdd:COG1185     1 KKEFELGGRTLTLETGKLAKQADGAVLVRYGDTVVLVTVVASKEPREGIDFFPLTVDYQEKFYAAGKIPGG-FFKREGRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  85 SEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGkYNDENLKI 163
Cdd:COG1185    80 SEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDpENDPDILAMIGASAALAISDIPFNGPIGAVRVG-YIDGEFVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 164 NLAKLRDEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRV 243
Cdd:COG1185   159 NPTVEQLEES-----------DLDLVVAGTKDAILMVEAEAKEVSEEVMLEAIMFGHEAIKKLIEAQEELAAEAGKEKRE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 244 IEKEEIDSQSVKLFNENILPKMPPAIFSgAGK----EKIDELHN-VWNKMVADNFPDREDFAleDNLFDDTENDILHQKA 318
Cdd:COG1185   228 YEPPEVDEELKAAVKELAEDKLKEAYQI-PDKqereEALDAIKEeVLEALAEEEDEEDEKEV--KEAFKKLEKKIVRRRI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPY 395
Cdd:COG1185   305 LEEGIRIDGRKLDEIRPISCEVG----VLprtHGSALFTRGETQALVVATLGTLRDEQIIDGLEGEESKRFMLHYNFPPF 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 396 SSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIA 475
Cdd:COG1185   381 SVGETGRMRGPGRREIGHGALAERALEPVLPSEEEFPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAPVAGIA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 476 MGLMHEtDEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:COG1185   461 MGLIKE-GDKYAVLTDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEP 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 556 RKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEYTVGEV 634
Cdd:COG1185   540 REELSPYAPRIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIEDDGTVKIAATdGEAAEKAIERIEGITAEPEVGEI 619
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDReKSRIGLSIRE 702
Cdd:COG1185   620 YEGKVVRIMDFGAFVEILPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDD-QGRIKLSRKA 686
 
Name Accession Description Interval E-value
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
5-702 0e+00

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 848.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   5 EYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKP 84
Cdd:COG1185     1 KKEFELGGRTLTLETGKLAKQADGAVLVRYGDTVVLVTVVASKEPREGIDFFPLTVDYQEKFYAAGKIPGG-FFKREGRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  85 SEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGkYNDENLKI 163
Cdd:COG1185    80 SEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDpENDPDILAMIGASAALAISDIPFNGPIGAVRVG-YIDGEFVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 164 NLAKLRDEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRV 243
Cdd:COG1185   159 NPTVEQLEES-----------DLDLVVAGTKDAILMVEAEAKEVSEEVMLEAIMFGHEAIKKLIEAQEELAAEAGKEKRE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 244 IEKEEIDSQSVKLFNENILPKMPPAIFSgAGK----EKIDELHN-VWNKMVADNFPDREDFAleDNLFDDTENDILHQKA 318
Cdd:COG1185   228 YEPPEVDEELKAAVKELAEDKLKEAYQI-PDKqereEALDAIKEeVLEALAEEEDEEDEKEV--KEAFKKLEKKIVRRRI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPY 395
Cdd:COG1185   305 LEEGIRIDGRKLDEIRPISCEVG----VLprtHGSALFTRGETQALVVATLGTLRDEQIIDGLEGEESKRFMLHYNFPPF 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 396 SSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIA 475
Cdd:COG1185   381 SVGETGRMRGPGRREIGHGALAERALEPVLPSEEEFPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAPVAGIA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 476 MGLMHEtDEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:COG1185   461 MGLIKE-GDKYAVLTDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEP 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 556 RKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEYTVGEV 634
Cdd:COG1185   540 REELSPYAPRIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIEDDGTVKIAATdGEAAEKAIERIEGITAEPEVGEI 619
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDReKSRIGLSIRE 702
Cdd:COG1185   620 YEGKVVRIMDFGAFVEILPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDD-QGRIKLSRKA 686
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1-704 0e+00

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 821.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   1 MQKKEYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRR 80
Cdd:PRK11824    2 FNKIVKSIEFGGRTLTLETGKLARQANGAVLVRYGDTVVLVTVVASKEPKEGQDFFPLTVDYEEKTYAAGKIPGG-FFKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  81 EGKPSEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGKYNDE 159
Cdd:PRK11824   81 EGRPSEKETLTSRLIDRPIRPLFPKGFRNEVQVVATVLSVDpENDPDILAMIGASAALSISGIPFNGPIAAVRVGYIDGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 160 nLKIN--LAKLrdEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEI 237
Cdd:PRK11824  161 -FVLNptVEEL--EES-----------DLDLVVAGTKDAVLMVESEAKELSEEVMLEAIEFGHEAIQELIDAQEELAAEA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 238 GKeKRVIEKEEIDSQSVKLFNENILPKMPPAIFSGAGKEKIDELHNVWNKmVADNFPDREDFALE----DNLFDDTENDI 313
Cdd:PRK11824  227 GP-KWEWQPPEVDEELKAAVKELAEAKLKEAYQITDKQEREAALDAIKEE-VLEALAAEEEEEEDekeiKEAFKKLEKKI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 314 LHQKAIQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHY 390
Cdd:PRK11824  305 VRRRILEEGIRIDGRKLDEIRPISIEVG----VLprtHGSALFTRGETQALVVATLGTLRDEQIIDGLEGEYKKRFMLHY 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 391 NFPPYSSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAP 470
Cdd:PRK11824  381 NFPPYSVGETGRVGSPGRREIGHGALAERALEPVLPSEEEFPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAP 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 471 VAGIAMGLMHEtDEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQK 550
Cdd:PRK11824  461 VAGIAMGLIKE-GDKYAVLTDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNE 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 551 EIKAPRKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEY 629
Cdd:PRK11824  540 AISEPRAELSPYAPRIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIEDDGTVKIAATdGEAAEAAKERIEGITAEP 619
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 630 TVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSIREAD 704
Cdd:PRK11824  620 EVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKAVL 693
polynuc_phos TIGR03591
polyribonucleotide nucleotidyltransferase; Members of this protein family are ...
9-703 0e+00

polyribonucleotide nucleotidyltransferase; Members of this protein family are polyribonucleotide nucleotidyltransferase, also called polynucleotide phosphorylase. Some members have been shown also to have additional functions as guanosine pentaphosphate synthetase and as poly(A) polymerase (see model TIGR02696 for an exception clade, within this family). [Transcription, Degradation of RNA]


Pssm-ID: 274664 [Multi-domain]  Cd Length: 688  Bit Score: 770.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   9 EIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKPSEDA 88
Cdd:TIGR03591   1 EYGGRTLTLETGKIARQADGAVVVRYGDTVVLVTAVAAKEAKEGQDFFPLTVDYQEKFYAAGKIPGG-FFKREGRPSEKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  89 ILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGkYNDENLKIN--L 165
Cdd:TIGR03591  80 TLTSRLIDRPIRPLFPKGFRNEVQVVATVLSYDpENDPDILAIIGASAALAISGIPFNGPIAAVRVG-YIDGQYVLNptV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 166 AKLrdEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRVIE 245
Cdd:TIGR03591 159 DEL--EKS-----------DLDLVVAGTKDAVLMVESEAKELSEEVMLGAILFGHEAIQPVIEAIEELAKEAGKEKREFE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 246 KEEIDSQSVKLFNENILPKMPPAIFSGAGK-EKIDELHNVWNKMVADNFPDREDFALEDN------LFDDTENDILHQKA 318
Cdd:TIGR03591 226 PPEVDEELKAKVKELAEEAVLKAAYQITEKqERYAALDAIKEEVLEALAAEEEDEELAYRekeikeAFKDLEKKIVRERI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPY 395
Cdd:TIGR03591 306 LKEGKRIDGRDLDTIRPISIEVG----VLprtHGSALFTRGETQALVVTTLGTERDEQIIDDLEGEYRKRFMLHYNFPPY 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 396 SSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIA 475
Cdd:TIGR03591 382 SVGEVGRLGGPGRREIGHGALAERALKAVLPSEEEFPYTIRVVSEILESNGSSSMASVCGGSLALMDAGVPIKAPVAGIA 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 476 MGLMHETDEkYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:TIGR03591 462 MGLIKEGDE-YAVLSDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREIMEQALEQAKEGRLHILDKMNKVISEP 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 556 RKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEYTVGEV 634
Cdd:TIGR03591 541 RAELSPYAPRIETIKINPDKIRDVIGPGGKVIREITEETGAKIDIEDDGTVKIAASdGEAAEAAIKMIEGITAEPEVGKI 620
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDReKSRIGLSIREA 703
Cdd:TIGR03591 621 YEGKVVRIMDFGAFVEILPGKDGLVHISEIANERVEKVEDVLKEGDEVKVKVLEIDR-QGRIKLSRKAV 688
RNase_PH_PNPase_2 cd11364
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase ...
332-555 1.09e-122

Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.


Pssm-ID: 206769 [Multi-domain]  Cd Length: 223  Bit Score: 364.95  E-value: 1.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 332 ELRDIYAQAGgVSAVLHGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPYSSGETGRAGFTNRREV 411
Cdd:cd11364     1 EIRPISCEVG-LLPRTHGSALFTRGETQVLCTVTLGTLEDAQKIDSLGGEKSKRFMLHYNFPPYSVGETGRVGGPGRREI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 412 GHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIAMGLMHETDEKYKILTD 491
Cdd:cd11364    80 GHGALAERALLPVLPSPEDFPYTIRVVSEVLESNGSSSMASVCGGSLALMDAGVPIKAPVAGIAMGLITEGIDDYRVLTD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083809137 492 IQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:cd11364   160 ILGLEDHLGDMDFKVAGTRDGITALQMDIKIPGITLEIMREALQQAKEGRLHILDIMEKAISEP 223
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
18-143 6.81e-30

3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components contain a copy of this domain. A hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.


Pssm-ID: 426074 [Multi-domain]  Cd Length: 129  Bit Score: 114.61  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  18 IFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFF--NLTVDYVEKFYATGKIlgsrfmRREGKPSEDAILASRVI 95
Cdd:pfam01138   7 IETGVLSQADGSALVELGDTKVLATVTGPIEPKEDRDFApgRLTVEYELAPFASGER------PGEGRPSEREIEISRLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1083809137  96 DRTLRPLF--DQSIRHAVQVIVTVISvDDNDPVILAVNAASLALAVSNIP 143
Cdd:pfam01138  81 DRALRPSIplEGYPRWTIRIDVTVLS-SDGSLLDAAINAASLALADAGIP 129
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
631-701 4.67e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.80  E-value: 4.67e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083809137  631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
629-705 4.51e-17

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 77.47  E-value: 4.51e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 629 YTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77
 
Name Accession Description Interval E-value
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
5-702 0e+00

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 848.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   5 EYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKP 84
Cdd:COG1185     1 KKEFELGGRTLTLETGKLAKQADGAVLVRYGDTVVLVTVVASKEPREGIDFFPLTVDYQEKFYAAGKIPGG-FFKREGRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  85 SEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGkYNDENLKI 163
Cdd:COG1185    80 SEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDpENDPDILAMIGASAALAISDIPFNGPIGAVRVG-YIDGEFVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 164 NLAKLRDEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRV 243
Cdd:COG1185   159 NPTVEQLEES-----------DLDLVVAGTKDAILMVEAEAKEVSEEVMLEAIMFGHEAIKKLIEAQEELAAEAGKEKRE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 244 IEKEEIDSQSVKLFNENILPKMPPAIFSgAGK----EKIDELHN-VWNKMVADNFPDREDFAleDNLFDDTENDILHQKA 318
Cdd:COG1185   228 YEPPEVDEELKAAVKELAEDKLKEAYQI-PDKqereEALDAIKEeVLEALAEEEDEEDEKEV--KEAFKKLEKKIVRRRI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPY 395
Cdd:COG1185   305 LEEGIRIDGRKLDEIRPISCEVG----VLprtHGSALFTRGETQALVVATLGTLRDEQIIDGLEGEESKRFMLHYNFPPF 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 396 SSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIA 475
Cdd:COG1185   381 SVGETGRMRGPGRREIGHGALAERALEPVLPSEEEFPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAPVAGIA 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 476 MGLMHEtDEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:COG1185   461 MGLIKE-GDKYAVLTDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEP 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 556 RKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEYTVGEV 634
Cdd:COG1185   540 REELSPYAPRIITIKIPPDKIRDVIGPGGKVIRKIIEETGAKIDIEDDGTVKIAATdGEAAEKAIERIEGITAEPEVGEI 619
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDReKSRIGLSIRE 702
Cdd:COG1185   620 YEGKVVRIMDFGAFVEILPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDD-QGRIKLSRKA 686
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
1-704 0e+00

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 821.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   1 MQKKEYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRR 80
Cdd:PRK11824    2 FNKIVKSIEFGGRTLTLETGKLARQANGAVLVRYGDTVVLVTVVASKEPKEGQDFFPLTVDYEEKTYAAGKIPGG-FFKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  81 EGKPSEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGKYNDE 159
Cdd:PRK11824   81 EGRPSEKETLTSRLIDRPIRPLFPKGFRNEVQVVATVLSVDpENDPDILAMIGASAALSISGIPFNGPIAAVRVGYIDGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 160 nLKIN--LAKLrdEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEI 237
Cdd:PRK11824  161 -FVLNptVEEL--EES-----------DLDLVVAGTKDAVLMVESEAKELSEEVMLEAIEFGHEAIQELIDAQEELAAEA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 238 GKeKRVIEKEEIDSQSVKLFNENILPKMPPAIFSGAGKEKIDELHNVWNKmVADNFPDREDFALE----DNLFDDTENDI 313
Cdd:PRK11824  227 GP-KWEWQPPEVDEELKAAVKELAEAKLKEAYQITDKQEREAALDAIKEE-VLEALAAEEEEEEDekeiKEAFKKLEKKI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 314 LHQKAIQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHY 390
Cdd:PRK11824  305 VRRRILEEGIRIDGRKLDEIRPISIEVG----VLprtHGSALFTRGETQALVVATLGTLRDEQIIDGLEGEYKKRFMLHY 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 391 NFPPYSSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAP 470
Cdd:PRK11824  381 NFPPYSVGETGRVGSPGRREIGHGALAERALEPVLPSEEEFPYTIRVVSEILESNGSSSMASVCGSSLALMDAGVPIKAP 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 471 VAGIAMGLMHEtDEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQK 550
Cdd:PRK11824  461 VAGIAMGLIKE-GDKYAVLTDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNE 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 551 EIKAPRKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEY 629
Cdd:PRK11824  540 AISEPRAELSPYAPRIETIKIPPDKIRDVIGPGGKTIREITEETGAKIDIEDDGTVKIAATdGEAAEAAKERIEGITAEP 619
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 630 TVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSIREAD 704
Cdd:PRK11824  620 EVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKAVL 693
polynuc_phos TIGR03591
polyribonucleotide nucleotidyltransferase; Members of this protein family are ...
9-703 0e+00

polyribonucleotide nucleotidyltransferase; Members of this protein family are polyribonucleotide nucleotidyltransferase, also called polynucleotide phosphorylase. Some members have been shown also to have additional functions as guanosine pentaphosphate synthetase and as poly(A) polymerase (see model TIGR02696 for an exception clade, within this family). [Transcription, Degradation of RNA]


Pssm-ID: 274664 [Multi-domain]  Cd Length: 688  Bit Score: 770.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   9 EIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKPSEDA 88
Cdd:TIGR03591   1 EYGGRTLTLETGKIARQADGAVVVRYGDTVVLVTAVAAKEAKEGQDFFPLTVDYQEKFYAAGKIPGG-FFKREGRPSEKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  89 ILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGkYNDENLKIN--L 165
Cdd:TIGR03591  80 TLTSRLIDRPIRPLFPKGFRNEVQVVATVLSYDpENDPDILAIIGASAALAISGIPFNGPIAAVRVG-YIDGQYVLNptV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 166 AKLrdEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRVIE 245
Cdd:TIGR03591 159 DEL--EKS-----------DLDLVVAGTKDAVLMVESEAKELSEEVMLGAILFGHEAIQPVIEAIEELAKEAGKEKREFE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 246 KEEIDSQSVKLFNENILPKMPPAIFSGAGK-EKIDELHNVWNKMVADNFPDREDFALEDN------LFDDTENDILHQKA 318
Cdd:TIGR03591 226 PPEVDEELKAKVKELAEEAVLKAAYQITEKqERYAALDAIKEEVLEALAAEEEDEELAYRekeikeAFKDLEKKIVRERI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVL---HGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPY 395
Cdd:TIGR03591 306 LKEGKRIDGRDLDTIRPISIEVG----VLprtHGSALFTRGETQALVVTTLGTERDEQIIDDLEGEYRKRFMLHYNFPPY 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 396 SSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIA 475
Cdd:TIGR03591 382 SVGEVGRLGGPGRREIGHGALAERALKAVLPSEEEFPYTIRVVSEILESNGSSSMASVCGGSLALMDAGVPIKAPVAGIA 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 476 MGLMHETDEkYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:TIGR03591 462 MGLIKEGDE-YAVLSDILGDEDHLGDMDFKVAGTRDGITALQMDIKIDGITREIMEQALEQAKEGRLHILDKMNKVISEP 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 556 RKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHEYTVGEV 634
Cdd:TIGR03591 541 RAELSPYAPRIETIKINPDKIRDVIGPGGKVIREITEETGAKIDIEDDGTVKIAASdGEAAEAAIKMIEGITAEPEVGKI 620
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDReKSRIGLSIREA 703
Cdd:TIGR03591 621 YEGKVVRIMDFGAFVEILPGKDGLVHISEIANERVEKVEDVLKEGDEVKVKVLEIDR-QGRIKLSRKAV 688
pppGpp_PNP TIGR02696
guanosine pentaphosphate synthetase I/polynucleotide phosphorylase; Sohlberg, et al. present ...
22-690 1.41e-178

guanosine pentaphosphate synthetase I/polynucleotide phosphorylase; Sohlberg, et al. present characterization of two proteins from Streptomyces coelicolor. The protein in this family was shown to have poly(A) polymerase activity and may be responsible for polyadenylating RNA in this species. Reference 2 showed that a nearly identical plasmid-encoded protein from Streptomyces antibioticus is a bifunctional enzyme that acts also as a guanosine pentaphosphate synthetase.


Pssm-ID: 131743 [Multi-domain]  Cd Length: 719  Bit Score: 526.69  E-value: 1.41e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  22 LAEQAHGSVMLKY-GETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKPSEDAILASRVIDRTLR 100
Cdd:TIGR02696  26 LARQAAGSVVAYLdDETMLLSATTASKQPKDQFDFFPLTVDVEERMYAAGRIPGS-FFRREGRPSTDAILTCRLIDRPLR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 101 PLFDQSIRHAVQVIVTVISVDDNDPV-ILAVNAASLALAVSNIPWNGPIGCVRIGKYNDENLKINLAKLRDEDSlngnlt 179
Cdd:TIGR02696 105 PSFVKGLRNEVQVVVTVLSLNPDHLYdVVAINAASASTQLAGLPFSGPIGGVRVALIDGQWVAFPTHEQLEGAV------ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 180 gemqykFDLTVCGK---NGN--INMIEASAREVSEKELEKALEEASKE------------ITKLENFQKNIVKEIGKEKr 242
Cdd:TIGR02696 179 ------FDMVVAGRvleNGDvaIMMVEAEATEKTWDLVKGGAEAPTEEvvaegleaakpfIKVLCRAQADLAEKAAKPT- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 243 viekEEID-----SQSVKLFNENILPKMPPAIFSGAGK----EKIDELHNVWNKMVADNFPDRE-DFAledNLFDDTEND 312
Cdd:TIGR02696 252 ----GEFPlfpdyQDDVYEAVEGAVKDELSAALTIAGKqereEALDEVKALVAAKLAEQFEGREkEIS---AAYRAVTKK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 313 ILHQKAIQENKRADGRGMDELRDIYAQAGGVSAVlHGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNF 392
Cdd:TIGR02696 325 LVRERVLTEGVRIDGRGVTDIRPLDAEVQVIPRV-HGSALFERGETQILGVTTLNMLKMEQQIDSLSPETSKRYMHHYNF 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 393 PPYSSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVA 472
Cdd:TIGR02696 404 PPYSTGETGRVGSPKRREIGHGALAERALVPVLPSREEFPYAIRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLKAPVA 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 473 GIAMGLMHET---DEKYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQ 549
Cdd:TIGR02696 484 GIAMGLISDEvdgETRYVALTDILGAEDAFGDMDFKVAGTSEFVTALQLDTKLDGIPASVLASALKQARDARLAILDVMA 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 550 KEIKAPrKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYF-TGKGDGAEKAKSIVLEMTH- 627
Cdd:TIGR02696 564 EAIDTP-DEMSPYAPRIITVKIPVDKIGEVIGPKGKMINQIQDETGAEISIEDDGTVYIgAADGPSAEAARAMINAIANp 642
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 628 -EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPF----RVERVSDIIKEGMIVPVKVISID 690
Cdd:TIGR02696 643 tMPEVGERFLGTVVKTTAFGAFVSLLPGKDGLLHISQIRKLaggkRVENVEDVLSVGQKIQVEIADID 710
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
22-701 4.30e-140

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 433.17  E-value: 4.30e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  22 LAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGKPSEDAILASRVIDRTLRP 101
Cdd:PLN00207   98 IGRQASGSVTVTDGETIVYTSVCLADVPSEPSDFFPLSVHYQERFSAAGRTSGG-FFKREGRTKDHEVLICRLIDRPLRP 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 102 LFDQSIRHAVQVIVTVISVDD-NDPVILAVNAASLALAVSNIPWNGPIGCVRIGKYNDENLkINLAKLRDEDSlngnltg 180
Cdd:PLN00207  177 TMPKGFYHETQILSWVLSYDGlHSPDSLAVTAAGIAVALSEVPNLKAIAGVRVGLIGGKFI-VNPTTKEMEES------- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 181 emqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKRV---------IEK--EEI 249
Cdd:PLN00207  249 ----ELDLIMAGTDSAILMIEGYCNFLPEEKLLEAVEVGQDAVRAICKEIEVLVKKCGKPKMLdaiklpppeLYKhvKEI 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 250 DSQS-VKLFNenILPKMPPA------------IFSGAG-------------KEKIDELHNVWNKMVADNFPDREDFALED 303
Cdd:PLN00207  325 AGDElVKALQ--IRGKIPRRkalssleekvlsILTEEGyvskdesfgtsetRADLLEDEDEDEEVVVDGEVDEGDVHIKP 402
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 304 N----------------LFDDTENDILHQKAIQENKRADGRGMDELRDIYAQAGGVSAVlHGSGIFYRGGTHVLSVLTLG 367
Cdd:PLN00207  403 IprksspllfsevdvklVFKEVTSKFLRRRIVEGGKRSDGRTPDEIRPINSSCGLLPRA-HGSALFTRGETQALAVVTLG 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 368 GPEDRHSIDGMQTKLE-KRFMHHYNFPPYSSGETGRAGFTNRREVGHGALAEKALAMVLPPLSEFPYTIRVVSESMASNG 446
Cdd:PLN00207  482 DKQMAQRIDNLVDADEvKRFYLQYSFPPSCVGEVGRIGAPSRREIGHGMLAERALEPILPSEDDFPYTIRVESTITESNG 561
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 447 STSQASICASTLALMDGGVPILAPVAGIAMGLMHETDE-----KYKILTDIQGPEDHHGDMDFKVAGTRKGVTAIQLDVK 521
Cdd:PLN00207  562 SSSMASVCGGCLALQDAGVPVKCPIAGIAMGMVLDTEEfggdgSPLILSDITGSEDASGDMDFKVAGNEDGITAFQMDIK 641
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 522 VEGVPIKILGEAMEQAKNARIIILDKIQKEIKAPRKEISPNAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAE-ITI 600
Cdd:PLN00207  642 VGGITLPIMERALLQAKDGRKHILAEMSKCSPPPSKRLSKYAPLIHIMKVKPEKVNMIIGSGGKKVKSIIEETGVEaIDT 721
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 601 EDDGTVYFTGKG-DGAEKAKSIVLEMTHEYTVGEVLKG-EVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKE 678
Cdd:PLN00207  722 QDDGTVKITAKDlSSLEKSKAIISSLTMVPTVGDIYRNcEIKSIAPYGAFVEIAPGREGLCHISELSSNWLAKPEDAFKV 801
                         730       740
                  ....*....|....*....|...
gi 1083809137 679 GMIVPVKVISIDrEKSRIGLSIR 701
Cdd:PLN00207  802 GDRIDVKLIEVN-DKGQLRLSRR 823
RNase_PH_PNPase_2 cd11364
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase ...
332-555 1.09e-122

Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.


Pssm-ID: 206769 [Multi-domain]  Cd Length: 223  Bit Score: 364.95  E-value: 1.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 332 ELRDIYAQAGgVSAVLHGSGIFYRGGTHVLSVLTLGGPEDRHSIDGMQTKLEKRFMHHYNFPPYSSGETGRAGFTNRREV 411
Cdd:cd11364     1 EIRPISCEVG-LLPRTHGSALFTRGETQVLCTVTLGTLEDAQKIDSLGGEKSKRFMLHYNFPPYSVGETGRVGGPGRREI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 412 GHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIAMGLMHETDEKYKILTD 491
Cdd:cd11364    80 GHGALAERALLPVLPSPEDFPYTIRVVSEVLESNGSSSMASVCGGSLALMDAGVPIKAPVAGIAMGLITEGIDDYRVLTD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083809137 492 IQGPEDHHGDMDFKVAGTRKGVTAIQLDVKVEGVPIKILGEAMEQAKNARIIILDKIQKEIKAP 555
Cdd:cd11364   160 ILGLEDHLGDMDFKVAGTRDGITALQMDIKIPGITLEIMREALQQAKEGRLHILDIMEKAISEP 223
RNase_PH_PNPase_1 cd11363
Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase ...
4-244 1.78e-82

Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors. It is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.


Pssm-ID: 206768 [Multi-domain]  Cd Length: 229  Bit Score: 260.91  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137   4 KEYSVEIGGKNLTAIFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFNLTVDYVEKFYATGKILGSrFMRREGK 83
Cdd:cd11363     1 KVFEVLVGGRTLTFETGKLAKQADGSVVVQYGDTVVLVTAVSSKKPKEGIDFFPLTVDYREKLYAAGKIPGG-FFKREGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  84 PSEDAILASRVIDRTLRPLFDQSIRHAVQVIVTVISVD-DNDPVILAVNAASLALAVSNIPWNGPIGCVRIGKYNDENLk 162
Cdd:cd11363    80 PSEKEILTSRLIDRPIRPLFPKGFRNEVQVIATVLSVDgVNDPDVLAINGASAALSLSDIPFNGPVGAVRVGRIDGEFV- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 163 INLAKLRDEDSlngnltgemqyKFDLTVCGKNGNINMIEASAREVSEKELEKALEEASKEITKLENFQKNIVKEIGKEKR 242
Cdd:cd11363   159 VNPTREELEES-----------DLDLVVAGTKDAVLMVEAGAKEVSEEDMLEAIKFGHEAIQQLIAAQEELAAEVGKEKR 227

                  ..
gi 1083809137 243 VI 244
Cdd:cd11363   228 EY 229
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
18-143 6.81e-30

3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components contain a copy of this domain. A hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.


Pssm-ID: 426074 [Multi-domain]  Cd Length: 129  Bit Score: 114.61  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  18 IFTDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFF--NLTVDYVEKFYATGKIlgsrfmRREGKPSEDAILASRVI 95
Cdd:pfam01138   7 IETGVLSQADGSALVELGDTKVLATVTGPIEPKEDRDFApgRLTVEYELAPFASGER------PGEGRPSEREIEISRLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1083809137  96 DRTLRPLF--DQSIRHAVQVIVTVISvDDNDPVILAVNAASLALAVSNIP 143
Cdd:pfam01138  81 DRALRPSIplEGYPRWTIRIDVTVLS-SDGSLLDAAINAASLALADAGIP 129
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
628-703 3.46e-22

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 92.55  E-value: 3.46e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSIREA 703
Cdd:COG1098     2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSID-EDGKISLSIKQA 76
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
632-700 5.45e-22

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: 89.91  E-value: 5.45e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSI 700
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISLSR 68
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
628-705 5.82e-22

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 100.79  E-value: 5.82e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:PRK00087  559 KYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISWKRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEE 636
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
332-466 6.17e-22

3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components contain a copy of this domain. A hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.


Pssm-ID: 426074 [Multi-domain]  Cd Length: 129  Bit Score: 91.88  E-value: 6.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 332 ELRDIYAQAGGVSAVlHGSGIFYRGGTHVLSVLTLGGPEDRhsidgMQTKLEKRFMHHYNFPPYSSGETGRAGFTNRREV 411
Cdd:pfam01138   1 ELRPIEIETGVLSQA-DGSALVELGDTKVLATVTGPIEPKE-----DRDFAPGRLTVEYELAPFASGERPGEGRPSEREI 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 412 GHGALAEKALAMVLPPLSEFPYTIRVVSESMASNGSTSQASICASTLALMDGGVP 466
Cdd:pfam01138  75 EISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
628-703 2.52e-20

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: 93.19  E-value: 2.52e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPF-RVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREA 703
Cdd:COG0539   271 KYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTkRVAHPSDVVKVGDEVEVKVLDIDPEERRISLSIKQL 347
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
616-701 5.48e-20

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: 92.03  E-value: 5.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 616 EKAKSIVLEmthEYTVGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSR 695
Cdd:COG0539   177 EEKREELLE---KLEEGDVVEGTVKNITDFGAFVDLGGV-DGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDREKER 252

                  ....*.
gi 1083809137 696 IGLSIR 701
Cdd:COG0539   253 ISLSLK 258
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
319-551 1.59e-19

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 88.54  E-value: 1.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 319 IQENKRADGRGMDELRDIYAQAGgvsaVLH---GSGIFYRGGTHVLSVLTlgGPED---RHSIDGMQTKLEKRfmhhYNF 392
Cdd:PRK03983   10 LEDGLRLDGRKPDELRPIKIEVG----VLKnadGSAYLEWGNNKIIAAVY--GPREmhpRHLQLPDRAVLRVR----YNM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 393 PPYSSGETGRAGfTNRREVGHGALAEKALAMVLPpLSEFPYT-IRVVSESMASNGSTSQASICASTLALMDGGVPILAPV 471
Cdd:PRK03983   80 APFSVDERKRPG-PDRRSIEISKVIREALEPAIM-LELFPRTvIDVFIEVLQADAGTRVAGITAASLALADAGIPMRDLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 472 AGIAMGLMHEtdekyKILTDIQGPEDHHGDMDFKVAGTRKG--VTAIQLDVKVEGVPIKilgEAMEQAKNArIIILDKIQ 549
Cdd:PRK03983  158 AGCAVGKVDG-----VIVLDLNKEEDNYGEADMPVAIMPRLgeITLLQLDGNLTREEFL---EALELAKKG-IKRIYQLQ 228

                  ..
gi 1083809137 550 KE 551
Cdd:PRK03983  229 RE 230
rpsA PRK06676
30S ribosomal protein S1; Reviewed
631-703 2.74e-18

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 87.62  E-value: 2.74e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREA 703
Cdd:PRK06676  192 EGDVVEGTVARLTDFGAFVDIGGV-DGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIDWETERISLSLKDT 263
RNase_PH_archRRP41 cd11366
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ...
332-551 3.83e-18

RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA.


Pssm-ID: 206771 [Multi-domain]  Cd Length: 214  Bit Score: 83.54  E-value: 3.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 332 ELRDIYAQAGgvsaVLH---GSGIFYRGGTHVLSVLTlgGPED---RHSIDGMQTKLEKRfmhhYNFPPYSSGETGRAGf 405
Cdd:cd11366     1 ELRPIKIEVG----VLKnadGSAYVEWGNNKIIAAVY--GPREvhpRHLQLPDRAVIRVR----YNMAPFSVDERKRPG- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 406 TNRREVGHGALAEKALAMVLPpLSEFPYT-IRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIAMGLMHEtde 484
Cdd:cd11366    70 PDRREIEISKVIKEALEPAII-LEEFPRTaIDVFVEVLQADAGTRVAGLNAASLALADAGIPMRDLVAACAAGKVDG--- 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 485 kyKILTDIQGPEDHHGDMDFKVAGTRKG--VTAIQLDVKVEGVPIKilgEAMEQAKNARIIILDkIQKE 551
Cdd:cd11366   146 --KIVLDLNKEEDNYGEADMPIAMMPNLgeITLLQLDGDLTPDEFK---QAIELAKKGCKRIYE-LQKE 208
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
631-701 4.67e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.80  E-value: 4.67e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083809137  631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK08059 PRK08059
general stress protein 13; Validated
625-702 7.85e-18

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 80.09  E-value: 7.85e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 625 MTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIRE 702
Cdd:PRK08059    1 MMSQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRA 78
rpsA PRK06676
30S ribosomal protein S1; Reviewed
624-704 2.73e-17

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 84.54  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 624 EMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREA 703
Cdd:PRK06676  270 GVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISHKHIATPSEVLEEGQEVKVKVLEVNEEEKRISLSIKAL 349

                  .
gi 1083809137 704 D 704
Cdd:PRK06676  350 E 350
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
632-704 4.00e-17

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: 76.51  E-value: 4.00e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSF---TDGMVHISELAPFRVER-VSDIIKEGMIVPVKVISIDREKsrIGLSIREAD 704
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLEGLkgrKEGLVHISQLSFEGRVAnPSDVVKRGQKVKVKVISIQNGK--ISLSMKDVD 75
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
629-705 4.51e-17

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 77.47  E-value: 4.51e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 629 YTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
631-702 1.02e-16

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 84.23  E-value: 1.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIRE 702
Cdd:PRK00087  477 EGDVVEGEVKRLTDFGAFVDIGGV-DGLLHVSEISWGRVEKPSDVLKVGDEIKVYILDIDKENKKLSLSLKK 547
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
631-701 1.24e-16

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: 74.93  E-value: 1.24e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTD--GMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:cd04452     3 EGELVVVTVKSIADMGAYVSLLEYGNieGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
632-699 1.91e-16

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: 74.19  E-value: 1.91e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLS 699
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
631-699 4.43e-16

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: 73.05  E-value: 4.43e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLS 699
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGV-DGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
RNase_PH cd11358
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ...
333-541 9.36e-16

RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Evolutionarily related members can be fond in prokaryotes, archaea, and eukaryotes. Bacterial ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain and is involved in mRNA degradation in a 3'-5' direction. Archaeal exosomes contain two individually encoded RNase PH-like 3'-5' exoribonucleases and are required for 3' processing of the 5.8S rRNA. The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and Rrp6, which are hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. All members of the RNase PH-like family form ring structures by oligomerization of six domains or subunits, except for a total of 3 subunits with tandem repeats in the case of PNPase, with a central channel through which the RNA substrate must pass to gain access to the phosphorolytic active sites.


Pssm-ID: 206766 [Multi-domain]  Cd Length: 218  Bit Score: 76.98  E-value: 9.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 333 LRDIYAQAGGVSAVlHGSGIFYRGGTHVLSVLTLGGPEDrhsiDGMQTKLEKRFMHHYNFPPYSSGETgRAGFTNRREVG 412
Cdd:cd11358     1 FRPVEIETGVLNQA-DGSALVKLGNTKVICAVTGPIVEP----DKLERPDKGTLYVNVEISPGAVGER-RQGPPGDEEME 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 413 HGALAEKAL-AMVLPPLS--EFPYTIRVVSESMASNGSTSQASICASTLALMDGGVP-------------ILAPVAGIAM 476
Cdd:cd11358    75 ISRLLERTIeASVILDKStrKPSWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPrvfvderspplllMKDLIVAVSV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083809137 477 GLmhetDEKYKILTDIQGPEDHHGDMDFKVAGTRKG-VTAIQLDVKVEGVPIKILgEAMEQAKNAR 541
Cdd:cd11358   155 GG----ISDGVLLLDPTGEEEELADSTLTVAVDKSGkLCLLSKVGGGSLDTEEIK-ECLELAKKRS 215
PRK05807 PRK05807
RNA-binding protein S1;
631-705 1.10e-15

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 74.40  E-value: 1.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTdGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSIREADK 705
Cdd:PRK05807    5 AGSILEGTVVNITNFGAFVEVEGKT-GLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQAMK 77
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
632-701 1.62e-15

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 71.55  E-value: 1.62e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKsRIGLSIR 701
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDARG-RISLSIK 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
631-705 3.14e-15

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 79.68  E-value: 3.14e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:COG2183   641 PGMILEGTVTNVTDFGAFVDIGVHQDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDE 715
rpsA PRK06299
30S ribosomal protein S1; Reviewed
616-700 3.41e-15

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 79.05  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 616 EKAKSIVLEMTHEytvGEVLKGEVVKIADFGAFVKLNSfTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSR 695
Cdd:PRK06299  189 AEEREELLENLEE---GQVVEGVVKNITDYGAFVDLGG-VDGLLHITDISWKRVNHPSEVVNVGDEVKVKVLKFDKEKKR 264

                  ....*
gi 1083809137 696 IGLSI 700
Cdd:PRK06299  265 VSLGL 269
rpsA PRK06299
30S ribosomal protein S1; Reviewed
628-705 6.50e-15

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 78.28  E-value: 6.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:PRK06299  457 KHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDE 534
rpsA PRK13806
30S ribosomal protein S1; Provisional
631-703 1.08e-14

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 77.07  E-value: 1.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKS----RIGLSIREA 703
Cdd:PRK13806  202 EGDVVEGTVTRLAPFGAFVELAPGVEGMVHISELSWSRVQKADEAVSVGDTVRVKVLGIERAKKgkglRISLSIKQA 278
PRK08582 PRK08582
RNA-binding protein S1;
631-703 2.18e-14

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 70.45  E-value: 2.18e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREkSRIGLSIREA 703
Cdd:PRK08582    5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDD-GKIGLSIKKA 76
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
635-699 2.49e-14

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: 68.18  E-value: 2.49e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 635 LKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLS 699
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
rpsA PRK13806
30S ribosomal protein S1; Provisional
629-703 2.68e-14

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 75.92  E-value: 2.68e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083809137 629 YTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELA-PFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREA 703
Cdd:PRK13806  290 LKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSwTRRVNKPEDVVAPGDAVAVKIKDIDPAKRRISLSLRDA 365
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
631-700 3.05e-14

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: 68.08  E-value: 3.05e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSI 700
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
RNase_PH cd11358
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ...
17-174 6.28e-14

RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Evolutionarily related members can be fond in prokaryotes, archaea, and eukaryotes. Bacterial ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain and is involved in mRNA degradation in a 3'-5' direction. Archaeal exosomes contain two individually encoded RNase PH-like 3'-5' exoribonucleases and are required for 3' processing of the 5.8S rRNA. The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and Rrp6, which are hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. All members of the RNase PH-like family form ring structures by oligomerization of six domains or subunits, except for a total of 3 subunits with tandem repeats in the case of PNPase, with a central channel through which the RNA substrate must pass to gain access to the phosphorolytic active sites.


Pssm-ID: 206766 [Multi-domain]  Cd Length: 218  Bit Score: 71.59  E-value: 6.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  17 AIFTDLAEQAHGSVMLKYGETIVLATVC---MSKDKQNGLGFFNLTVDYVEKFYATGKilgsrfmRREGKPSEDAILASR 93
Cdd:cd11358     5 EIETGVLNQADGSALVKLGNTKVICAVTgpiVEPDKLERPDKGTLYVNVEISPGAVGE-------RRQGPPGDEEMEISR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  94 VIDRTLRPLF--DQSIRH---AVQVIVTVISVDDNdPVILAVNAASLALAVSNIPW-------------NGPIGCVRIGK 155
Cdd:cd11358    78 LLERTIEASVilDKSTRKpswVLYVDIQVLSRDGG-LLDACWNAAIAALKDAGIPRvfvderspplllmKDLIVAVSVGG 156
                         170
                  ....*....|....*....
gi 1083809137 156 YNDENLKINLakLRDEDSL 174
Cdd:cd11358   157 ISDGVLLLDP--TGEEEEL 173
rpsA PRK07899
30S ribosomal protein S1; Reviewed
626-704 7.78e-14

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 74.31  E-value: 7.78e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 626 THeyTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREAD 704
Cdd:PRK07899  290 TH--AIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELAERHVEVPEQVVQVGDEVFVKVIDIDLERRRISLSLKQAN 366
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
615-702 9.14e-14

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: 74.39  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 615 AEKAKSIVLEMTHEytvGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKS 694
Cdd:TIGR00717 174 RSQAREELLENLKE---GDVVKGVVKNITDFGAFVDLGGV-DGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKG 249

                  ....*...
gi 1083809137 695 RIGLSIRE 702
Cdd:TIGR00717 250 RISLSLKQ 257
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
324-553 1.25e-13

RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206775 [Multi-domain]  Cd Length: 226  Bit Score: 70.65  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 324 RADGRGMDELRDIYAQAGgVSAVLHGSGIFYRGGTHVLSVLTlgGP-EDRHSIDGMQTKLEKRFmhHYNFPPYSSGETGR 402
Cdd:cd11370     3 RLDGRRPNELRRIRCRIG-VFSSADGSAYLEQGNTKVLAAVY--GPhEPRNRSQALHDRAVVNC--EYSMATFSTGERKR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 403 AGFTNRREVGHGALAEKALAMVLppLSE-FPYT-IRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIAMGLMH 480
Cdd:cd11370    78 RGKGDRRSTELSLAIRQTFEAVI--LTHlYPRSqIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGYLD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 481 ETdekykILTDIQGPEDHHGDMDFKVA--GTRKGVTAIQLDVKvegVPIKILGEAMEQAKNARIIILDKIQKEIK 553
Cdd:cd11370   156 ST-----PLLDLNYLEESGDLPDLTVAvlPKSDKVVLLQMESR---LHLDRLEKVLELAIEGCKVIREIMDEVVR 222
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
631-701 6.86e-13

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 69.47  E-value: 6.86e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTD--GMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK03987    8 EGELVVGTVKEVKDFGAFVTLDEYPGkeGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
SUI2 COG1093
Translation initiation factor 2, alpha subunit (eIF-2alpha) [Translation, ribosomal structure ...
631-701 1.87e-12

Translation initiation factor 2, alpha subunit (eIF-2alpha) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, alpha subunit (eIF-2alpha) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440710 [Multi-domain]  Cd Length: 259  Bit Score: 67.92  E-value: 1.87e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTD--GMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:COG1093    10 EGELVVGTVKEVKDFGAYVTLDEYEGkeGFIHISEVASGWIKNIRDYVREGQKVVCKVLRVDPKRGHIDLSLK 82
rpsA PRK06299
30S ribosomal protein S1; Reviewed
628-701 4.78e-12

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 69.04  E-value: 4.78e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVER-VSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK06299  283 KYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKhPSKVVSVGQEVEVMVLEIDEEKRRISLGLK 357
rpsA PRK06299
30S ribosomal protein S1; Reviewed
624-701 5.54e-12

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 69.04  E-value: 5.54e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 624 EMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFR-VERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK06299  366 EFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDKkGEEAVELYKKGDEVEAVVLKVDVEKERISLGIK 444
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
562-628 9.43e-12

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 60.95  E-value: 9.43e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 562 NAPKILIIKINTDMIGMVIGGGGKTIKEIKEKTGAEITIEDDGTVYFTGK-GDGAEKAKSIVLEMTHE 628
Cdd:cd02393     1 YAPRITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIEDDGTVTIFATdKESAEAAKAMIEDIVAE 68
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
633-700 1.22e-11

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: 60.57  E-value: 1.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 633 EVLKGEVVKIADFGAFVKLNSF-TDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDrEKSRIGLSI 700
Cdd:cd05686     5 QIFKGEVASVTEYGAFVKIPGCrKQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGRE-MKDKMKLSL 72
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
632-698 2.92e-11

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: 59.43  E-value: 2.92e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELA-PFRVERVSDIIKEGMIVPVKVISIDREKSRIGL 698
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISwTQRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
630-707 3.27e-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: 59.65  E-value: 3.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137 630 TVGEVLKGEVVKIADFGAFVKL-NSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREAdkYF 707
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIdGTNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLKAS--YF 77
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
624-701 3.38e-11

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: 66.30  E-value: 3.38e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 624 EMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:TIGR00717 439 KFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
623-703 9.51e-11

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: 64.76  E-value: 9.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 623 LEMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELA-PFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:TIGR00717 264 EAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSwVKKNSHPSKVVKKGDEVEVMILDIDPERRRLSLGLK 343

                  ..
gi 1083809137 702 EA 703
Cdd:TIGR00717 344 QC 345
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
631-708 2.08e-09

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 55.86  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR--EADKYFF 708
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRtlEEEKQHF 82
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
629-702 3.77e-09

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 59.75  E-value: 3.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083809137 629 YTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKE-GMIVPVKVISIDREKSRIGLSIRE 702
Cdd:TIGR00717 357 HPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKkGDEIEAVVLAVDKEKKRISLGVKQ 431
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
632-701 6.11e-09

S1_RPS1_repeat_ec6: 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 6 (ec6) 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: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 53.04  E-value: 6.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIK 70
rpsA PRK07899
30S ribosomal protein S1; Reviewed
632-701 6.13e-09

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 58.90  E-value: 6.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSfTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK07899  209 GQVRKGVVSSIVNFGAFVDLGG-VDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDMDRERVSLSLK 277
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
623-702 1.46e-08

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 58.18  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 623 LEMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPF-RVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK12269  570 LEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVkKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLK 649

                  .
gi 1083809137 702 E 702
Cdd:PRK12269  650 Q 650
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
633-703 1.75e-08

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: 52.67  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 633 EVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRV-----------ERVSDIIKEGMIVPVKVISIDR-----EKSRI 696
Cdd:cd04460     1 EVVEGEVVEVVDFGAFVRIGPV-DGLLHISQIMDDYIsydpknkrligEETKRVLKVGDVVRARIVAVSLkerrpRESKI 79

                  ....*..
gi 1083809137 697 GLSIREA 703
Cdd:cd04460    80 GLTMRQP 86
rpsA PRK06676
30S ribosomal protein S1; Reviewed
623-704 8.59e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 54.88  E-value: 8.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 623 LEMTHEYTVGEVLKGEVVKIADFGAFVKL-NSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PRK06676    9 LNSVKEVEVGDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELSNDHIEDINDVVKVGDELEVYVLKVEDGEGNLLLSKR 88

                  ...
gi 1083809137 702 EAD 704
Cdd:PRK06676   89 RLE 91
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
628-705 1.08e-07

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: 54.28  E-value: 1.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 628 EYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISElapFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREADK 705
Cdd:COG0539    15 ELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSE---FSDEPGELEVKVGDEVEVYVEKVEDGEGEIVLSKKKADR 89
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
629-698 2.00e-07

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 48.73  E-value: 2.00e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 629 YTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISEL-------APFRVERVSDiikegmIVPVKVISIDREKSRIGL 698
Cdd:cd05689     1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMdwtnkniHPSKVVSLGD------EVEVMVLDIDEERRRISL 71
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
632-701 2.09e-07

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: 48.68  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
RPB7 COG1095
DNA-directed RNA polymerase, subunit E'/Rpb7 [Transcription]; DNA-directed RNA polymerase, ...
597-701 5.41e-07

DNA-directed RNA polymerase, subunit E'/Rpb7 [Transcription]; DNA-directed RNA polymerase, subunit E'/Rpb7 is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 440712 [Multi-domain]  Cd Length: 171  Bit Score: 50.18  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 597 EITIEDDGTVYFtgkGDGAE------KAKSIVLEMtheytvGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRV- 669
Cdd:COG1095    50 DVKVIGEGKIVP---GDGATyhdvefDALTFKPEL------QEVVEGEVVEVVEFGAFVRIGPI-DGLLHISQIMDDYVd 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1083809137 670 ----------ERVSDIIKEGMIVPVKVISID-REK----SRIGLSIR 701
Cdd:COG1095   120 ydekngrligKESKRTLKVGDVVRARIVAVSlNEKsprdSKIGLTMR 166
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
616-701 6.96e-07

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 52.79  E-value: 6.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 616 EKAKSIVLEMTHEYTVGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSR 695
Cdd:PRK12269  478 ERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGF-DGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKR 556

                  ....*.
gi 1083809137 696 IGLSIR 701
Cdd:PRK12269  557 INLSLK 562
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
631-701 2.34e-06

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 48.67  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFtDGMVHISELAPFRV-----------ERVSDIIKEGMIVPVKVISI-----DREKS 694
Cdd:PRK08563   81 LQEVVEGEVVEVVEFGAFVRIGPV-DGLLHISQIMDDYIsydpkngrligKESKRVLKVGDVVRARIVAVslkerRPRGS 159

                  ....*..
gi 1083809137 695 RIGLSIR 701
Cdd:PRK08563  160 KIGLTMR 166
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
630-701 3.32e-06

S1_Rrp5_repeat_sc10: 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 10 (sc10). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240211 [Multi-domain]  Cd Length: 73  Bit Score: 45.32  E-value: 3.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083809137 630 TVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:cd05706     2 KVGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDYSEALPYKFKKNDIVRACVLSVDVPNKKIALSLR 73
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
631-704 6.24e-06

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 49.56  E-value: 6.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIREAD 704
Cdd:PRK00087  302 RGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEISSLKESVKVGDEIEVKVLKLEDEDGYVVLSKKEAD 375
S1_Rrp5_repeat_hs14 cd05705
S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
632-699 1.25e-05

S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 14 (hs14). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240210 [Multi-domain]  Cd Length: 74  Bit Score: 43.54  E-value: 1.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMV---HISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLS 699
Cdd:cd05705     4 GQLLRGYVSSVTKQGVFFRLSSSIVGRVlfqNVTKYFVSDPSLYNKYLPEGKLLTAKVLSVNSEKNLVELS 74
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
333-483 4.15e-05

RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206777 [Multi-domain]  Cd Length: 199  Bit Score: 45.25  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 333 LRDIYAQAGGVSAVlHGSGIFYRGGTHVLSVLTlgGPEDRHSIDGMQTK--LEKRFmhhynfppyssgetgragftnRRE 410
Cdd:cd11372     1 LRPLSCELGLLSRA-DGSARFSQGDTSVLAAVY--GPIEVKLRKELPDRatLEVIV---------------------RPK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 411 VGHGALAEKALAM----VLPP---LSEFPYT-IRVVSESMASNGSTSQASICASTLALMDGGVPILAPVAGIAMGLMHET 482
Cdd:cd11372    57 SGLPGVKEKLLELllrsTLEPiilLHLHPRTlISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITEDG 136

                  .
gi 1083809137 483 D 483
Cdd:cd11372   137 E 137
RNase_PH_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
17-143 5.43e-05

MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206776 [Multi-domain]  Cd Length: 210  Bit Score: 44.86  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  17 AIF--TDLAEQAHGSVMLKYGETIVLATVCMSKDKQNGLGFFN---LTVDYveKF--YATGKIlgsrfmRREGKPSEDAI 89
Cdd:cd11371     3 PIFlkTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSDrgrLNCEV--KFapFATPGR------RRHGQDSEERE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1083809137  90 LASRvIDRTLRP-----LFDQSIrhaVQVIVTVISVDDNDPVIlAVNAASLALAVSNIP 143
Cdd:cd11371    75 LSSL-LHQALEPavrleKYPKSQ---IDVFVTVLESDGSVLAA-AITAASLALADAGIE 128
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
632-698 5.74e-05

S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 41.45  E-value: 5.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGL 698
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
632-699 9.32e-05

S1_Rrp5_repeat_sc11: 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 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 41.13  E-value: 9.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLS 699
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT 68
VacB COG0557
Exoribonuclease R [Transcription];
631-705 1.23e-04

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 45.48  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKL-NSFTDGMVHISELAP----FRvERVSDIIKE--------GMIVPVKVISIDREKSRIG 697
Cdd:COG0557   622 VGEEFEGVISGVTSFGLFVELdELGVEGLVHVSSLGDdyyeYD-ERRQALVGErtgkryrlGDRVEVRVVRVDLDRRQID 700

                  ....*...
gi 1083809137 698 LSIREADK 705
Cdd:COG0557   701 FELVEGGS 708
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
631-702 1.39e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 44.41  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNSFTdGMVHISELA------PFRVERVSDIIKegmivpVKVISIDREKSRIGLSIRE 702
Cdd:PRK07400  196 VGEVVVGTVRGIKPYGAFIDIGGVS-GLLHISEIShehietPHSVFNVNDEMK------VMIIDLDAERGRISLSTKQ 266
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
631-696 1.63e-04

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: 40.85  E-value: 1.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKL-NSFTDGMVHISELAP-----------FRVERVSDIIKEGMIVPVKVISIDREKSRI 696
Cdd:cd04471     1 VGEEFDGVISGVTSFGLFVELdNLTVEGLVHVSTLGDdyyefdeenhaLVGERTGKVFRLGDKVKVRVVRVDLDRRKI 78
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
617-700 1.64e-04

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: 40.65  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 617 KAKSIVLEMThEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRI 696
Cdd:cd04461     1 KEGTLPTNFS-DLKPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRF 79

                  ....
gi 1083809137 697 GLSI 700
Cdd:cd04461    80 LLSL 83
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
630-692 2.67e-04

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: 39.90  E-value: 2.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083809137 630 TVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELapfrveRVSDIIKEGMIVPVKVISIDRE 692
Cdd:cd04473    15 EVGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNL------LRDYEVGDEVIVQVTDIPENGN 71
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
638-701 3.74e-04

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 43.11  E-value: 3.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083809137 638 EVVKIADFGAFVKLNSFTD--GMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:PTZ00248   24 KVVRITEMGAYVSLLEYDDieGMILMSELSKRRIRSINKLIRVGRHEVVVVLRVDKEKGYIDLSKK 89
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
632-701 5.52e-04

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 38.75  E-value: 5.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 632 GEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSDIIKEGMIVPVKVISIDREKSRIGLSIR 701
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
585-626 8.57e-04

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 38.32  E-value: 8.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1083809137 585 KTIKEIKEKTGAEITIEDDGT----VYFTGKGDGAEKAKSIVLEMT 626
Cdd:cd02394    22 ANIKRIREESGVSIRIPDDEAnsdeIRIEGSPEGVKKAKAEILELV 67
rpoE TIGR00448
DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form; This family seems to be ...
586-702 1.73e-03

DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form; This family seems to be confined to the archea and eukaryotic taxa and are quite dissimilar to E.coli rpoE. [Transcription, DNA-dependent RNA polymerase]


Pssm-ID: 129540 [Multi-domain]  Cd Length: 179  Bit Score: 40.15  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 586 TIKEIKEkTGAEITIEDDGTVYFtgkgdgaekaksivlEMTHEYTV-----GEVLKGEVVKIADFGAFVKLNSFtDGMVH 660
Cdd:TIGR00448  47 TIYDIED-IGEGKVIPGDGSAYH---------------NVTFRALVfkpelGEIVEGEVIEIVEFGAFVSLGPF-DGLFH 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083809137 661 ISEL----APFRVERVSDIIKE------------GMIVPVKVISIDREKSRIGLSIRE 702
Cdd:TIGR00448 110 VSQVtddyCYYDPKESALIGKEtkkvldegdkvrARIVALSLKDRRPEGSKIGLTMRQ 167
RNase_PH_archRRP41 cd11366
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ...
79-170 2.15e-03

RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA.


Pssm-ID: 206771 [Multi-domain]  Cd Length: 214  Bit Score: 40.01  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  79 RREGKPSEDAILASRVIDRTLRP--LFDQSIRHAVQVIVTVISVDDNDPVIlAVNAASLALAVSNIPWNGPIGCVRIGKY 156
Cdd:cd11366    65 RKRPGPDRREIEISKVIKEALEPaiILEEFPRTAIDVFVEVLQADAGTRVA-GLNAASLALADAGIPMRDLVAACAAGKV 143
                          90
                  ....*....|....
gi 1083809137 157 nDENLKINLAKLRD 170
Cdd:cd11366   144 -DGKIVLDLNKEED 156
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
624-702 3.52e-03

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 40.85  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 624 EMTHEYTVGEVLKGEVVKIADFGAFVKLNSFTDGMVHISELAPFRVERVSD-IIKEGMIVPVKVISIDREKSRIGLSIRE 702
Cdd:PRK12269  658 EIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADhELEVGKEIECMVIECDPQARRIRLGVKQ 737
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
79-170 5.05e-03

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 39.23  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137  79 RREGKPSEDAILASRVIDRTLRP--LFDQSIRHAVQVIVTVISVDDNDPViLAVNAASLALAVSNIPWNGPIGCVRIGKY 156
Cdd:PRK03983   87 RKRPGPDRRSIEISKVIREALEPaiMLELFPRTVIDVFIEVLQADAGTRV-AGITAASLALADAGIPMRDLVAGCAVGKV 165
                          90
                  ....*....|....
gi 1083809137 157 NDEnLKINLAKLRD 170
Cdd:PRK03983  166 DGV-IVLDLNKEED 178
rpsA PRK06676
30S ribosomal protein S1; Reviewed
587-702 6.10e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 39.47  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083809137 587 IKEIKE--KTGAEIT------IEDDGTVYFTGKGDGAEKAKSivlEMTHEYTVGEVLKGEVVKIADFGAFVKLNSfTDGM 658
Cdd:PRK06676   56 IEDINDvvKVGDELEvyvlkvEDGEGNLLLSKRRLEAEKAWD---KLEEKFEEGEVVEVKVTEVVKGGLVVDVEG-VRGF 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1083809137 659 VHISELAPFRVERVSDIIkeGMIVPVKVISIDREKSRIGLSIRE 702
Cdd:PRK06676  132 IPASLISTRFVEDFSDFK--GKTLEVKIIELDPEKNRVILSRRA 173
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
585-624 8.88e-03

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 35.33  E-value: 8.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1083809137 585 KTIKEIKEKTGAEITIEDDG------TVYFTGKGDGAEKAKSIVLE 624
Cdd:pfam00013  20 SNIKEIREETGAKIQIPPSEsegnerIVTITGTPEAVEAAKALIEE 65
PRK11642 PRK11642
ribonuclease R;
631-664 9.10e-03

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 39.34  E-value: 9.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1083809137 631 VGEVLKGEVVKIADFGAFVKLNS-FTDGMVHISEL 664
Cdd:PRK11642  643 VGNVFKGVISSVTGFGFFVRLDDlFIDGLVHVSSL 677
 
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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