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Conserved domains on  [gi|925922904|emb|CUE97555|]
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3'-to-5' exoribonuclease RNase R [Staphylococcus aureus]

Protein Classification

ribonuclease R( domain architecture ID 11493488)

ribonuclease R is a 3' to 5' hydrolytic exoribonuclease able to digest highly structured RNA

EC:  3.1.13.-
Gene Symbol:  rnr
Gene Ontology:  GO:0008997|GO:0003723|GO:0006401
PubMed:  11948193|9603904

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNase_R TIGR02063
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ...
1-711 0e+00

ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]


:

Pssm-ID: 273947 [Multi-domain]  Cd Length: 709  Bit Score: 1044.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904    1 MNLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKhsyrGQSKLIKGTLSQN 80
Cdd:TIGR02063   1 SPLRELILEFLKSKKGKPISLKELAKAFHLKGADEKKALRKRLRALEDDGLVKKNRRGLYALP----ESLKLVKGTVIAH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   81 KKGFAFLRPEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGEhKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDD 160
Cdd:TIGR02063  77 RDGFGFLRPEDDDEDDIFIPPRQMNGAMHGDRVLVRITGKPDG-GDRFEARVIKILERANDQIVGTFYIENGIGFVIPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  161 KRIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVP 240
Cdd:TIGR02063 156 KRIYLDIFIPPEQILGAEEGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYEFPEEVLDEAAKIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  241 DHIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRV 320
Cdd:TIGR02063 236 EEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGTSVYLPDRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  321 IPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPnIREQYNEITPMLD 400
Cdd:TIGR02063 316 IPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKDA-LDKKEPPLKEMLK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  401 LAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQ 480
Cdd:TIGR02063 395 NLFELYKILRKKRKKRGAIDFDSKEAKIILDENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHLEKAKLPFIYRVHER 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  481 PKSDRLRQFFDFITNFGIMIKG-TGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHF 559
Cdd:TIGR02063 475 PSEEKLQNLREFLKTLGITLKGgTSDKPQPKDFQKLLEKVKGRPEEELINTVLLRSMQQAKYSPENIGHFGLALEYYTHF 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  560 TSPIRRYPDLTVHRLIRKYLIEKS--MDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGI 637
Cdd:TIGR02063 555 TSPIRRYPDLIVHRLIKKALFGGEntTTEKEREYLEAKLEEIAEHSSKTERRADEAERDVNDWKKAEYMSEKIGEEFEGV 634
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904  638 VSSVANFGMFIELPN-TIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIV 711
Cdd:TIGR02063 635 ISGVTSFGLFVELENnTIEGLVHISTLKDDYYVFDEKGLALVGERTGKVFRLGDRVKVRVVKADLDTGKIDFELV 709
 
Name Accession Description Interval E-value
RNase_R TIGR02063
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ...
1-711 0e+00

ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]


Pssm-ID: 273947 [Multi-domain]  Cd Length: 709  Bit Score: 1044.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904    1 MNLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKhsyrGQSKLIKGTLSQN 80
Cdd:TIGR02063   1 SPLRELILEFLKSKKGKPISLKELAKAFHLKGADEKKALRKRLRALEDDGLVKKNRRGLYALP----ESLKLVKGTVIAH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   81 KKGFAFLRPEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGEhKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDD 160
Cdd:TIGR02063  77 RDGFGFLRPEDDDEDDIFIPPRQMNGAMHGDRVLVRITGKPDG-GDRFEARVIKILERANDQIVGTFYIENGIGFVIPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  161 KRIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVP 240
Cdd:TIGR02063 156 KRIYLDIFIPPEQILGAEEGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYEFPEEVLDEAAKIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  241 DHIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRV 320
Cdd:TIGR02063 236 EEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGTSVYLPDRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  321 IPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPnIREQYNEITPMLD 400
Cdd:TIGR02063 316 IPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKDA-LDKKEPPLKEMLK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  401 LAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQ 480
Cdd:TIGR02063 395 NLFELYKILRKKRKKRGAIDFDSKEAKIILDENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHLEKAKLPFIYRVHER 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  481 PKSDRLRQFFDFITNFGIMIKG-TGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHF 559
Cdd:TIGR02063 475 PSEEKLQNLREFLKTLGITLKGgTSDKPQPKDFQKLLEKVKGRPEEELINTVLLRSMQQAKYSPENIGHFGLALEYYTHF 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  560 TSPIRRYPDLTVHRLIRKYLIEKS--MDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGI 637
Cdd:TIGR02063 555 TSPIRRYPDLIVHRLIKKALFGGEntTTEKEREYLEAKLEEIAEHSSKTERRADEAERDVNDWKKAEYMSEKIGEEFEGV 634
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904  638 VSSVANFGMFIELPN-TIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIV 711
Cdd:TIGR02063 635 ISGVTSFGLFVELENnTIEGLVHISTLKDDYYVFDEKGLALVGERTGKVFRLGDRVKVRVVKADLDTGKIDFELV 709
VacB COG0557
Exoribonuclease R [Transcription];
2-717 0e+00

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 1037.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   2 NLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKhsyrGQSKLIKGTLSQNK 81
Cdd:COG0557    3 NSRETILAFLKEDAYKPLSKKELAKALGLKDEESREALKRRLRALEREGQLVKTRRGRYRLP----EKLDLVEGRVRGHR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  82 KGFAFLRPeDEDMEDIFIPPTKINRALDGDTVIVEIhqSKGEHKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDDK 161
Cdd:COG0557   79 DGFGFVIP-DDGEEDIFIPPRELNGALHGDRVLVRV--TKEDRRGRPEGRVVEILERANTRVVGRFEKEKGFGFVVPDDK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 162 RIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVPD 241
Cdd:COG0557  156 RLLQDIFIPPDDLNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPGDPGAEILIAIRKHGLPHEFPEEVLAEAEALPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 242 HIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVI 321
Cdd:COG0557  236 EVPEADLKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGWRLGVHIADVSHYVRPGSALDREARKRGTSVYLPDRVI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 322 PMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPNIREQYNEITPMLDL 401
Cdd:COG0557  316 PMLPERLSNGLCSLNPGEDRLAMSCEMEIDAKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREEYADLVPMLEE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 402 AQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQP 481
Cdd:COG0557  396 LYELAKILRKAREKRGAIDFDLPETKIILDEEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKLKLPFLYRVHEEP 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 482 KSDRLRQFFDFITNFGIMIKGtGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTS 561
Cdd:COG0557  476 DPEKLEALREFLANLGLKLKG-GDEPTPKDLQKLLEQVKGRPEEELLNTLLLRSMKQAVYSPENIGHFGLALEAYTHFTS 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 562 PIRRYPDLTVHRLIRKYLiEKSMDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGIVSSV 641
Cdd:COG0557  555 PIRRYPDLLVHRALKAYL-EGKRSPGLQEYLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEFEGVISGV 633
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 642 ANFGMFIELPNT-IEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIVGMPLPK 717
Cdd:COG0557  634 TSFGLFVELDELgVEGLVHVSSLGDDYYEYDERRQALVGERTGKRYRLGDRVEVRVVRVDLDRRQIDFELVEGGSEA 710
PRK11642 PRK11642
ribonuclease R;
18-745 9.19e-155

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 471.15  E-value: 9.19e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  18 PMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYqkkhSYRGQSKLIKGTLSQNKKGFAFLRPEDEDmEDI 97
Cdd:PRK11642  34 PASREELAVELNIEGEEQLEALRRRLRAMERDGQLVFTRRQCY----ALPERLDLLKGTVIGHRDGYGFLRVEGRK-DDL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  98 FIPPTKINRALDGDTVIVEIHQSkgEHKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDDKRIMQDIFIPKGQSLGA 177
Cdd:PRK11642 109 YLSSEQMKTCIHGDQVLAQPLGA--DRKGRREARIVRVLVPKTSQIVGRYFTDAGVGFVVPDDSRLSFDILIPPEQIMGA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 178 VDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVPDHIENTEIKGRHDLRDE 257
Cdd:PRK11642 187 RMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDL 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 258 LTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSNGICSLNP 337
Cdd:PRK11642 267 PLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPSQVVPMLPEVLSNGLCSLNP 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 338 NVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIItEKDPNIREQYNEITPMLDLAQDLSNRLIQMRKRRG 417
Cdd:PRK11642 347 QVDRLCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHIL-QGDQDLREQYAPLVKHLEELHNLYKVLDKAREERG 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 418 EIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQFFDFITNFG 497
Cdd:PRK11642 426 GISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAKEPALFRIHDKPSTEAITSFRSVLAELG 505
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 498 IMIKGtGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIrK 577
Cdd:PRK11642 506 LELPG-GNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGLALQSYAHFTSPIRRYPDLSLHRAI-K 583
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 578 YLIEKSMDNKEvkRWE---------DKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGIVSSVANFGMFI 648
Cdd:PRK11642 584 YLLAKEQGHKG--NTTetggyhysmEEMLQLGQHCSMTERRADEATRDVADWLKCDFMLDQVGNVFKGVISSVTGFGFFV 661
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 649 ELPNT-IEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIVGmplpkndrSQRPARG 727
Cdd:PRK11642 662 RLDDLfIDGLVHVSSLDNDYYRFDQVGQRLIGESSGQTYRLGDRVEVRVEAVNMDERKIDFSLIS--------SERAPRN 733
                        730
                 ....*....|....*...
gi 925922904 728 KTIQAKTRGKSLDKSKSD 745
Cdd:PRK11642 734 VGKTAREKAKKGDAGKKG 751
RNB pfam00773
RNB domain; This domain is the catalytic domain of ribonuclease II.
251-579 1.16e-132

RNB domain; This domain is the catalytic domain of ribonuclease II.


Pssm-ID: 459934 [Multi-domain]  Cd Length: 314  Bit Score: 396.65  E-value: 1.16e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  251 RHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSN 330
Cdd:pfam00773   1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  331 GICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPNIREQynEITPMLDLAQDLSNRLI 410
Cdd:pfam00773  81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKP--DLAEDLRLLYELAKILR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  411 QMRKRRGEIDFDISEAKVLVNEDGiPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQFF 490
Cdd:pfam00773 159 AKRLQRGALDLDTPENKLILDEEG-VIDILIQERTDAHSLIEEFMLLANEAVARHLQELGIPALYRVHPEPDLEKLNSLI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  491 DFItnfgimikgtGEDIHPTTLQKVQEEVEGrpEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLT 570
Cdd:pfam00773 238 KLL----------QLLPDDKGLSKSLEKIKD--DERLLSILLLRTMPRAEYSPEPLGHFGLGLDIYTHFTSPIRRYPDLI 305

                  ....*....
gi 925922904  571 VHRLIRKYL 579
Cdd:pfam00773 306 VHRQLKALL 314
RNB smart00955
This domain is the catalytic domain of ribonuclease II;
251-581 1.24e-123

This domain is the catalytic domain of ribonuclease II;


Pssm-ID: 214935 [Multi-domain]  Cd Length: 286  Bit Score: 371.99  E-value: 1.24e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   251 RHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSN 330
Cdd:smart00955   1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNGGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDRVIPMLPEELSN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   331 GICSLNPNVDRLTLSCRMEIDASG-RVVKHEIFDSVIHSDYRMTYDAVNQIITekdpnireqyneitpmldlaqdlsnrl 409
Cdd:smart00955  81 GLCSLNPGEDRLALSVEMTLDADGgEILDYEFYRSVIRSKARLTYEEVDAILE--------------------------- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   410 iqmrkrrgeidfdiseaKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQF 489
Cdd:smart00955 134 -----------------KIVLDEEGKIEDIVPRERNDAHSLVEEFMILANEAVARFLAKNGIPGLYRVHEGPDPEKLAEL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   490 F-DFITNFGIMIKGtgeDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPD 568
Cdd:smart00955 197 LkEFLALLGLLLLG---GDGPKALAKLLEKIRDSPEERLLELLLLRSMPHAEYSVDNSGHFGLALDAYTHFTSPIRRYPD 273
                          330
                   ....*....|...
gi 925922904   569 LTVHRLIRKYLIE 581
Cdd:smart00955 274 LIVHRQLKAALRG 286
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
630-711 1.82e-36

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: 131.75  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPN-TIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDF 708
Cdd:cd04471    1 VGEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGDDYYEFDEENHALVGERTGKVFRLGDKVKVRVVRVDLDRRKIDF 80

                 ...
gi 925922904 709 QIV 711
Cdd:cd04471   81 ELV 83
 
Name Accession Description Interval E-value
RNase_R TIGR02063
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ...
1-711 0e+00

ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]


Pssm-ID: 273947 [Multi-domain]  Cd Length: 709  Bit Score: 1044.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904    1 MNLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKhsyrGQSKLIKGTLSQN 80
Cdd:TIGR02063   1 SPLRELILEFLKSKKGKPISLKELAKAFHLKGADEKKALRKRLRALEDDGLVKKNRRGLYALP----ESLKLVKGTVIAH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   81 KKGFAFLRPEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGEhKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDD 160
Cdd:TIGR02063  77 RDGFGFLRPEDDDEDDIFIPPRQMNGAMHGDRVLVRITGKPDG-GDRFEARVIKILERANDQIVGTFYIENGIGFVIPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  161 KRIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVP 240
Cdd:TIGR02063 156 KRIYLDIFIPPEQILGAEEGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYEFPEEVLDEAAKIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  241 DHIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRV 320
Cdd:TIGR02063 236 EEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGTSVYLPDRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  321 IPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPnIREQYNEITPMLD 400
Cdd:TIGR02063 316 IPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKDA-LDKKEPPLKEMLK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  401 LAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQ 480
Cdd:TIGR02063 395 NLFELYKILRKKRKKRGAIDFDSKEAKIILDENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHLEKAKLPFIYRVHER 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  481 PKSDRLRQFFDFITNFGIMIKG-TGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHF 559
Cdd:TIGR02063 475 PSEEKLQNLREFLKTLGITLKGgTSDKPQPKDFQKLLEKVKGRPEEELINTVLLRSMQQAKYSPENIGHFGLALEYYTHF 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  560 TSPIRRYPDLTVHRLIRKYLIEKS--MDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGI 637
Cdd:TIGR02063 555 TSPIRRYPDLIVHRLIKKALFGGEntTTEKEREYLEAKLEEIAEHSSKTERRADEAERDVNDWKKAEYMSEKIGEEFEGV 634
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904  638 VSSVANFGMFIELPN-TIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIV 711
Cdd:TIGR02063 635 ISGVTSFGLFVELENnTIEGLVHISTLKDDYYVFDEKGLALVGERTGKVFRLGDRVKVRVVKADLDTGKIDFELV 709
VacB COG0557
Exoribonuclease R [Transcription];
2-717 0e+00

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 1037.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   2 NLKQSIEEIINQPEYEPMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYQKKhsyrGQSKLIKGTLSQNK 81
Cdd:COG0557    3 NSRETILAFLKEDAYKPLSKKELAKALGLKDEESREALKRRLRALEREGQLVKTRRGRYRLP----EKLDLVEGRVRGHR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  82 KGFAFLRPeDEDMEDIFIPPTKINRALDGDTVIVEIhqSKGEHKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDDK 161
Cdd:COG0557   79 DGFGFVIP-DDGEEDIFIPPRELNGALHGDRVLVRV--TKEDRRGRPEGRVVEILERANTRVVGRFEKEKGFGFVVPDDK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 162 RIMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVPD 241
Cdd:COG0557  156 RLLQDIFIPPDDLNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPGDPGAEILIAIRKHGLPHEFPEEVLAEAEALPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 242 HIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVI 321
Cdd:COG0557  236 EVPEADLKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGWRLGVHIADVSHYVRPGSALDREARKRGTSVYLPDRVI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 322 PMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPNIREQYNEITPMLDL 401
Cdd:COG0557  316 PMLPERLSNGLCSLNPGEDRLAMSCEMEIDAKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREEYADLVPMLEE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 402 AQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQP 481
Cdd:COG0557  396 LYELAKILRKAREKRGAIDFDLPETKIILDEEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKLKLPFLYRVHEEP 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 482 KSDRLRQFFDFITNFGIMIKGtGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTS 561
Cdd:COG0557  476 DPEKLEALREFLANLGLKLKG-GDEPTPKDLQKLLEQVKGRPEEELLNTLLLRSMKQAVYSPENIGHFGLALEAYTHFTS 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 562 PIRRYPDLTVHRLIRKYLiEKSMDNKEVKRWEDKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGIVSSV 641
Cdd:COG0557  555 PIRRYPDLLVHRALKAYL-EGKRSPGLQEYLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEFEGVISGV 633
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 642 ANFGMFIELPNT-IEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIVGMPLPK 717
Cdd:COG0557  634 TSFGLFVELDELgVEGLVHVSSLGDDYYEYDERRQALVGERTGKRYRLGDRVEVRVVRVDLDRRQIDFELVEGGSEA 710
3_prime_RNase TIGR00358
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ...
61-711 0e+00

VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]


Pssm-ID: 273033 [Multi-domain]  Cd Length: 654  Bit Score: 680.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   61 QKKHSYRGQSKLIKGTLSQNKKGFAFLRPEDEDMEDIFIPPTKINRALDGDTVIVEIHqSKGEhKGKIEGEVKSIEKHSV 140
Cdd:TIGR00358   5 TLKYALPEKDDLVKGVVKAHNKGFGFLRPDDDDKKDYFIPPPQMKKVMHGDLVEACPL-SQPQ-RGRFEAEVERILEPAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  141 TQVVGTYSEARHFGFVIPDDKRIMQDIFIPK-GQSLGAVDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSII 219
Cdd:TIGR00358  83 TRFVGKFLGENDFGFVVPDDPRIYLDIIVPKaSVKNELAEGDKVVVELTEYPLRRNLFYGEITQILGNNDDPLIPWWVTL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  220 YQHGIEIEFPDEVLQEAEAVPDHIENTEIKGRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTE 299
Cdd:TIGR00358 163 ARHEIPFEFPDGVEQQAAKLQFDVDEQAKKYREDLTDLAFVTIDGADAKDLDDAVYVKKLPDGGWKLYVAIADVSYYVAE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  300 GSALDKEAYDRATSVYLVDRVIPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQ 379
Cdd:TIGR00358 243 NSPLDKEAKHRGFSVYLPGFVIPMLPEELSNGLCSLNPNEDRLVLVCEMTISAQGRITDNEFYPATIESKARLTYDKVND 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  380 IItEKDPNIREQYNEITPMLDLAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIAN 459
Cdd:TIGR00358 323 WL-ENDDELQPEYETLVEQLKALHQLSQALGEWRHKRGLIDFEHPETKFIVDEEGRVIDIVAEVRRIAEKIIEEAMIVAN 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  460 ETVAEHFSKLDVPFIYRVHEQPKSDRLRQFFDFITNFGI-MIKGTGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQ 538
Cdd:TIGR00358 402 ICAARFLHNHKVPGIYRVHPGPSKKKLQSLLEFLAELGLtLPGGNAENVTTLDGACWLREVKDRPEYEILVTRLLRSLSQ 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  539 AHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIRKYLIEKSMDNKEVKrWEDKLPELAEHTSKRERRAIEAERDTD 618
Cdd:TIGR00358 482 AEYSPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEQTDTERYQ-PQDELLQIAEHCSDTERRARDAERDVA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  619 ELKKAEYMIQHIGDEFEGIVSSVANFGMFIELP-NTIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVT 697
Cdd:TIGR00358 561 DWLKCRYLLDKVGTEFSGEISSVTRFGMFVRLDdNGIDGLIHISTLHNDYYVFDQEKMALIGKGTGKVYRIGDRVTVKLT 640
                         650
                  ....*....|....
gi 925922904  698 HVDVDERLIDFQIV 711
Cdd:TIGR00358 641 EVNMETRSIIFELV 654
PRK11642 PRK11642
ribonuclease R;
18-745 9.19e-155

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 471.15  E-value: 9.19e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  18 PMSVSDFQDALGLSSADSFRDLIKVLVELEQSGLIERTKTDRYqkkhSYRGQSKLIKGTLSQNKKGFAFLRPEDEDmEDI 97
Cdd:PRK11642  34 PASREELAVELNIEGEEQLEALRRRLRAMERDGQLVFTRRQCY----ALPERLDLLKGTVIGHRDGYGFLRVEGRK-DDL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  98 FIPPTKINRALDGDTVIVEIHQSkgEHKGKIEGEVKSIEKHSVTQVVGTYSEARHFGFVIPDDKRIMQDIFIPKGQSLGA 177
Cdd:PRK11642 109 YLSSEQMKTCIHGDQVLAQPLGA--DRKGRREARIVRVLVPKTSQIVGRYFTDAGVGFVVPDDSRLSFDILIPPEQIMGA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 178 VDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDEVLQEAEAVPDHIENTEIKGRHDLRDE 257
Cdd:PRK11642 187 RMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDL 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 258 LTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSNGICSLNP 337
Cdd:PRK11642 267 PLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPSQVVPMLPEVLSNGLCSLNP 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 338 NVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIItEKDPNIREQYNEITPMLDLAQDLSNRLIQMRKRRG 417
Cdd:PRK11642 347 QVDRLCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHIL-QGDQDLREQYAPLVKHLEELHNLYKVLDKAREERG 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 418 EIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQFFDFITNFG 497
Cdd:PRK11642 426 GISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAKEPALFRIHDKPSTEAITSFRSVLAELG 505
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 498 IMIKGtGEDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIrK 577
Cdd:PRK11642 506 LELPG-GNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGLALQSYAHFTSPIRRYPDLSLHRAI-K 583
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 578 YLIEKSMDNKEvkRWE---------DKLPELAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDEFEGIVSSVANFGMFI 648
Cdd:PRK11642 584 YLLAKEQGHKG--NTTetggyhysmEEMLQLGQHCSMTERRADEATRDVADWLKCDFMLDQVGNVFKGVISSVTGFGFFV 661
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 649 ELPNT-IEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDFQIVGmplpkndrSQRPARG 727
Cdd:PRK11642 662 RLDDLfIDGLVHVSSLDNDYYRFDQVGQRLIGESSGQTYRLGDRVEVRVEAVNMDERKIDFSLIS--------SERAPRN 733
                        730
                 ....*....|....*...
gi 925922904 728 KTIQAKTRGKSLDKSKSD 745
Cdd:PRK11642 734 VGKTAREKAKKGDAGKKG 751
RNB pfam00773
RNB domain; This domain is the catalytic domain of ribonuclease II.
251-579 1.16e-132

RNB domain; This domain is the catalytic domain of ribonuclease II.


Pssm-ID: 459934 [Multi-domain]  Cd Length: 314  Bit Score: 396.65  E-value: 1.16e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  251 RHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSN 330
Cdd:pfam00773   1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  331 GICSLNPNVDRLTLSCRMEIDASGRVVKHEIFDSVIHSDYRMTYDAVNQIITEKDPNIREQynEITPMLDLAQDLSNRLI 410
Cdd:pfam00773  81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKP--DLAEDLRLLYELAKILR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  411 QMRKRRGEIDFDISEAKVLVNEDGiPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQFF 490
Cdd:pfam00773 159 AKRLQRGALDLDTPENKLILDEEG-VIDILIQERTDAHSLIEEFMLLANEAVARHLQELGIPALYRVHPEPDLEKLNSLI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  491 DFItnfgimikgtGEDIHPTTLQKVQEEVEGrpEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLT 570
Cdd:pfam00773 238 KLL----------QLLPDDKGLSKSLEKIKD--DERLLSILLLRTMPRAEYSPEPLGHFGLGLDIYTHFTSPIRRYPDLI 305

                  ....*....
gi 925922904  571 VHRLIRKYL 579
Cdd:pfam00773 306 VHRQLKALL 314
RNB smart00955
This domain is the catalytic domain of ribonuclease II;
251-581 1.24e-123

This domain is the catalytic domain of ribonuclease II;


Pssm-ID: 214935 [Multi-domain]  Cd Length: 286  Bit Score: 371.99  E-value: 1.24e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   251 RHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALDKEAYDRATSVYLVDRVIPMIPHRLSN 330
Cdd:smart00955   1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNGGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDRVIPMLPEELSN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   331 GICSLNPNVDRLTLSCRMEIDASG-RVVKHEIFDSVIHSDYRMTYDAVNQIITekdpnireqyneitpmldlaqdlsnrl 409
Cdd:smart00955  81 GLCSLNPGEDRLALSVEMTLDADGgEILDYEFYRSVIRSKARLTYEEVDAILE--------------------------- 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   410 iqmrkrrgeidfdiseaKVLVNEDGIPTDVQLRQRGEGERLIESFMLIANETVAEHFSKLDVPFIYRVHEQPKSDRLRQF 489
Cdd:smart00955 134 -----------------KIVLDEEGKIEDIVPRERNDAHSLVEEFMILANEAVARFLAKNGIPGLYRVHEGPDPEKLAEL 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904   490 F-DFITNFGIMIKGtgeDIHPTTLQKVQEEVEGRPEQMVISTMMLRSMQQAHYDDVNLGHFGLSAEYYTHFTSPIRRYPD 568
Cdd:smart00955 197 LkEFLALLGLLLLG---GDGPKALAKLLEKIRDSPEERLLELLLLRSMPHAEYSVDNSGHFGLALDAYTHFTSPIRRYPD 273
                          330
                   ....*....|...
gi 925922904   569 LTVHRLIRKYLIE 581
Cdd:smart00955 274 LIVHRQLKAALRG 286
Rnb COG4776
Exoribonuclease II [Transcription];
61-715 5.48e-67

Exoribonuclease II [Transcription];


Pssm-ID: 443808 [Multi-domain]  Cd Length: 644  Bit Score: 234.36  E-value: 5.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  61 QKKHSYRGQSKLIKGTLSQNKKGFAFLrpEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGEHKGKIEgevKSIEKhSV 140
Cdd:COG4776   10 QLKQQLHEQTPRVEGVVKATDKGFGFL--EVDDQKSYFIPPPQMKKVMHGDRIKAVIRTEKDKESAEPE---TLIEP-FL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 141 TQVVGTYSEARHFGFVIPDDKRIMQDIFIPKGQSLGAV--DGHKVLVQITKYA-DGSDNPEGHISAILGHKNDPGVDILS 217
Cdd:COG4776   84 TRFVGRVQKKDGRLFVVPDHPLIKDAIKARPKKGLEEGlkEGDWVVAELKRHPlKGDRGFFAEITEFIADADDPFAPWWV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 218 IIYQHGIEIEFPdEVLQEAEAVPDHIEnteikgRHDLRDELTITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYV 297
Cdd:COG4776  164 TLARHNLEREAP-EGDDEWELLDEGLE------REDLTALPFVTIDSESTEDMDDALYIEKLENGGWKLTVAIADPTAYI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 298 TEGSALDKEAYDRATSVYLVDRVIPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVV-KHEIFDSVIHSDYRMTYDA 376
Cdd:COG4776  237 PEGSELDKEARQRAFTNYLPGFNIPMLPRELSDDLCSLKENEKRPALVCRVTIDADGSIGdDIEFFAAWIRSKAKLAYDN 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 377 VNQIITEKD------PNIREQyneitpmLDLAQDLSNRLIQMRKR-------RGEIDFDIseakvlvNEDGIPTDVQLRQ 443
Cdd:COG4776  317 VSDWLEGKGewqpenEEIAEQ-------IRLLHQFALARSQWRQQhalvfkdRPDYRFEL-------DEKGNVLDIHAEP 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 444 RGEGERLIESFMLIANETVAEHFSKlDVPF-IYRVHEQPKSDRLRQFFDFITNFGIMIkgTGEDIhpTTLQ---KVQEEV 519
Cdd:COG4776  383 RRIANRIVEEAMIAANICAARVLRE-HLGFgIFNVHSGFDPEKLEQAVELLAEHGIEF--DPEQL--LTLEgfcALRREL 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 520 EGRPEQMVIStmMLRSMQQ-AHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIRKYLIeksmdNKEVKRWEDklpE 598
Cdd:COG4776  458 DAQPTSYLDS--RLRRFQTfAEISTEPGPHFGLGLDAYATWTSPIRKYGDMVNHRLIKAVIL-----GQPAEKPDE---E 527
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 599 LAEHTSKRERRAIEAERDTDELKKAEYMIQHIGDE--FEGIVSSVANFGM-----------FIELPntiegMVHiANMTD 665
Cdd:COG4776  528 LTERLAERRRLNRMAERDVADWLYARYLKPKVGSGqvFTAEIIDINRGGLrvrllengavaFIPAS-----FIH-SVRDE 601
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|
gi 925922904 666 DYYRFEERQMALIGERqakVFRIGDTVKVKVTHVDVDERlidfQIVGMPL 715
Cdd:COG4776  602 LVCSQEEGTVYIKGEV---RYKLGDTIQVTLAEVREETR----SIIAKPA 644
PRK05054 PRK05054
exoribonuclease II; Provisional
72-715 6.37e-52

exoribonuclease II; Provisional


Pssm-ID: 179920 [Multi-domain]  Cd Length: 644  Bit Score: 192.01  E-value: 6.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  72 LIKGTlsqnKKGFAFLrpEDEDMEDIFIPPTKINRALDGDTVIVEIHQSKGehkgKIEGEVKSIEKHSVTQVVGTYSEAR 151
Cdd:PRK05054  25 VVKAT----EKGFGFL--EVDAQKSYFIPPPQMKKVMHGDRIIAVIHTEKD----REIAEPEELIEPFLTRFVGRVQKKD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 152 HFGFVIPDDKRIMQDIFIPKGQSLGAV--DGHKVLVQITKYADGSDNP-EGHISAILGHKNDPGVDILSIIYQHGIEief 228
Cdd:PRK05054  95 DRLSIVPDHPLLKDAIPCRAAKGLNHEfkEGDWVVAELRRHPLKGDRGfYAEITQFITDADDHFAPWWVTLARHNLE--- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 229 pdevlQEAeavPDHIENTEIKGRHDLRDELT----ITIDGADAKDLDDAISVKKLANGNTQLTVSIADVSYYVTEGSALD 304
Cdd:PRK05054 172 -----REA---PAGGVAWEMLDEGLEREDLTaldfVTIDSASTEDMDDALYVEKLPDGGLQLTVAIADPTAYIAEGSKLD 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 305 KEAYDRATSVYLVDRVIPMIPHRLSNGICSLNPNVDRLTLSCRMEIDASGRVV-KHEIFDSVIHSDYRMTYDAVNQIItE 383
Cdd:PRK05054 244 KAARQRAFTNYLPGFNIPMLPRELSDDLCSLRPNERRPALACRVTIDADGTIEdDIRFFAAWIESKAKLAYDNVSDWL-E 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 384 KDPNIREQYNEITPMLDLAQDLSNRLIQMRKRRGEIDFDISEAKVLVNEDGIPTDVQLRQRGEGERLIESFMLIAN---- 459
Cdd:PRK05054 323 NGGDWQPESEAIAEQIRLLHQFCLARSEWRKQHALVFKDRPDYRFELGEKGEVLDIVAEPRRIANRIVEESMIAANicaa 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 460 ETVAEHFSkldvpF-IYRVHEQPKSDRLRQFFDFITNFGimIKGTGEDIhpTTLQ---KVQEEVEGRPEQMVISTmmLRS 535
Cdd:PRK05054 403 RVLRDKLG-----FgIYNVHSGFDPANAEQAVALLKEHG--LHFDAEEL--LTLEgfcKLRRELDAQPTGYLDSR--IRR 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 536 MQQ-AHYDDVNLGHFGLSAEYYTHFTSPIRRYPDLTVHRLIRKYLIEKsmdnKEVKRWEDKLPELAEHtskreRRAIE-A 613
Cdd:PRK05054 472 FQSfAEISTEPGPHFGLGLEAYATWTSPIRKYGDMINHRLLKAVIKGE----TAERPQDEITVQLAER-----RRLNRmA 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 614 ERDTDELKKAEYMIQHIGDE--FEGIVSSVANFGM-----------FIELP-----------NTIEGMVHIAnmtddyyr 669
Cdd:PRK05054 543 ERDVGDWLYARYLKDKAGTDtrFAAEIIDISRGGMrvrllengavaFIPASflhavrdelvcNQENGTVQIK-------- 614
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*.
gi 925922904 670 feerqmaliGErqaKVFRIGDTVKVKVTHVDVDERlidfQIVGMPL 715
Cdd:PRK05054 615 ---------GE---TVYKLGDVIDVTLAEVRMETR----SIIARPV 644
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
630-711 1.82e-36

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: 131.75  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPN-TIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDERLIDF 708
Cdd:cd04471    1 VGEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGDDYYEFDEENHALVGERTGKVFRLGDKVKVRVVRVDLDRRKIDF 80

                 ...
gi 925922904 709 QIV 711
Cdd:cd04471   81 ELV 83
CSD2 pfam17876
Cold shock domain; Crystallographic structure analysis of E. coli wild-type RNase II revealed ...
155-229 1.52e-32

Cold shock domain; Crystallographic structure analysis of E. coli wild-type RNase II revealed that the amino-terminal region starts with an alpha-helix followed by two consecutive five-stranded anti-parallel beta-barrels, identified as cold-shock domains (CSD1 and CSD2). This entry relates to CSD2 which lacks the typical sequence motifs RNPI and RNPII but contributes to RNA binding.


Pssm-ID: 465546 [Multi-domain]  Cd Length: 74  Bit Score: 120.19  E-value: 1.52e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904  155 FVIPDDKRIMQDIFIPKGQSLGAVDGHKVLVQITKYADGsDNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFP 229
Cdd:pfam17876   1 FVVPDDKRIPQDIFIPKEDLKGAKDGDKVVVEITEYPDG-KNPEGKIVEVLGDPGDPGVEILSIIRKHGLPHEFP 74
OB_RNB pfam08206
Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease ...
75-135 8.85e-15

Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease B proteins in one or two copies.


Pssm-ID: 429863 [Multi-domain]  Cd Length: 58  Bit Score: 69.10  E-value: 8.85e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925922904   75 GTLSQNKKGFAFLRPEDEDmEDIFIPPTKINRALDGDTVIVEIHqsKGEHKGKIEGEVKSI 135
Cdd:pfam08206   1 GTVRGHKKGFGFLIPDDEE-DDIFIPPNQMKKAMHGDRVLVRIT--KGDRRGRREGRIVRI 58
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
635-704 4.19e-13

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: 65.77  E-value: 4.19e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 635 EGIVSSVANFGMFIELpNTIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDER 704
Cdd:cd04460    4 EGEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYISYDPKNKRLIGEETKRVLKVGDVVRARIVAVSLKER 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
630-708 9.74e-13

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 63.78  E-value: 9.74e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925922904   630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEErqmaligerqaKVFRIGDTVKVKVTHVDVDERLIDF 708
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPE-----------EVLKVGDEVKVKVLSVDEEKGRIIL 69
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
635-704 2.01e-12

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 66.39  E-value: 2.01e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925922904 635 EGIVSSVANFGMFIEL-PntIEGMVHIANMTDDYYRFEERQMALIGERQAKVFRIGDTVKVKVTHVDVDER 704
Cdd:PRK08563  86 EGEVVEVVEFGAFVRIgP--VDGLLHISQIMDDYISYDPKNGRLIGKESKRVLKVGDVVRARIVAVSLKER 154
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
630-710 2.07e-12

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: 63.08  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEERqmaligerqakVFRIGDTVKVKVTHVDVDERLIDFQ 709
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDE-----------VIKVGDEVKVKVLKVDKDRRRIILS 71

                  .
gi 925922904  710 I 710
Cdd:pfam00575  72 I 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
631-705 3.04e-10

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: 56.52  E-value: 3.04e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRfeerqmaligeRQAKVFRIGDTVKVKVTHVDVDERL 705
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVK-----------DVKDVLKEGDKVKVKVLSIDARGRI 64
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
616-704 1.20e-09

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 61.60  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 616 DTDELKKAEYMIQ------HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDdyyrfeerqmaligERQAKV---F 686
Cdd:PRK11824 601 DGEAAEAAKERIEgitaepEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD--------------ERVEKVedvL 666
                         90
                 ....*....|....*...
gi 925922904 687 RIGDTVKVKVThvDVDER 704
Cdd:PRK11824 667 KEGDEVKVKVL--EIDKR 682
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
634-706 4.41e-09

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: 53.15  E-value: 4.41e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925922904 634 FEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEErqmaligerqaKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPS-----------EVFKVGDEVEVKVLEVDPEKGRI 62
OB_RNB pfam08206
Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease ...
153-201 9.60e-09

Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease B proteins in one or two copies.


Pssm-ID: 429863 [Multi-domain]  Cd Length: 58  Bit Score: 52.16  E-value: 9.60e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 925922904  153 FGFVIPDDKriMQDIFIPKGQSLGAVDGHKVLVQITKYADGSDNPEGHI 201
Cdd:pfam08206  10 FGFLIPDDE--EDDIFIPPNQMKKAMHGDRVLVRITKGDRRGRREGRIV 56
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
608-700 1.63e-08

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: 57.36  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 608 RRAI-EAERdtdELKKAEYMIQ-HIGDEFEGIVSSVANFGMFIELPNtIEGMVHIANMTddYYRFeerqmaligERQAKV 685
Cdd:COG0539  168 RRAVlEEER---EEKREELLEKlEEGDVVEGTVKNITDFGAFVDLGG-VDGLLHISEIS--WGRV---------KHPSEV 232
                         90
                 ....*....|....*
gi 925922904 686 FRIGDTVKVKVTHVD 700
Cdd:COG0539  233 LKVGDEVEVKVLKID 247
rpsA PRK06299
30S ribosomal protein S1; Reviewed
630-706 2.10e-08

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 57.48  E-value: 2.10e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrFEERqmaliGERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:PRK06299 373 VGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDIS-----WDKK-----GEEAVELYKKGDEVEAVVLKVDVEKERI 439
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
631-706 2.16e-08

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: 51.46  E-value: 2.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFV-----------SHPSDVVSVGDIVEVKVISIDEERGRI 65
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
630-741 3.68e-08

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 52.49  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRfeerqmaLIGErqakVFRIGDTVKVKVTHVDVDERlIDFQ 709
Cdd:COG1098    5 VGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVK-------DIND----YLKVGDEVKVKVLSIDEDGK-ISLS 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 925922904 710 IVGMpLPKNDRSQRPARGKtiQAKTRGKSLDK 741
Cdd:COG1098   73 IKQA-EEKPKRPPRPRRNS--RPKAGFESFED 101
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
629-706 6.51e-08

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: 55.44  E-value: 6.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDyyrfeERqmaliGERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:COG0539  273 PVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWT-----KR-----VAHPSDVVKVGDEVEVKVLDIDPEERRI 340
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
631-705 9.52e-08

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: 49.46  E-value: 9.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERL 705
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERV-----------EKVEDVLKVGDEVKVKVIEVDDRGRI 64
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
631-705 1.98e-07

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: 48.64  E-value: 1.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrFEERqmaliGERQAKVFRIGDTVKVKVTHVDVD-ERL 705
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDIS-----WTQR-----VRHPSEIYKKGQEVEAVVLNIDVErERI 66
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
630-706 2.16e-07

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: 48.39  E-value: 2.16e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 630 IGDEFEGIVSSVANFGMFIELpNTIEGMVHIANMTddYYRFeerqmaligERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMS--WGRV---------KHPSEVVNVGDEVEVKVLKIDKERKRI 65
rpsA PRK06676
30S ribosomal protein S1; Reviewed
629-706 3.40e-07

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 53.34  E-value: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrfeerqmaliGERQAK---VFRIGDTVKVKVTHVDVDERL 705
Cdd:PRK06676 276 PEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQIS--------------HKHIATpseVLEEGQEVKVKVLEVNEEEKR 341

                 .
gi 925922904 706 I 706
Cdd:PRK06676 342 I 342
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
629-708 1.15e-06

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: 46.94  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNT-IEGMVHIANMTDDyyRFEERQmaligerqaKVFRIGDTVKVKVTHVDVDERLID 707
Cdd:cd05708    1 KVGQKIDGTVRRVEDYGVFIDIDGTnVSGLCHKSEISDN--RVADAS---------KLFRVGDKVRAKVLKIDAEKKRIS 69

                 .
gi 925922904 708 F 708
Cdd:cd05708   70 L 70
rpsA PRK06299
30S ribosomal protein S1; Reviewed
631-706 1.18e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 52.09  E-value: 1.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDyyRFEERqmaligerqAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:PRK06299 461 GSIVTGTVTEVKDKGAFVELEDGVEGLIRASELSRD--RVEDA---------TEVLKVGDEVEAKVINIDRKNRRI 525
CSP smart00357
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ...
74-135 1.31e-06

Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.


Pssm-ID: 214633 [Multi-domain]  Cd Length: 64  Bit Score: 46.05  E-value: 1.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904    74 KGTLSQNKKGFAFLRPEDEDmEDIFIPPTKINRAL----DGDTVIVEIHQSKGehKGKIEGEVKSI 135
Cdd:smart00357   1 TGVVKWFNKGFGFIRPDDGG-KDVFVHPSQIQGGLkslrEGDEVEFKVVSPEG--GEKPEAENVVK 63
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
631-710 1.55e-06

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 51.66  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDyyRFEERQmaligerqaKVFRIGDTVKVKVTHVDVDERLIDFQI 710
Cdd:TIGR00717 447 GSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSEN--RDEDKT---------DEIKVGDEVEAKVVDIDKKNRKVSLSV 515
rpsA PRK06299
30S ribosomal protein S1; Reviewed
608-702 2.06e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 51.32  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 608 RRA-IEAERdtdELKKAEYMIQ-HIGDEFEGIVSSVANFGMFIELpNTIEGMVHIANMTddYYRFEErqmaligerQAKV 685
Cdd:PRK06299 180 RRAvLEEER---AEEREELLENlEEGQVVEGVVKNITDYGAFVDL-GGVDGLLHITDIS--WKRVNH---------PSEV 244
                         90
                 ....*....|....*..
gi 925922904 686 FRIGDTVKVKVTHVDVD 702
Cdd:PRK06299 245 VNVGDEVKVKVLKFDKE 261
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
629-706 2.75e-06

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 50.72  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDdyyrfeeRQMALIGErqakVFRIGDTVKVKVTHVDVDERLI 706
Cdd:PRK00087 561 PVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISW-------KRIDKPED----VLSEGEEVKAKILEVDPEEKRI 627
rpsA PRK13806
30S ribosomal protein S1; Provisional
631-706 2.78e-06

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 50.49  E-value: 2.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddYYRfeerqmaligeRQAK---VFRIGDTVKVKVTHVDVDERLI 706
Cdd:PRK13806 293 GDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMS--WTR-----------RVNKpedVVAPGDAVAVKIKDIDPAKRRI 358
PRK08582 PRK08582
RNA-binding protein S1;
626-744 4.37e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 46.95  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 626 MIQHIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERl 705
Cdd:PRK08582   1 MSIEVGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYV-----------KDINDHLKVGDEVEVKVLNVEDDGK- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 925922904 706 IDFQI---VGMPLPKNDRSQRPARGKTIQAKTRGKSLDKSKS 744
Cdd:PRK08582  69 IGLSIkkaKDRPKRQHDRPRHEDNRGGGNDVAPKEDFEQKMS 110
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
618-702 1.44e-05

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 48.48  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 618 DELKKAEYM--IQHIGD-----EFEGIVSSVANFGMFIElpntI----EGMVHIANMTDdyyRFEERQMaligerqaKVF 686
Cdd:COG2183  622 PEFKTPTFRegVLKIEDlkpgmILEGTVTNVTDFGAFVD----IgvhqDGLVHISQLSD---RFVKDPR--------EVV 686
                         90
                 ....*....|....*.
gi 925922904 687 RIGDTVKVKVTHVDVD 702
Cdd:COG2183  687 KVGDIVKVKVLEVDLK 702
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
631-706 1.91e-05

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 48.19  E-value: 1.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904  631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:TIGR00717 273 GDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKN----------SHPSKVVKKGDEVEVMILDIDPERRRL 338
rpsA PRK13806
30S ribosomal protein S1; Provisional
608-704 2.17e-05

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 47.80  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 608 RRAIEAERDTDElkkAEYMIQ-HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddYYRFEERQMALigerqakvf 686
Cdd:PRK13806 182 RALLEREQKEAL---EAFMETvKEGDVVEGTVTRLAPFGAFVELAPGVEGMVHISELS--WSRVQKADEAV--------- 247
                         90
                 ....*....|....*...
gi 925922904 687 RIGDTVKVKVTHVDVDER 704
Cdd:PRK13806 248 SVGDTVRVKVLGIERAKK 265
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
608-706 5.47e-05

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 46.65  E-value: 5.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  608 RRAIEAERdtdELKKAEYMIQ-HIGDEFEGIVSSVANFGMFIELpNTIEGMVHIANMTDDYYRfeerqmaligeRQAKVF 686
Cdd:TIGR00717 167 RAYLEEER---SQAREELLENlKEGDVVKGVVKNITDFGAFVDL-GGVDGLLHITDMSWKRVK-----------HPSEYV 231
                          90       100
                  ....*....|....*....|
gi 925922904  687 RIGDTVKVKVTHVDVDERLI 706
Cdd:TIGR00717 232 KVGQEVKVKVIKFDKEKGRI 251
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
630-706 9.13e-05

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: 41.47  E-value: 9.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYyrfeerqmaliGERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd05706    3 VGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDY-----------SEALPYKFKKNDIVRACVLSVDVPNKKI 68
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
631-706 2.20e-04

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: 40.25  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrFEERQMAligerQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd05689    4 GTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMD-----WTNKNIH-----PSKVVSLGDEVEVMVLDIDEERRRI 69
rpsA PRK06676
30S ribosomal protein S1; Reviewed
608-710 2.22e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 44.48  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 608 RRAI-EAERdtdELKKAEYMIQ-HIGDEFEGIVSSVANFGMFIELpNTIEGMVHIANMTddYYRFeerqmaligERQAKV 685
Cdd:PRK06676 171 RRAVvEEER---AAKKEELLSSlKEGDVVEGTVARLTDFGAFVDI-GGVDGLVHISELS--HERV---------EKPSEV 235
                         90       100
                 ....*....|....*....|....*
gi 925922904 686 FRIGDTVKVKVTHVDVDERLIDFQI 710
Cdd:PRK06676 236 VSVGQEVEVKVLSIDWETERISLSL 260
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
634-699 2.74e-04

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: 40.30  E-value: 2.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925922904 634 FEGIVSSVANFGMFIELPNTI---EGMVHIANMTddyyrfEERQMALIGErqakVFRIGDTVKVKVTHV 699
Cdd:cd05684    4 YKGKVTSIMDFGCFVQLEGLKgrkEGLVHISQLS------FEGRVANPSD----VVKRGQKVKVKVISI 62
rpsA PRK06299
30S ribosomal protein S1; Reviewed
629-706 2.89e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 44.38  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDyyrfeerqmaligerQ-----AKVFRIGDTVKVKVTHVDVDE 703
Cdd:PRK06299 285 PVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWT---------------KknkhpSKVVSVGQEVEVMVLEIDEEK 349

                 ...
gi 925922904 704 RLI 706
Cdd:PRK06299 350 RRI 352
rpsA PRK07899
30S ribosomal protein S1; Reviewed
630-706 3.85e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 43.88  E-value: 3.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrfeERQMaligERQAKVFRIGDTVKVKVTHVDVDERLI 706
Cdd:PRK07899 293 IGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-------ERHV----EVPEQVVQVGDEVFVKVIDIDLERRRI 358
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
631-706 4.38e-04

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: 39.14  E-value: 4.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEERQmaligerqakvFRIGDTVKVKVTHVDVDERLI 706
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHPEKK-----------FKPGLKVKCRVLSVEPERKRL 65
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
630-733 5.44e-04

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: 43.18  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904  630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMT-DDYYRFEERQmaligerqakvFRIGDTVKVKVTHVDVDERLIDF 708
Cdd:TIGR00717 359 VGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISwDKDGREADHL-----------YKKGDEIEAVVLAVDKEKKRISL 427
                          90       100
                  ....*....|....*....|....*.
gi 925922904  709 QIVGM-PLPKNDRSQRPARGKTIQAK 733
Cdd:TIGR00717 428 GVKQLtENPWEKFAAKYKVGSVVKGK 453
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
630-710 6.36e-04

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 43.55  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTddyyrfeERQMALIGERQAKvFRIGDTVKVKVTHVDVDERLIDFQ 709
Cdd:PRK12269 752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLV-------ENRDGDPGEALRK-YAVGDRVKAVIVDMNVKDRKVAFS 823

                 .
gi 925922904 710 I 710
Cdd:PRK12269 824 V 824
PRK08059 PRK08059
general stress protein 13; Validated
630-729 1.01e-03

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 39.64  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERLIDFQ 709
Cdd:PRK08059   7 VGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFV-----------KDIHDFLSVGDEVKVKVLSVDEEKGKISLS 75
                         90       100
                 ....*....|....*....|.
gi 925922904 710 IVGM-PLPKNDRSQRPARGKT 729
Cdd:PRK08059  76 IRATeEAPEAKRKKGKILIPN 96
OB_Dis3 pfam17849
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 ...
155-223 1.29e-03

Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 protein. This domain along with CSD1 binds to RNA.


Pssm-ID: 436091 [Multi-domain]  Cd Length: 77  Bit Score: 37.97  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925922904  155 FVIPDDKRI---------MQDIFIPKGQSLgavDGHKVLVQITKYADGSDNPEGHISAILGHKNDPGVDILSIIYQHG 223
Cdd:pfam17849   3 LFVPRDKRIpririptksAPEEFLENPEDL---EGKLFVVKIDDWPENSRYPLGHIVKVLGEIGDIETETEAILLENG 77
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
606-700 1.59e-03

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 41.86  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 606 RERRAIEAERDTDELKKaeymiqhiGDEFEGIVSSVANFGMFIELpNTIEGMVHIANMTddYYRFeerqmaligERQAKV 685
Cdd:PRK00087 461 EEEKEKKKEETWNSLEE--------GDVVEGEVKRLTDFGAFVDI-GGVDGLLHVSEIS--WGRV---------EKPSDV 520
                         90
                 ....*....|....*
gi 925922904 686 FRIGDTVKVKVTHVD 700
Cdd:PRK00087 521 LKVGDEIKVYILDID 535
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
629-702 1.67e-03

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 37.95  E-value: 1.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925922904 629 HIGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVD 702
Cdd:cd04461   13 KPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFV-----------TDPSFGFKKGQSVTAKVTSVDEE 75
S1_Rrp5_repeat_hs12_sc9 cd05703
S1_Rrp5_repeat_hs12_sc9: Rrp5 is a trans-acting factor important for biogenesis of both the ...
631-707 2.39e-03

S1_Rrp5_repeat_hs12_sc9: 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 12 (hs12) and S. cerevisiae S1 repeat 9 (sc9). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240208 [Multi-domain]  Cd Length: 73  Bit Score: 37.17  E-value: 2.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYRFEERQmaligerqaKVFRIGDTVKVKVTHVDVDERLID 707
Cdd:cd05703    1 GQEVTGFVNNVSKEFVWLTISPDVKGRIPLLDLSDDVSVLEHPE---------KKFPIGQALKAKVVGVDKEHKLLR 68
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
631-696 3.12e-03

S1_Rrp5_repeat_hs11_sc8: 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 11 (hs11) and S. cerevisiae S1 repeat 8 (sc8). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240207 [Multi-domain]  Cd Length: 70  Bit Score: 36.80  E-value: 3.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925922904 631 GDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYyrfeerqmaLIGERQAKVFRIGDTVKVKV 696
Cdd:cd05702    1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVFDEW---------PDGKNPLSKFKIGQKIKARV 57
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
615-745 4.30e-03

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 40.65  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 615 RDTDELKKAEYMIQHI------GDEFEGI-VSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFR 687
Cdd:PLN00207 732 KDLSSLEKSKAIISSLtmvptvGDIYRNCeIKSIAPYGAFVEIAPGREGLCHISELSSNWL-----------AKPEDAFK 800
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 925922904 688 IGDTVKVKVTHVDVDERLIDFQIVGMPLPKNDR-SQRPARGKTIQAKTRGKSLDKSKSD 745
Cdd:PLN00207 801 VGDRIDVKLIEVNDKGQLRLSRRALLPEANSEKsSQKQQGGSTKDKAPQKKYVNTSSRP 859
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
634-705 7.28e-03

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: 35.92  E-value: 7.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925922904 634 FEGIVSSVANFGMFIELPN-TIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVTHVDVDERL 705
Cdd:cd05686    7 FKGEVASVTEYGAFVKIPGcRKQGLVHKSHMSSCRV-----------DDPSEVVDVGEKVWVKVIGREMKDKM 68
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
636-706 7.39e-03

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 35.66  E-value: 7.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925922904 636 GIVSSVANFGMFIELPNTIEGMVHIANMTDDYyrfeerqmaliGERQAKVFRIGDTVKVKVTHVDVD-ERLI 706
Cdd:cd05698    6 GTIVKVKPNGCIVSFYNNVKGFLPKSELSEAF-----------IKDPEEHFRVGQVVKVKVLSCDPEqQRLL 66
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
630-711 7.58e-03

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: 36.05  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYyrfeerqmaligerqakvfRIGDTVKVKVTHVDvDERLIDFQ 709
Cdd:cd04473   16 VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNLLRDY-------------------EVGDEVIVQVTDIP-ENGNIDLI 75

                 ..
gi 925922904 710 IV 711
Cdd:cd04473   76 PV 77
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
630-703 8.02e-03

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 36.99  E-value: 8.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925922904 630 IGDEFEGIVSSVANFGMFIELPNTIEGMVHIANMTDDYYrfeerqmaligERQAKVFRIGDTVKVKVthVDVDE 703
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFI-----------DNIHQLLKVGEEVLVQV--VDFDE 63
 
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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