(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIL1_GEOS0

ID   A0A0F6BIL1_GEOS0        Unreviewed;       761 AA.
AC   A0A0F6BIL1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN   Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   OrderedLocusNames=GY4MC1_0422 {ECO:0000313|EMBL:ADP73262.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73262.1};
RN   [1] {ECO:0000313|EMBL:ADP73262.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73262.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01895, ECO:0000256|SAAS:SAAS01124678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00089931}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002293; ADP73262.1; -; Genomic_DNA.
DR   RefSeq; WP_013400012.1; NC_014650.1.
DR   EnsemblBacteria; ADP73262; ADP73262; GY4MC1_0422.
DR   KEGG; gmc:GY4MC1_0422; -.
DR   KO; K12573; -.
DR   OMA; DWYEYRS; -.
DR   OrthoDB; 1602988at2; -.
DR   BioCyc; GSP581103:G1GOQ-469-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR040476; CSD2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR011805; RNase_R.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF17876; CSD2; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 2.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 2.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIL1.
DR   SWISS-2DPAGE; A0A0F6BIL1.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895, ECO:0000256|SAAS:SAAS00462075};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089915};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895, ECO:0000256|SAAS:SAAS00446781};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895, ECO:0000256|SAAS:SAAS00462054};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN          627..707
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          714..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          599..619
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        714..731
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  87269 MW;  1B91F4ED7EF290D3 CRC64;
     MDQSLVERIL TFMQDEAYKP LTVQELEEAF GITDAAAFKE FVKALVAMEE QGLVVRTRSN
     RYGVPEKMNL VRGKVSGHAK GFAFVVPDDP ELDDIFIPPS EMKNAMHGDT VLVRVHADSS
     GARREGTIVR ILERGVTEVV GTYTESKYFG FVIPDDKKIV NDIFIPKHAA NGAVEGHKVV
     VRLTSYPQGR MSAEGEVVKI LGHKNDPGVD ILSIIHKHGL PLQFPDEVLE HANRISDTIS
     EKDLQGRRDL RDQMIVTIDG EDAKDLDDAV TVTKLANGHY KLGVHIADVS YYVEEGSPID
     REAYERGTSV YLVDRVIPMI PHRLSNGICS LNPKVDRLTI SCEMEINERG EVVSHEIFQS
     VIRTTERMTY SDVNKILVDK DEELRKKYAP LVPMFELMAE LAEILRNKRM KRGAIDFDFK
     EAKVLVDENG KPYDVVLRER SVAERLIEEF MLAANETVAE HFHWLNVPFI YRVHEDPKPE
     KLQRFLEFIT NFGYVVKGTG NQIHPRALQE ILEAVRGEPE EMLISTVMLR SMKQARYDAE
     SLGHYGLSTD FYTHFTSPIR RYPDLIVHRL IRTYLINGQM DEQTQQKWAE KLPDIAAHAS
     NMERRAVEAE RETDDLKKTE FMEDKIGMEF DGIISSVTNF GLFVELPNTI EGLVHVSYLT
     DDYYHYDERS YAMIGERTGK VYRIGDQITV RVINVNKDER IVDFEIVGMK DRRRKEPKHA
     PVVIEGKKRK KRNKDEKTKK AKKFYEDIPK LKAKKKKKKK K
//

If you have problems or comments...

PBIL Back to PBIL home page