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Database: UniProt
Entry: A0A1M6BTK1_9FLAO
LinkDB: A0A1M6BTK1_9FLAO
Original site: A0A1M6BTK1_9FLAO 
ID   A0A1M6BTK1_9FLAO        Unreviewed;       739 AA.
AC   A0A1M6BTK1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-MAY-2019, entry version 12.
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   ORFNames=SAMN04487908_10349 {ECO:0000313|EMBL:SHI52027.1};
OS   Aequorivita viscosa.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=797419 {ECO:0000313|EMBL:SHI52027.1, ECO:0000313|Proteomes:UP000184172};
RN   [1] {ECO:0000313|EMBL:SHI52027.1, ECO:0000313|Proteomes:UP000184172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26349 {ECO:0000313|EMBL:SHI52027.1,
RC   ECO:0000313|Proteomes:UP000184172};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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
CC         yield nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01895,
CC         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
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR   EMBL; FQYV01000003; SHI52027.1; -; Genomic_DNA.
DR   RefSeq; WP_073214730.1; NZ_FQYV01000003.1.
DR   BioCyc; GCF_900106795:BLW28_RS02180-MONOMER; -.
DR   Proteomes; UP000184172; Unassembled WGS sequence.
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; 1.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000184172};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   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,
KW   ECO:0000256|SAAS:SAAS00446781};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184172};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN      652    733       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   739 AA;  84892 MW;  D6496F0361DF8F25 CRC64;
     MPKHKRKKNN KIANLSQTIL NILRKDHSKP YTYKQIAAKL QLDDPSSRNQ IIKKLKDLQG
     KGSIQEIERG KYILTPSQNY YTGKVDIAGR GQGYIIVEDL EDDIYVSSKN LNKALNGDIV
     EVYVFKRKKG GKTEGEVTKI IERKRTEFVG TIQVQENFAF VDVTDYKMYT DIFVPKNNIN
     GAKNGEKVLV LMEEWPAKAD SPLGKVIKVL GMPGEHNTEI HSILAQYGLP YEFPAEVEDY
     ANKIDTSIKA SEIKKRRDMR DILTFTIDPK DAKDFDDALS FQKLENGNVE IGIHIADVSH
     YVTPGNELDD EAYERATSVY LVDRVVPMLP EILSNNACSL RPHEEKYTFS AVFEMNQKAE
     IVKQWFGKTV TLSDTRFAYE EAQHIIETNV TSSAVEKSLN LTIPSDISIT DTEYTVQPEI
     ADAVLEMDRL AKKLRSRRMR AGAISFDKVE VKFILDEKSN PTGVYFKESK DANKLIEEFM
     LLANRSVAEF IGKQNPKKTF VYRVHDEPDD EKIAALENII RRFGYKLDTK DRHSTATSMN
     KLLKDVHGKK EQNLIDTLTI RSMSKALYTT NNIGHYGLAF DYYTHFTSPI RRYPDIMVHR
     LLQHYLDEGK SANQEDYEER CSHSSDMENL ATSAERDSIK YMQIKYMQDH QDEDFLGVIS
     GVTEWGIYIE IISNKCEGMV RLQDMQDDRY DFDRDEYAVI GQRTKKVYTL GDEVYVRVKN
     ADLVKKHLDF SMLGHREEA
//
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