ID I3I8Z6_9GAMM Unreviewed; 959 AA.
AC I3I8Z6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=O59_002861 {ECO:0000313|EMBL:EIK44531.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK44531.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK44531.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK44531.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIK44531.1}.
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DR EMBL; AICM01000006; EIK44531.1; -; Genomic_DNA.
DR RefSeq; WP_007643473.1; NZ_JH668202.1.
DR AlphaFoldDB; I3I8Z6; -.
DR STRING; 1134474.O59_002861; -.
DR PATRIC; fig|1134474.3.peg.2693; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000003395; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
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; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
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; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 661..742
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 750..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 105989 MW; 8C35F2C7838C9BAF CRC64;
MSKRKSPFKD PFAAREAEKY ENPIPSREYI LELLDTAAEP VTHEQMCAML KLTGEDQIEA
LRRRLIAMAR DGQLISNRRD AYVRLDKIDV VRGRVQGHRD GYGFVIPSEG GEDIYLHNRQ
MRKVFDGDEV LVRLSGEQYR GKEEGAIIEV LIRNTTQLAG RFFNEEGVQF VRPENPRITH
DIMIPFGAYG GAKHGQIVVA EITQQPDKNR LPTGRVVQVL GDHMAPGMEI ELAIQAHGIP
SVWPEAVIAE AARLSHEVEE KDKLHRVDVR HLPFVTIDGE DARDFDDAVL CERRKGGWRL
YVAIADVSHY VQVESALDVE ARARGNSVYF PDYVVPMLPE ALSNGLCSLN PNVDRLCMIC
EMNISTAGRI TGYQFYEGVM HSHARLTYTK VGEILTGEGE TRAALREEYK AVIPQLELLH
KLYECLRAAR DERGAIDFET TETRIQFNDE RKIERIVPIK RNDAHKLIEE CMLCANVCAA
TFIEKHNLVG LFRVHEGPTE TKLANLRAYL SELGLGLAGG DKPTPGDYQQ LLQMIQDRSD
GHLIQTVMLR SLRQAMYQVE NHGHFGLGYE AYTHFTSPIR RYPDLLVHRA IRSVIRSTEP
TTHVRRVDTA KAIPKKFIYP YTAAEMLVFG EQCSRTERRA DEATRDVVSW LKCEYLRDQV
GAIYDGHVSA VTSFGLFVEL NELYVEGLIH ITSLPHDYYR FEPAQHRLMG ERTRKVFGLG
DSLVVRVVRV DLDNRKIDFE LESEAAIRRP KSQVKPKVAK RDAKNAAKKS AANKQDVKQV
VAKPAIATAV PEKAATKKPA TKNTATKKTT AKKPAVKKPA SVKPASTKPE GSKSGGAKAA
VAKVTGKKLA ATDVAAAKPA VKKSNSKVSV AKAESAGAAK KTAAPKTAAV KKVAAAVPAK
KTTKAASEVS HGRKNAKATS KAAPATVQPS PSGATKGKAV ARAAAPTAKK PVAKAKTTK
//
