ID K6YYX1_9ALTE Unreviewed; 803 AA.
AC K6YYX1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ECO:0000313|EMBL:GAC16405.1};
GN ORFNames=GLIP_3794 {ECO:0000313|EMBL:GAC16405.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16405.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC16405.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC16405.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC16405.1}.
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DR EMBL; BAEN01000070; GAC16405.1; -; Genomic_DNA.
DR RefSeq; WP_008846207.1; NZ_BAEN01000070.1.
DR AlphaFoldDB; K6YYX1; -.
DR STRING; 1127673.GLIP_3794; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000006334; 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; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000006334};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 650..731
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 91385 MW; 81EC63439DF545D6 CRC64;
MNIKNKQNLE KNDPHFLREK DKYENPVASR EYLFQVLVEQ KTPLTFLEIC QFVKALDEDS
RVGVQRRLRA MEREGQIVFN RQKKYGLADK MELIKGRVIG HRDGFGFLKR DDGEKDLFIH
QAQMQALLHD DIVLVKESGT DNRGRREARI ARIIEPRTEP IVGRYFVEHG VSMVIPDDSR
IGHEIMIPAE HVNGARQGNV VVVEILQRPR KRVNPIGKIL EVLGEHMAPG MEIEMALRTF
DIPHQWPKAV SKQIANLNEQ VPEEAKQNRI DLRQLPLVTI DGEDARDFDD AVFCEPLDEG
GWQLWVAIAD VSYYVKTGTA LDNEAQVRGN SVYFPEQVVP MLPEVLSNGL CSLNPEVDRL
CMVCEMTVSA QGKLKDYQFY EAVMNSKARL TYSKVGEILD GNPELHKRYA EHVPHLRNLH
NMYRVLKRAR NNRGAIEFET QESKFVFNAQ RKIDHIVPVV RNDAHKLIEE CMILANVSAA
KFLEQNKAPA LYRIHDEPNE DRLTSFTSYL KEVGIEHRIG KEAKPQDFTD LVSKIQGRPD
QELIQTMLLR SMKQAVYDSD NIGHFGLALE AYAHFTSPIR RYPDLVVHRA IKAVLDKQAS
RKSKTGGKSY NAEEVEALGE QCSMTERRAD DATRDVADWL KCEFMLDHVG DVFEGVIASV
TGFGFFVRLG EFHIDGLVHI SSLENDYYHF DEVKQCLVGE AMGKRYRLGD PLKVKVAAVN
LDERKIDFIL DEPKGRGARK AAGAKRGKTN KKDNADRESN QNNNATATKQ PAKKGTGKPS
RRTTDKSSSK APKSKRRTAK RNK
//
