ID A0A0K2JJL4_SPIKU Unreviewed; 705 AA.
AC A0A0K2JJL4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SKUN_001583 {ECO:0000313|EMBL:ALA98441.1};
OS Spiroplasma kunkelii CR2-3x.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=273035 {ECO:0000313|EMBL:ALA98441.1, ECO:0000313|Proteomes:UP000062963};
RN [1] {ECO:0000313|EMBL:ALA98441.1, ECO:0000313|Proteomes:UP000062963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR2-3x {ECO:0000313|EMBL:ALA98441.1,
RC ECO:0000313|Proteomes:UP000062963};
RX PubMed=26494665;
RA Davis R.E., Shao J., Dally E.L., Zhao Y., Gasparich G.E., Gaynor B.J.,
RA Athey J.C., Harrison N.A., Donofrio N.;
RT "Complete Genome Sequence of Spiroplasma kunkelii Strain CR2-3x, Causal
RT Agent of Corn Stunt Disease in Zea mays L.";
RL Genome Announc. 3:e01216-e01215(2015).
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}.
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DR EMBL; CP010899; ALA98441.1; -; Genomic_DNA.
DR RefSeq; WP_053391458.1; NZ_CP010899.1.
DR AlphaFoldDB; A0A0K2JJL4; -.
DR STRING; 273035.SKUN_001583; -.
DR KEGG; skn:SKUN_001583; -.
DR PATRIC; fig|273035.7.peg.1949; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000062963; Chromosome.
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 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; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 624..704
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 705 AA; 81903 MW; 2A23F6C605C894FC CRC64;
MHDRIVAILK KQTKPIDTIE LKQLLDINKI NDNKMMLKVL VELENDNIIG VTQQNRFYYF
DPKIYLRGVI SINKKGFGFI KISENQKEYY VKQDDLNNAL DQDQVLFILK KQKNINNYKK
AEAQVIKVLK RNNEYVVGVI KKNRHKQKYL EILNNKLMQY SAEIINLADA IENTIVKGII
TNINSKNNLM QVKIIEIIGN TNQVGVDVLA ILHEFNIRTK FNEETLNEAK QIKQDVDVAR
MLADKSRRDL QAEMFVTIDG NDSKDFDDAI LVKKNQNGNY LLLVAIADVA HYVPQNSYLD
KEAFDRGCSV YLIDRVVPML PEKLSNGICS LNPFEPRLTL ICEMEINKQG HVVNSSIYEA
ITISKVRLTY DEVNKLFCQE KNQISGEIAK MLFLSQQLYQ ILVLKKEHDG VVDFDLDEQK
FIVDKNGKIK DIVVRERADA EKLIESFMIR ANETVAETIY WMDLPFVYRV HDKPKPKKLF
DLYTQLSYLG LNIKGKLENI HSKDLQQILN KLKDKENFKV ISALVLRSME KAKYSAINDG
HFGLASRCYT HFTSPIRRYP DLVVHRLLKE YLFQGKVKIT NLEQKRTFVS HASQQSSLTE
LRAMECEREV DKMKEVEYME DKIGYEYNGI IAGVTSFGIF VELSNTIEGL IHITDLKNDY
YVFDEKNLKL IGERKRKEYF LGKKVRIKVK KASKKLRQID FELVD
//
