ID D0LU85_HALO1 Unreviewed; 1004 AA.
AC D0LU85;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Hoch_4960 {ECO:0000313|EMBL:ACY17449.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17449.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY17449.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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 -!- FUNCTION: Might have a role in establishing the nucleoid structure of
CC elementary bodies. {ECO:0000256|ARBA:ARBA00002344}.
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 -!- SIMILARITY: Belongs to the histone H1/H5 family. HCT subfamily.
CC {ECO:0000256|ARBA:ARBA00008424}.
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DR EMBL; CP001804; ACY17449.1; -; Genomic_DNA.
DR AlphaFoldDB; D0LU85; -.
DR STRING; 502025.Hoch_4960; -.
DR KEGG; hoh:Hoch_4960; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_3_7; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
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; IPR009970; HC2.
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; PF07382; HC2; 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; 3.
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:UP000001880};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 864..945
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 70..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..182
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 108694 MW; B88505D40C870A8F CRC64;
MTNTDLFDTG SVLAALEDAG AAGLKIAALE DALGLSDDQD GEAQRARLRR LLTKMAKDGA
LTRPARGVYA APAKAATQGA KKATKKAAAK KAAAKKAATK KAATKKAATK KAATKKAATK
KAATKKAATK KAATKKAATK KAATKKAATK KAATKKAATK KAATKKAATK KAATKKAATK
KAATKKKDAA AKQSATKTAA SDEPSTKKAA AKKAPKKKAP AKSPKSKRGA AKAAAPAHEE
PASEAPEAVE DAASGEGTDE FYEPPERERL HPSQIPGAEI TRTRRGETRP EEDLSRTGRI
TVHPAGYGFV ELEDGTGTVF VPARHRGAAL DGDRVVLNTW SGYKGTEGRV IEVLSRGRAK
LTGTLQRTGR AVYLEPDDPR IATDYGHVPL IDGPPQSKVG QAAVVEICRY PTHERPELVG
RLVRVLGKPD DPRTEIEKIL AFADLPTEFP RDVARRGDET STTVRTRDQV DRVDLRDRPF
VTIDPVTARD FDDAVCIEDG PHGGPRVWVA VADVSHYVEI DDPIDREAAV RGVSVYLPDR
VVPMLPLPLS AGICSLNPEV DRCAMVVRLD LTDDGRVLER DFAAAVIRSH ARLDYPGVAA
ALSGDFRGRR DHYRPWAPAL SRLAALAQRM RTRRRARGAL ELTLAEPYVI LDADEAELVR
DIVRSKGAED VRQAYELVEE FMIAANEAVG KYFAERNLPT VWRIHAPPEP DRLHELLPVL
ANFGIKLTVE DIEAATKPTG MRRIIEAIEG QPAAASLSFQ VLRSLKQAQY STDPIGHFGL
ASPFYLHFTS PIRRYADLLV HRQLKHYLHA DGKPSGGGAR IPAADIDTLA ERCAQISTHE
RRAVEVEREA VSMYRAYFMR GQVGEQFTGR VSAVTNFGAF VELDAPFVEG LIKLDDLGAD
AFGFDASSMR LRGRRSGLRL GLGDPVTIEV TNVSVARRRI DFKLISVAGR SSPSGGESSG
EDEGTPYWKS RRSRNKRPGG RDKDRGKGKN KGKSRSGKRR SRRQ
//
