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Database: UniProt
Entry: A0A1H3Y4R3_ALKAM
LinkDB: A0A1H3Y4R3_ALKAM
Original site: A0A1H3Y4R3_ALKAM 
ID   A0A1H3Y4R3_ALKAM        Unreviewed;       521 AA.
AC   A0A1H3Y4R3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN04488051_101515 {ECO:0000313|EMBL:SEA05854.1};
OS   Alkalimonas amylolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX   NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA05854.1, ECO:0000313|Proteomes:UP000198773};
RN   [1] {ECO:0000313|EMBL:SEA05854.1, ECO:0000313|Proteomes:UP000198773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA05854.1,
RC   ECO:0000313|Proteomes:UP000198773};
RA   de Groot N.N.;
RL   Submitted (OCT-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 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|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; FNRM01000001; SEA05854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3Y4R3; -.
DR   STRING; 152573.SAMN04488051_101515; -.
DR   Proteomes; UP000198773; 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   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; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; 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; 2.
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:UP000198773};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          374..455
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          456..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  58810 MW;  5FFFF3A7530ECA75 CRC64;
     MPFVTIDGED ARDFDDAVYA EPRDDGGWRL WVAIADVSSY VQVDTPLDQE ALLRGTSVYF
     PDQVVPMLPE ALSNGLCSLN PHVDRLCLVA EMDIGANGKL MNYRFFEAVM NSKARLTYSK
     VHAILQGDLA LRQQYEANLT ALETLYSLYR RLAKTRAQRG AIEFETVETR FIFNSHRKIE
     QIVPVHRNDA HKLIEECMIM ANVAAARFLE KHKTPALYRV HEQPDPDRFA NFRRFLAELG
     IETTLPDEPE PLQLVQELAK LADRPDRELI ETTLLRSMKQ AVYQGDNQGH FGLALPAYAH
     FTSPIRRYPD LVVHRSIKSI LQQQGQRTKG AHRYSPEQVE QLGEHCSMTE RRADDATREV
     SDWLKCEYMQ DHLGMEFDGV VSTVTSFGLF IRLTELYIEG LVHVTSLKND YYHFDAERQI
     LMGEHSRQGY RLGDLVKVKV MAVNLESRTI DLALEESGTP RRSKGKAKDK DPASPLPGKV
     VVKSAKKPAG TRRKAVAAKP AAKGRPGKPA GKGKPKAKKK S
//
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