ID   RNDI_DICDI              Reviewed;         223 AA.
AC   Q7M438; Q54U37;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Ribonuclease DdI;
DE            Short=RNase DdI;
DE            EC=4.6.1.19;
DE   Flags: Precursor;
GN   Name=ddiA; Synonyms=ddi; ORFNames=DDB_G0281293;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-223, FUNCTION, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=9756633; DOI=10.1093/oxfordjournals.jbchem.a022189;
RA   Inokuchi N., Saitoh S., Kobayashi H., Itagaki T., Koyama T., Uchiyama S.,
RA   Iwama M., Ohgi K., Irie M.;
RT   "Characterization and primary structure of a base non-specific and acid
RT   ribonuclease from Dictyostelium discoideum.";
RL   J. Biochem. 124:848-856(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=10052134; DOI=10.1271/bbb.63.141;
RA   Inokuchi N., Saitoh S., Kobayashi H., Itagaki T., Koyama T., Uchiyama S.,
RA   Irie M.;
RT   "Comparison of base specificity and other enzymatic properties of two
RT   protozoan ribonucleases from Physarum polycephalum and Dictyostelium
RT   discoideum.";
RL   Biosci. Biotechnol. Biochem. 63:141-145(1999).
CC   -!- FUNCTION: Releases mononucleotides from RNA in the order of 3'-GMP >
CC       3'-UMP > 3'-AMP > 3'-CMP. {ECO:0000269|PubMed:10052134,
CC       ECO:0000269|PubMed:9756633}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC         phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC         H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC         COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046};
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+) and Zn(2+).
CC       {ECO:0000269|PubMed:9756633}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:9756633};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9756633}.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; AAFI02000040; EAL66943.1; -; Genomic_DNA.
DR   PIR; JE0316; JE0316.
DR   RefSeq; XP_640939.1; XM_635847.1.
DR   AlphaFoldDB; Q7M438; -.
DR   SMR; Q7M438; -.
DR   PaxDb; Q7M438; -.
DR   EnsemblProtists; EAL66943; EAL66943; DDB_G0281293.
DR   GeneID; 8623004; -.
DR   KEGG; ddi:DDB_G0281293; -.
DR   dictyBase; DDB_G0281293; ddiA.
DR   eggNOG; KOG1642; Eukaryota.
DR   HOGENOM; CLU_069912_2_1_1; -.
DR   InParanoid; Q7M438; -.
DR   OMA; DMRRYWP; -.
DR   PhylomeDB; Q7M438; -.
DR   PRO; PR:Q7M438; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; -; 1.
DR   InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR   InterPro; IPR001568; RNase_T2-like.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR018188; RNase_T2_His_AS_1.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR11240; PTHR11240; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; SSF55895; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Lyase; Lysosome; Nuclease; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:9756633"
FT   CHAIN           26..223
FT                   /note="Ribonuclease DdI"
FT                   /id="PRO_0000030989"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        46..51
FT                   /evidence="ECO:0000305"
FT   DISULFID        78..120
FT                   /evidence="ECO:0000305"
FT   DISULFID        183..213
FT                   /evidence="ECO:0000305"
FT   DISULFID        194..205
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="T -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="Y -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  24584 MW;  18696C460DAC494C CRC64;
     MRLIAALLSV LLIASTAQST VTIYESSKPG DFDFYLFVQQ WIYSYCDSQT CIQNKEREAF
     TIHGLWPENS DGSYPSFCSG PSFNVNAIQD LEDQLNFDWP SLTGPNTDFW THEFSKHGTC
     SITGPITDIH DYFATGIKLY TEFNITAALE SENIYPSDSN TYKPVDITNA ITTHFGGKPG
     IQCSSGQLST VAVCIDKNSL SIMDCPDLQG WSCSGSVKFP STA