RNMC_MOMCH
ID RNMC_MOMCH Reviewed; 191 AA.
AC P23540;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Ribonuclease MC;
DE Short=RNase MC;
DE EC=4.6.1.19;
OS Momordica charantia (Bitter gourd) (Balsam pear).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX NCBI_TaxID=3673;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=2060635; DOI=10.1016/0014-5793(91)80675-s;
RA Ide H., Kimura M., Arai M., Funatsu G.;
RT "The complete amino acid sequence of ribonuclease from the seeds of bitter
RT gourd (Momordica charantia).";
RL FEBS Lett. 284:161-164(1991).
RN [2]
RP ERRATUM OF PUBMED:2060635.
RX PubMed=1894001; DOI=10.1016/0014-5793(91)80924-r;
RA Ide H., Kimura M., Arai M., Funatsu G.;
RL FEBS Lett. 289:126-126(1991).
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 -!- MISCELLANEOUS: Has a remarkably high specificity toward CPU, APU, and
CC UPU.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S17505; S17505.
DR PDB; 1BK7; X-ray; 1.75 A; A=1-191.
DR PDB; 1J1F; X-ray; 1.60 A; A=1-191.
DR PDB; 1J1G; X-ray; 1.60 A; A=2-191.
DR PDB; 1UCA; X-ray; 1.48 A; A=1-191.
DR PDB; 1UCC; X-ray; 1.77 A; A=1-191.
DR PDB; 1UCD; X-ray; 1.30 A; A=1-191.
DR PDB; 1UCG; X-ray; 1.65 A; A/B=2-191.
DR PDB; 1V9H; X-ray; 2.00 A; A=1-191.
DR PDBsum; 1BK7; -.
DR PDBsum; 1J1F; -.
DR PDBsum; 1J1G; -.
DR PDBsum; 1UCA; -.
DR PDBsum; 1UCC; -.
DR PDBsum; 1UCD; -.
DR PDBsum; 1UCG; -.
DR PDBsum; 1V9H; -.
DR AlphaFoldDB; P23540; -.
DR SMR; P23540; -.
DR BRENDA; 4.6.1.19; 3398.
DR EvolutionaryTrace; P23540; -.
DR Proteomes; UP000504603; Unplaced.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Lyase; Nuclease; Reference proteome.
FT CHAIN 1..191
FT /note="Ribonuclease MC"
FT /id="PRO_0000206508"
FT ACT_SITE 34
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT DISULFID 48..92
FT /evidence="ECO:0000250"
FT DISULFID 152..185
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1UCD"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1UCD"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1UCD"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1UCD"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1UCD"
SQ SEQUENCE 191 AA; 21260 MW; A67958CB471DC7D2 CRC64;
FDSFWFVQQW PPAVCSFQKS GSCPGSGLRT FTIHGLWPQG SGTSLTNCPQ GSPFDITKIS
HLQSQLNTLW PNVLRANNQQ FWSHEWTKHG TCSESTFNQA AYFKLAVDMR NNYDIIGALR
PHAAGPNGRT KSRQAIKGFL KAKFGKFPGL RCRTDPQTKV SYLVQVVACF AQDGSTLIDC
TRDTCGANFI F
