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Database: UniProt
Entry: A0A022Q5W5_ERYGU
LinkDB: A0A022Q5W5_ERYGU
Original site: A0A022Q5W5_ERYGU 
ID   A0A022Q5W5_ERYGU        Unreviewed;       317 AA.
AC   A0A022Q5W5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Strictosidine synthase conserved region domain-containing protein {ECO:0000259|Pfam:PF03088};
DE   Flags: Fragment;
GN   ORFNames=MIMGU_mgv1a0246431mg {ECO:0000313|EMBL:EYU22994.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU22994.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU22994.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
CC   -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC       {ECO:0000256|ARBA:ARBA00009191}.
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DR   EMBL; KI632189; EYU22994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022Q5W5; -.
DR   STRING; 4155.A0A022Q5W5; -.
DR   eggNOG; KOG1520; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR   PANTHER; PTHR10426:SF88; PROTEIN STRICTOSIDINE SYNTHASE-LIKE 4-RELATED; 1.
DR   PANTHER; PTHR10426; STRICTOSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF20067; SSL_N; 1.
DR   Pfam; PF03088; Str_synth; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW   Signal {ECO:0000256|SAM:SignalP}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..317
FT                   /note="Strictosidine synthase conserved region domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001506602"
FT   DOMAIN          159..246
FT                   /note="Strictosidine synthase conserved region"
FT                   /evidence="ECO:0000259|Pfam:PF03088"
FT   NON_TER         317
FT                   /evidence="ECO:0000313|EMBL:EYU22994.1"
SQ   SEQUENCE   317 AA;  35015 MW;  37E0262BCACC0F76 CRC64;
     MANIAILISR LPVVAAVLLY QIDPFDPAPY PDHELTRNGE PLFIPKRNSQ MLLGSEKIGF
     GELPAPEDIA YDPKTGVIYT GCVDGWLRRV SLKGSAAAAA DFVVEEWVNT GGRPLGIVHG
     IHGEVIVADA DKGLLNISRD GVIELLTDEA DGLKFKLTDA VDIGPDGTLY FTDASYKHNF
     KNHFEDFLEG RPNGRFLSYD PSTKQTQVLV KDLYFANGVA LSADQSFVIF CETAMMRCKK
     YYIQGPSKGS VDIFVENLPG LPDNIRYDGE GQYWIALTTD TSVWKLAQRY PFIRKVIAMV
     DRYIGRPSTE KNGGVIA
//
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