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Database: UniProt
Entry: A0A067FZ63_CITSI
LinkDB: A0A067FZ63_CITSI
Original site: A0A067FZ63_CITSI 
ID   A0A067FZ63_CITSI        Unreviewed;       393 AA.
AC   A0A067FZ63;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Strictosidine synthase conserved region domain-containing protein {ECO:0000259|Pfam:PF03088};
GN   ORFNames=CISIN_1g016199mg {ECO:0000313|EMBL:KDO71440.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO71440.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO71440.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK784889; KDO71440.1; -; Genomic_DNA.
DR   RefSeq; XP_006467059.1; XM_006466996.2.
DR   AlphaFoldDB; A0A067FZ63; -.
DR   STRING; 2711.A0A067FZ63; -.
DR   PaxDb; 2711-XP_006467059-1; -.
DR   GeneID; 102625294; -.
DR   KEGG; cit:102625294; -.
DR   eggNOG; KOG1520; Eukaryota.
DR   OrthoDB; 1066791at2759; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          180..266
FT                   /note="Strictosidine synthase conserved region"
FT                   /evidence="ECO:0000259|Pfam:PF03088"
SQ   SEQUENCE   393 AA;  43637 MW;  480A02F563D50C0A CRC64;
     MPNSMPESVS ADTSSSSSSS RLWLVTVFLT GGPVFLAMLV YKLDSFDPAP IPVHEFTHPP
     LTAALRNERM LQGSEKVGYG VLKGPEDLLY DAHSKLIYTG CEDGWIKRVT LNDSPADSLV
     HNWINTGGRP LGIAFANSDP DADRITMIVA DAYKGLLKIS GNSTVLLTDE AEGQKFKLTD
     GVDVADDGMI YFTDASNKYY LREYILDIFE GKPNGRLLSF DPVTKETKVL VSDLYFANGV
     VLSPDQTHLV YCETSMRRCR KFYIKGKNAG RVEKFIETLP GLPDNIRYDG EGHYLIALAT
     EFSTYWDLAY RYPFIRKVSG MVVRYLGMPP MGKSSSGVFI VDLDGKPIAH YYDPEMSLIS
     SAIKIGDHLY CGSVHHRGIL HLDVNQHPAR AII
//
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