ID R0IHN8_9BRAS Unreviewed; 390 AA.
AC R0IHN8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Strictosidine synthase conserved region domain-containing protein {ECO:0000259|Pfam:PF03088};
GN ORFNames=CARUB_v10009397mg {ECO:0000313|EMBL:EOA37930.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA37930.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(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; KB870805; EOA37930.1; -; Genomic_DNA.
DR RefSeq; XP_006305032.1; XM_006304970.1.
DR AlphaFoldDB; R0IHN8; -.
DR STRING; 81985.R0IHN8; -.
DR GeneID; 17898312; -.
DR KEGG; crb:17898312; -.
DR eggNOG; KOG1520; Eukaryota.
DR OrthoDB; 1066791at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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:SF106; ADIPOCYTE PLASMA MEMBRANE-ASSOCIATED PROTEIN HEMOMUCIN-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:UP000029121};
KW Signal {ECO:0000256|SAM:SignalP}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..390
FT /note="Strictosidine synthase conserved region domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004353059"
FT DOMAIN 179..266
FT /note="Strictosidine synthase conserved region"
FT /evidence="ECO:0000259|Pfam:PF03088"
SQ SEQUENCE 390 AA; 43968 MW; 9D99F8B96122F26A CRC64;
MAMSIVAKIF IVFAIYCALD PFHHSSISKF PDFQTYKIDM PPLSSLPKER DRQNLLQNSE
IRFLNEVQGP ESIAFDPQGR GPYTGVADGR ILFWNGTRWT DFAYTSNNRS ELCDPKPSLL
DYLKDEHICG RPLGLRFDKN TGDLYIADAY LGIMKVGPQG GLATSLTTEA DGLPLRFTND
LDIDDQGNVY FTDSSSFFQR RKFLLLIVSG EDSGRVLKYN AKTKETTTLV RNLQFPNGLS
LGKDGSFFIF CEGSIGRLQK YWLKGEKAGT SEVVALLHGF PDNIRTNKDG DFWVAVHCHR
NIFTHVMAHH PRVRKFFLKL PISVKFQYLL QVGGWPHAVA VKYSEEGKVL KVLEDSQGKV
VKAVSEVEEK DGKLWMGSVL MSFIAVYDLP
//
