ID   ILL1_ORYSI              Reviewed;         442 AA.
AC   Q84XG9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=IAA-amino acid hydrolase ILR1-like 1;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=ILL1; Synonyms=IAR; ORFNames=OsI_002388;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lin C.F., Yang J.S.;
RT   "Isolation and chararcterization of a putative IAR in rice.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Hydrolyzes certain amino acid conjugates of the plant growth
CC       regulator indole-3-acetic acid (IAA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR   EMBL; AY187620; AAO25632.1; -; mRNA.
DR   EMBL; CM000126; EAY74541.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84XG9; -.
DR   SMR; Q84XG9; -.
DR   STRING; 39946.Q84XG9; -.
DR   MEROPS; M20.014; -.
DR   EnsemblPlants; BGIOSGA001413-TA; BGIOSGA001413-PA; BGIOSGA001413.
DR   Gramene; BGIOSGA001413-TA; BGIOSGA001413-PA; BGIOSGA001413.
DR   HOGENOM; CLU_023257_0_0_1; -.
DR   OMA; VNKGMMH; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009850; P:auxin metabolic process; IEA:InterPro.
DR   CDD; cd08017; M20_IAA_Hyd; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR044757; ILR1-like_Hyd.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF119; IAA-AMINO ACID HYDROLASE ILR1-LIKE 1; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..442
FT                   /note="IAA-amino acid hydrolase ILR1-like 1"
FT                   /id="PRO_0000351637"
FT   MOTIF           439..442
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ   SEQUENCE   442 AA;  47195 MW;  CCF1952348EA4B39 CRC64;
     MAAASSSRVL LAAVAVLAAA LAGCGAGAAL DDPAGLLRRA KEAEFAGWMV GLRRRIHENP
     ELGYEEFATS ELVRRELDAL GIPYRHPFAV TGVVATVGTG GPPFVALRAD MDALPMQESV
     EWEHKSKVPG KMHGCGHDAH VAMLLGSARI LQEHRDELKG TVVLVFQPAE EGGGGAKKMI
     DDGTVENIEA IFGVHVADVV PIGVVASRPG PVMAGSGFFE AVISGKGGHA ALPHHTIDPI
     LAASNVIVSL QQLVSREADP LDSQVVTVGK FQGGGAFNVI PDSVTIGGTF RAFLKESFNQ
     LKQRIEEVIV SQASVQRCNA VVDFLDKDRP FFPPTINSAG LHDFFVKVAS EMVGPKNVRD
     KQPLMGAEDF AFYADAIPAT YYYFLGMYNE TRGPQAPHHS PYFTINEDAL PYGAALQASL
     ATRYLLEHQP PTTGKAKAHD EL
//