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Database: UniProt
Entry: I1HHP1_BRADI
LinkDB: I1HHP1_BRADI
Original site: I1HHP1_BRADI 
ID   I1HHP1_BRADI            Unreviewed;       323 AA.
AC   I1HHP1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   08-NOV-2023, entry version 54.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE            Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE            EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN   Name=100832852 {ECO:0000313|EnsemblPlants:KQK05422};
GN   ORFNames=BRADI_2g19980v3 {ECO:0000313|EMBL:KQK05422.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK05422.1};
RN   [1] {ECO:0000313|EMBL:KQK05422.1, ECO:0000313|EnsemblPlants:KQK05422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK05422.1,
RC   ECO:0000313|EnsemblPlants:KQK05422};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK05422.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK05422.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK05422}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK05422};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001585,
CC         ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR006431}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR006431,
CC       ECO:0000256|RuleBase:RU003421}.
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DR   EMBL; CM000881; KQK05422.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1HHP1; -.
DR   EnsemblPlants; KQK05422; KQK05422; BRADI_2g19980v3.
DR   Gramene; KQK05422; KQK05422; BRADI_2g19980v3.
DR   HOGENOM; CLU_043739_2_1_1; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   ExpressionAtlas; I1HHP1; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   NCBIfam; TIGR01249; pro_imino_pep_1; 1.
DR   PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR   PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW   Protease {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT   DOMAIN          41..303
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT   ACT_SITE        299
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ   SEQUENCE   323 AA;  36831 MW;  E86D83BD3F3E5521 CRC64;
     MDLSPRKDLY PHVEPYDTGR LKVSDVHTIY YEQSGNPGGH PVVFLHGGPG AGTSPGNRRF
     FDPEFYRIVL FDQRGAGKST PHACLEENTT WDLVSDIEKL REHLDIPEWQ VFGGSWGSTL
     ALAYSQTHPD KVTGIVIRGI FLLRKKELDW FYEGGAATIF PDAWEPFRDF IPEDERNCFI
     AAYSKRLTSS DANLQIEAAK RWTMWEMMTA HLIQNHENIK RGNDDKFSLA FARIENHYFV
     NKGFLPSDSH LLDNVDKIRH IKAFIVQGRY DVCCPMMSAW DLHKAWPEAE FKVVPDAGHS
     ANEIGVAAEL VSANEKFKSM LRK
//
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