ID A0A0E0A4X0_9ORYZ Unreviewed; 481 AA.
AC A0A0E0A4X0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G02940.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G02940.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G02940.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0A4X0; -.
DR STRING; 40148.A0A0E0A4X0; -.
DR MEROPS; M14.A02; -.
DR EnsemblPlants; OGLUM06G02940.1; OGLUM06G02940.1; OGLUM06G02940.
DR Gramene; OGLUM06G02940.1; OGLUM06G02940.1; OGLUM06G02940.
DR eggNOG; KOG2649; Eukaryota.
DR HOGENOM; CLU_006722_1_4_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18172; M14_CP_plant; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..481
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002353358"
FT TRANSMEM 443..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..134
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 222..232
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 481 AA; 53944 MW; A66CB5E580BF620F CRC64;
MAISRRLLLS LFLLRAFSSL PAQAAARGAS HPSGTSGNYG SFLRNLLQDN PMITEELVRG
YMSNSELEIA VHAIGSRCPN ISRIYSIGKS VNGVALWVIE ISDKPGQKEA EPAFKYVGNV
HGDEPVGREV LIKLANWLCD NYLKDPLATL IVKNMHLHIL PTMNPDGFAL RRRGNANNVD
LNRDFPDQFF PNNDEINYRQ PETRAIMNWV KQEHFTASAS LHGGALVANY PWDGSRDQSK
QYYGCPDDKT FRYMASVYSQ SHYNMSLSKE FKGGITNGAF WYPIYGGMQD WNYIHGGCFE
LTLEISDVKW PKAAELPVIW EHNRMSMLNL AASLVKTGVH GRIFAADTGH PIPGSLTIKG
IGSEIRASRT YGDYHRMLAP GENYKVIASM EGFRTKATRI VVEEKAVSLD FILDRDGANG
LIRNDLGCPC DDDKLFHVQG ARLELYLFVL LIIIALYVLF KRKTTSKFTI HRHSPKRPIA
V
//
