ID A0A0E0L7Q0_ORYPU Unreviewed; 440 AA.
AC A0A0E0L7Q0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G02700.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC06G02700.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC06G02700.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR AlphaFoldDB; A0A0E0L7Q0; -.
DR EnsemblPlants; OPUNC06G02700.2; OPUNC06G02700.2; OPUNC06G02700.
DR Gramene; OPUNC06G02700.2; OPUNC06G02700.2; OPUNC06G02700.
DR Proteomes; UP000026962; Chromosome 6.
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 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:UP000026962};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..440
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002366333"
FT TRANSMEM 402..419
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 440 AA; 49387 MW; B0E5F8B5E4035DAD CRC64;
MAISRRRLLS LFLLCAFSSL PAQAAARGGS HPSGTGGNYG SFLRNLLQDN PMVTEELIHG
YMSNSELEIA VHAIGSRCPN ISRIYSIGKS VNGVTLWVIE ISDKPGQKEA EPAFKYVGNV
HGDEPVGREV LIKLANWLCD NYLKDPLATL IVENMHLHIL PTMNPDGFAL RRRGNANNVD
LNRDFPDQFF PINDEINYRQ PETRAIMNWV KQEHFTASAS LHGGALVANY PWDGSRDQRY
PIYGGMQDWN YIHGGCFELT LEVSDVKWPK SAELPVIWEH NRMSMLNLAA SLVKTGVHGR
IFAADTGHPI PGSLTIKGID SEIRASRTYG DYHRMLAPGE NYEVMASMEG FRTKATRIVV
DEKAVSLDFI LDRDGANGQV IRNDLDYPCD HDKLFHVQGA RLELYLFVLL IIIALYVLFK
RKTTSKFTTH RHSPKRPIAV
//
