ID   A0A0E0NNA2_ORYRU        Unreviewed;       791 AA.
AC   A0A0E0NNA2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI02G39950.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI02G39950.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC         Ala commonly occur as P1 or P1' residues, but more distant residues
CC         are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC         Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00024603};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   AlphaFoldDB; A0A0E0NNA2; -.
DR   STRING; 4529.A0A0E0NNA2; -.
DR   MEROPS; M03.A01; -.
DR   EnsemblPlants; ORUFI02G39950.1; ORUFI02G39950.1; ORUFI02G39950.
DR   Gramene; ORUFI02G39950.1; ORUFI02G39950.1; ORUFI02G39950.
DR   eggNOG; KOG2089; Eukaryota.
DR   HOGENOM; CLU_001805_4_1_1; -.
DR   OMA; QPLEGPW; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 3.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR045666; OpdA_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF83; LD37516P; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF19310; TOP_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          122..244
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          324..784
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   791 AA;  87980 MW;  3A10FADAAED0FD7B CRC64;
     MGPPRVGVGV GVGGGSGIGV AMVFLIVSAS SFLIRLPLVA RARLPNPTSS SYTSRSRSRA
     LLLLPASSPL RAFCPASRRP SPATCSAAYA SSSMATDDNP LLADFDFPPF DRVEPIHVRP
     AVRTLLARLE GELTDLEKGV QPTWGKLVEP LERIVDSLEV VWGTVDHLKA VKDSSDLRAA
     VEDVQPDKVK FQLRLGQSKP IYQAFNAIRN SSDWETLSEA RKRIVEAQIK EAVLSGVALE
     DEQREKFNQI EQELEKLTQK FSENVLDATK KFEKLITDKN EIDGLPATAL GLAAQTAASK
     GHENASAENG PWIITLDAPS YIAVMQHARN RALREEVYRA YLTRASSGDL DNTNIISQIL
     KLRLEKAKLL GYKNYAEVSM AQKMATVDRV EELLEKLRAA SWDHAVKDME DLKAFAKESA
     SPEANDLAHW DLSFWSERLR ESKYDINEED LRPYFALPKV MDGLFSLANR LFGVSVEPAD
     GLAPVWNSDV KFYCVKDSSN SPVAYFYFDP YSRPSEKRGG AWMNVVFSRS RVLARNGSPV
     RLPVAHMVCN QTPPVGDKPS LMTFREVETV FHEFGHALQH MLTKQDEGFV SGIRGVEWDA
     VELPSQFMEN WCYHKNTLLS IAKHYETGEL LPEEIYAKLV AAKNFRAGTF SLRQIRFASV
     DMELHTTYDP NGSLSIYDVD RRVAERTQVL APLPEDKFLC SFSHIFAGGY AAGYYSYKWA
     EVLSADAFSA FEDVGLDNEK AIEETGRRFR ETVLALGGGK SPLEVFVSFR GREPSPEALL
     RHNGLLPVAA L
//