ID A0A0D3H5Z0_9ORYZ Unreviewed; 1584 AA.
AC A0A0D3H5Z0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-aminoacylpeptide hydrolase {ECO:0000256|ARBA:ARBA00029840};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART09G07440.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART09G07440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART09G07440.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART09G07440.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Microsome
CC membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR STRING; 65489.A0A0D3H5Z0; -.
DR MEROPS; M01.A25; -.
DR PaxDb; 65489-OBART09G07440-1; -.
DR EnsemblPlants; OBART09G07440.1; OBART09G07440.1; OBART09G07440.
DR Gramene; OBART09G07440.1; OBART09G07440.1; OBART09G07440.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_002097_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 9.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 2.
DR Gene3D; 1.25.50.20; -; 2.
DR Gene3D; 2.60.40.1910; -; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 2.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF203; AMINOPEPTIDASE M1-C; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 2.
DR Pfam; PF01433; Peptidase_M1; 2.
DR Pfam; PF17900; Peptidase_M1_N; 2.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 1..96
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 131..347
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 426..684
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 786..908
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 943..1159
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 1240..1558
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 1016
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 1015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 1019
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 1038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 1100
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1584 AA; 179066 MW; 54C542DAB5A5CD77 CRC64;
MDFNGTLNDQ MRGFYRSKYE YKGETKNMAV TQFEAVDARR CFPCWDEPAF KAKFKLTLEV
PSELVALSNM PVTCETIAGP IKTIHYEESP LMSTYLVAIV VGLFDYVEGV TSEGNKVRVY
TQVGKSSQGK FALDIGVKSL NFYKDYFDTP YPLPKLDMVA IPDFAAGAME NYGLVTYREV
SLLFDEQSSS ASFKQNVAIT VAHELAHQWF GNLVTMEWWT HLWLNEGFAT WMSHLSVDSF
FPQWNIWTQF LDSTTSALKL DSQAESHPIE VEIHHASEVD EIFDAISYDK GASVIRMLQS
YLGAEHFQKA LASYIKKYAY SNAKTEDLWA VLEEVSGEPV KDLMTTWTKQ QGYPVISVKL
KGHDLELEQD QFLLNGTSGA GIWIVPITLG CCSHDKQKRL LLKHKHDNIK AIVSQCDSRQ
KGGNFWIKLN IDETGFYRVK YDDELTAALR NALQTKKLSL MDEIGIVDDA HALSIACKQT
LSSLLHLLYA FRDEADYSVL SHINSVTSSV AKISIDATPD LAGDIKQLFI KLLLPPAKKL
GWDPKDGESH LDAMLRPMLL VALVQLGHDK TINEGFRRFQ IFFDDRNTSL LTPDTRKAAY
LSVMHNVSST NRSGYDALLK VYRKSAEGEE KLRVLGTLSS CQDKDIVLES LNLIFTDEVR
NQDAYRVLGG VIIEARETAW SWLKFTSKEK EAEISQFFAT RTKPGYERTL KQSLERVLIN
ARWIEGIRAA EAEAVMAAAA AEFRGQARLP RFAAPRRYEL RLRPDLAACM FSGEASVAVD
GLAPAEVSVF EEDEILVLEF AGELPLGEGV LAMRFNGTLN DQMRGFYRSK YEYKGETKNM
AVTQFESVDA RRCFPCWDEP SFKAKFKLTL EVPSELVALS NMPIVNEKIA GPIKTVEYEE
SPVMSTYLVA IVVGLFDYIE GVTSEGNKVR VYTQVGKSNQ GKFALDVGVK SLNLYKEFFD
TPYPLPKLDM VAIPDFTNGA MENYGLVTYR EIYLLFDEQS SSASTKQNVA ITVAHELAHQ
WFGNLVTMEW WTHLWLNEGF ATWMSYLAVD SFFPEWNIWT QFLDSTTSAL KLDSLAESHP
IEVEIHHASE IDSIFDSISY DKGASVIRML QSYLGAERFQ KALASYIKKY AYSNAKTEDL
WAVLEEVSGE PVKNLMTTWT KKQGYPVIGV KLKGHDVELE QDQFLLDGSS DSGMWIVPIT
LGYNSHDMQK RFLLKHKFSD IKGINSQYDD QDRQNSGNFW IKLNIDETGF YRVKYDDELT
TALRNALQMK KLSLMDKIGI VEDAHALSIA GKQTLSSLLH LLYACRDEDD FSVLSHINSV
TSSVAKISVD ATPELAGEIK QLFIKLLLPT AEKLGWDPKN SESHLDAMLR PVLLVGLVQL
GHDKTISEGV RRFQIFFDDR NTSLLPPDTR KAAYLSVMHN VSSTNRSGYD ALLKIYREST
EVEERLNVLG ILSSCQDKDI VLESLNFIFT DEVRNQDAYL VLRSVIIDAR ETAWSWLKEN
WDRITKTFAA SAILSDYVKS IVTLFTSKEK EAEISQFFAT RTKPGFKRAL KQSLENVRIS
ARWVDGIRGE AELAQTVHDL LIKL
//
