ID A0A443P7A6_9MAGN Unreviewed; 447 AA.
AC A0A443P7A6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:RWR86641.1};
GN ORFNames=CKAN_01555000 {ECO:0000313|EMBL:RWR86641.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR86641.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR86641.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR86641.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR86641.1}.
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DR EMBL; QPKB01000006; RWR86641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443P7A6; -.
DR STRING; 337451.A0A443P7A6; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07331; M48C_Oma1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 263..421
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 447 AA; 50096 MW; 6EB42F626C30265E CRC64;
MGFFNKAKLV INAFPFLSSK ILTGNGHHRG IATASNAIRP AQTIFNKKFT CGFHYSSLYS
SLKPSSIKSK LNYATAGTRR FYYVDRYQVK HFRRRGPQRW FQNPRTVFVV VVVSSGVLIT
VYYGNLETIP YTQRKHFVLM SREMERKIGE AQFQLLKASS KGKILPPIHP DGIRVKSIAS
DIINALQRGI GHERVWSDIS YSNEEPALPS SSSRGSPNIV SALRGEELKV DEQWPREDEI
LDDEWVQESR KAGKARGSQP ATQHLEGLNW EVIVLDEPVV NAFCLPGGKI VVFTGLLNHF
RTDAELAAII SHEVGHAIAR HSAEIFTKNM WLGILQLVLL QLIYMPDVVH AMSQLLLKLP
FSRRMEIEAD HIGILLMAAA GYDPRVAPKM FEKLGQITGS DSSLQDYLST HPSGKTRAKL
LAQSKVMEEA LAIYSERLLG HGVEGFL
//
