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Database: UniProt
Entry: A0A0D3HGI8_9ORYZ
LinkDB: A0A0D3HGI8_9ORYZ
Original site: A0A0D3HGI8_9ORYZ 
ID   A0A0D3HGI8_9ORYZ        Unreviewed;       958 AA.
AC   A0A0D3HGI8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
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:OBART10G18270.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART10G18270.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART10G18270.1};
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:OBART10G18270.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC       Note=Can bind about 5 Ca(2+) ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR621190-2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-
CC       2};
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DR   AlphaFoldDB; A0A0D3HGI8; -.
DR   STRING; 65489.A0A0D3HGI8; -.
DR   MEROPS; M10.A01; -.
DR   PaxDb; 65489-OBART10G18270-1; -.
DR   EnsemblPlants; OBART10G18270.1; OBART10G18270.1; OBART10G18270.
DR   Gramene; OBART10G18270.1; OBART10G18270.1; OBART10G18270.
DR   eggNOG; KOG1565; Eukaryota.
DR   HOGENOM; CLU_321706_0_0_1; -.
DR   Proteomes; UP000026960; Chromosome 10.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 4.
DR   InterPro; IPR033739; M10A_MMP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF249; METALLOENDOPROTEINASE 1-MMP; 1.
DR   Pfam; PF00413; Peptidase_M10; 4.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00235; ZnMc; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 4.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR621190-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR621190-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR621190-2}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..958
FT                   /note="Peptidase metallopeptidase domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002264115"
FT   DOMAIN          53..179
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   DOMAIN          240..419
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   DOMAIN          607..784
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   REGION          206..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT   BINDING         298
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         326
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
SQ   SEQUENCE   958 AA;  105726 MW;  6ADA03E32D45DC2F CRC64;
     MFPRRRGDAA CLLLLAIACI LSCVAVAGAR PMPPPPTLRH HGGVVSRYAF WTGKPRWTRH
     GRPMVLTYAV SHTDAVGYLP GDAVLAVFRS AFARWAEVIP SSRDGALLAH SLPAKDGDRD
     TAAAAVDLET VATHEIGHAL GLDHSTSESS VMYPYVGTRE RKVRLTVDDV EGIQELYGVN
     PSFSFLDYFT PDHDTPRSHV ARLTATQPAL AQTTMTTTLQ PRPEDNNNDS GAGPFTFFPG
     KPRWTRPDRV LTYAVSPTAT ADHLSPSAVR AALRSAFARW ADVIPMRFLE AERYDAADIK
     VGFYLYTDGR CDGCACIDSD DDDDDGDDCE GVLAHSSMPE KSGQIHLHAA HRWTVNLAAD
     TAPLAVDLES VAAHEIGHVL GLDHSSSRSS MMYPFISCRE RKVRLTTDDV HGIQELYGAN
     PHFSFGAYFK QDILSRIQQM KKEKKKKARG SSFWQRGLAL TCALVNKDSM IGYISELYSS
     IKELDMMNKI NYVYFLDYVG NRTVEKKDPN MHQLRESIRI LTVEIKRWMR FAQIHWVELM
     PTLEDLNPCI ARYVTTINTL VLQLTGGTYT YTMFLLCGCG TGSQPTRLRS QDNNGGGGAA
     AFTFLRGRPR WNRPDMRLTY AVSPLATADH LPRDAVREAF RSALARWAEV TPLRFAEAAR
     YEEADIRVGL YLHASGAGGD GCDGCGHIDD KSSRDGALLA HSLPAKDGRI HMHAARRWTV
     DLDRDTAAAA VDLESVATHE IGHVLGLGHS SSKSSVMYRY VRYRERKVDL TEDDVHGVQE
     LYGANPHFSF NHIDQNKLAP TTTTTPPLQP RPEDSNDNDN GGAVATSLFT FLPGKPRWTR
     PFLTYAVSPA TAVTVGNHVP LNAVRAVFRR AFARWAGVIP VRFVEALRDD DTADIMIGFY
     LHTADGKCDA CGCVCKGGGE EALAHAHPRW TVNLAADTAP LAVDLESVAV HTRRRRAR
//
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