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Database: UniProt
Entry: A0A2T7EBE1_9POAL
LinkDB: A0A2T7EBE1_9POAL
Original site: A0A2T7EBE1_9POAL 
ID   A0A2T7EBE1_9POAL        Unreviewed;       363 AA.
AC   A0A2T7EBE1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Peptidase metallopeptidase domain-containing protein {ECO:0000259|SMART:SM00235};
GN   ORFNames=GQ55_3G199900 {ECO:0000313|EMBL:PUZ65150.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ65150.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ65150.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. Matrix
CC       metalloproteinases (MMPs) subfamily. {ECO:0000256|ARBA:ARBA00009614}.
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DR   EMBL; CM009751; PUZ65150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7EBE1; -.
DR   STRING; 1504633.A0A2T7EBE1; -.
DR   EnsemblPlants; PUZ65150; PUZ65150; GQ55_3G199900.
DR   Gramene; PUZ65150; PUZ65150; GQ55_3G199900.
DR   Proteomes; UP000244336; Chromosome 3.
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); 1.
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   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF257; PEPTIDASE METALLOPEPTIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
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};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244336};
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..363
FT                   /note="Peptidase metallopeptidase domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015625950"
FT   DOMAIN          152..322
FT                   /note="Peptidase metallopeptidase"
FT                   /evidence="ECO:0000259|SMART:SM00235"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-1"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         251
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         254
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         254
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         277
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         281
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         287
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         295
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   363 AA;  39182 MW;  5CA257E2E4EBCF59 CRC64;
     MLPWRQPAAC LLLVALLVGI LPCRHVANAA LPTPAAAAGL HRHPDGAAPA LRSLKHRQGA
     GRGSRVAGVA ELKRHMGRLG YMRPGAEHDD AFDDHMEAAV KRYQSRLGLP VTSRLDPATL
     GRITSPRCGV SDGRGAVVMS DSAASRFTFF DGEPRWTGPG PIVLTYSVSS AATVSYLPPE
     AVRAAFRSAF ARWAKVIPVE FVEIDEDYSY HEADVRVGCY EGDHGDGSPF DGEKGVVAHA
     YGPEDGRLHL DAAEHWTLDV DSETEGSALD LESVATHEIG HTLGLGHSSS PEAVMYPYIN
     FGERKVELSG DDIEGVQLLY GSNPRFRHEQ HDPSPSVSPG RRNWLGSVSF VCVVLVMLVT
     HVK
//
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