ID A0A1S3C9Y8_CUCME Unreviewed; 461 AA.
AC A0A1S3C9Y8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protease Do-like 8, chloroplastic {ECO:0000313|RefSeq:XP_008459309.1};
GN Name=LOC103498478 {ECO:0000313|RefSeq:XP_008459309.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008459309.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008459309.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR RefSeq; XP_008459309.1; XM_008461087.2.
DR AlphaFoldDB; A0A1S3C9Y8; -.
DR eggNOG; KOG1320; Eukaryota.
DR InParanoid; A0A1S3C9Y8; -.
DR OrthoDB; 313901at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|RefSeq:XP_008459309.1};
KW Protease {ECO:0000313|RefSeq:XP_008459309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT DOMAIN 332..448
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 461 AA; 48718 MW; 3E1D991AA653544C CRC64;
MHVLACNAPQ LRMMGKSGVS TSTHLLGRRE LCFDGVSSVC SSSQPSTSNP STSESIFIQR
RADDDSGDLG SVVSRKFLFT TRRTLFVSLS LSLWPYPSSV FTAQALGDPS VTIDEVTPTI
SPSGSLFPTE ERIAQLFEKN TYSVVNIFDV TLRPQLNVTG MVEIPEGNGS GVVWDDQGHI
VTNYHVIASA LARNPSAGQV VARVNILASD GIQKNFEGKL IGADRTKDLA VLKVDASNDL
LRPIKVGQSS SLKVGQQCLA IGNPFGFDHT LTVGVISGLN RDIFSQTGVT IGGGIQTDAA
INPGNSGGPL LDSKGNLIGI NTAIFTQTGT SAGVGFAIPS STVVKIVPQL IQFGRVVRAG
INVDFAPDLI ANQLNVRDGA LILQVPANSP AAKAGLLPTT RGFAGNIVLG DIIAAIDNKP
VKNKAELYKL LDEYNAGDKI ILKIKRGGQT LELPLILEES Q
//