ID A0A068UNL8_COFCA Unreviewed; 754 AA.
AC A0A068UNL8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDP09844.1};
GN ORFNames=GSCOC_T00030318001 {ECO:0000313|EMBL:CDP09844.1};
OS Coffea canephora (Robusta coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP09844.1, ECO:0000313|Proteomes:UP000295252};
RN [1] {ECO:0000313|Proteomes:UP000295252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; HG739125; CDP09844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068UNL8; -.
DR STRING; 49390.A0A068UNL8; -.
DR EnsemblPlants; CDP09844; CDP09844; GSCOC_T00030318001.
DR Gramene; CDP09844; CDP09844; GSCOC_T00030318001.
DR InParanoid; A0A068UNL8; -.
DR OMA; VQGAFRW; -.
DR PhylomeDB; A0A068UNL8; -.
DR Proteomes; UP000295252; Chromosome 8.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795:SF463; OS12G0427600 PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000295252};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..754
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001654950"
FT DOMAIN 43..123
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 147..585
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 373..460
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 655..751
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 754 AA; 81460 MW; 8C6836D3F59E9987 CRC64;
MAGMFVFPIA FLLFNFSSAF SDETKPVPVQ TQPARDPLKN LTTYIVHLRL PAGDNSTQLN
DLESWYQSFL PKNTTGLNDA SRMVHSFRHV FTGFAAKLSP EEVKEMEKKE GFLDARPEKT
LNLQTTHSPK FLGLYTNSQF QWQYGRGEGV IIGIIDSGIT PGHPSFSDEG MQPPPPSWKG
KCEFVGTGCN KKLIGARDLL GPKPGQPLDE IGHGTHTAST AAGNFVEGAN VMRQANGTAA
GMAPRAHLSI YRACYPSGMC TESAIVAAMD FAIQDNVTML SMSLGGPSKL PFFDDPIALG
AFQANKKGIF VSCSASNSGP ENGSLSNEAP WILTVGASTI DRDIRATALL GNGDEFDGQS
IYQPTDFPPN LLPLVYLGMN GDTFAALCTK NSLKKAGVKG KVVLCETSDL MATVEQGQNV
KDAGGAAMII MNQEIEGYTI IADLHVLPAT HVSFAAGQAI KAYINSTCMP RATILFKGTI
LGVKNAPAVA SFSSRGPNNA SPGILKPDII GPGVNILAAW PESVENITNT SSTFNILSGT
SMSCPHLTGI AALLKSAHPN WSPAAIKSAI MTTASFVNRN DGHILNEQMF PADVFATGAG
HVNPPRAIDP GLTYDIQPDD YIPYLCGLGY TDDQIMKIVQ SPVKCSAIHR IQEAELNYPS
FAIQLKSSKQ TYKRVVTNVG EALSTYYVDI DKIQGVEIDV QPRVLNFRKV NQKITYQISF
RRLNMSVGNW YEQGAITWNS EKHRVRSPIS VKFA
//
