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Database: UniProt
Entry: A0A151RCR7_CAJCA
LinkDB: A0A151RCR7_CAJCA
Original site: A0A151RCR7_CAJCA 
ID   A0A151RCR7_CAJCA        Unreviewed;      1399 AA.
AC   A0A151RCR7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cucumisin {ECO:0000313|EMBL:KYP40420.1};
DE            EC=3.4.21.62 {ECO:0000313|EMBL:KYP40420.1};
GN   ORFNames=KK1_038228 {ECO:0000313|EMBL:KYP40420.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP40420.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP40420.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KQ483836; KYP40420.1; -; Genomic_DNA.
DR   STRING; 3821.A0A151RCR7; -.
DR   OMA; PFGTIHK; -.
DR   Proteomes; UP000075243; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 2.
DR   CDD; cd04852; Peptidases_S8_3; 2.
DR   Gene3D; 2.60.40.2310; -; 2.
DR   Gene3D; 3.50.30.30; -; 2.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF791; SUBTILISIN-LIKE SERINE ENDOPEPTIDASE FAMILY PROTEIN; 1.
DR   Pfam; PF17766; fn3_6; 2.
DR   Pfam; PF05922; Inhibitor_I9; 2.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 2.
DR   PROSITE; PS51892; SUBTILASE; 2.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 2.
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:UP000075243};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          6..50
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          71..513
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          570..665
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   DOMAIN          692..770
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          791..1242
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          1298..1393
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        462
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        799
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        860
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        1191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KYP40420.1"
SQ   SEQUENCE   1399 AA;  150883 MW;  1BFC929EBE3BE521 CRC64;
     SDIEPAEAIL HSYKKSFNGF VVKLTEDEAE RMAEMEDVVS VFPNKKNRLH TTKSWDFIGV
     SPQVKRSNIE SDIIVGVIDS GVWPESKSFS DQGFGPPPKK WKGSCHNFTC NNKIIGAKYI
     NIEGYYSKSD IISPIDTGGH GTHTASMVAG NWVNSASVLG FGSGTARGGV PSARIAVYKA
     IGCGSEADTL AAFDEAIADG VDIISLSLGP FEPKHYFEDA IDIGSFHAMK RGILTSHAAG
     NDGPRPSTIT NYSPWLLSVA ATTIDRKFML GTAAKPLSGT SINTFDLKNK MFPLIFSGNA
     PNTADGYNSS ISRLCLDNSL DKHLVKGKIV LCDGFDSSKV GGLSGAVGML VGSPISKDSP
     FTLALPAALL SQRNILSVFS YMTSTSNSTA TIFRSVEVND TAAPYVASFS ARGPNPFTPN
     TLKPDLAAPG VNILAAWTPL NPISHFKGDK RPAHYNLAFG TSMACPHASA AAAYVKSFHP
     NWSPAMIKSA LMTTATPMSP TPNPDVEFAY GAGQINPVKA ANPGLVYDIS EADYVKFLCG
     EGLTNEQLRK ITRDHSSCSK HSKKEAVYEF NLPSFALHVN VSEYFSHVFN RTVTNVGLAT
     SSYKAKVVSP SLLDIQVEPN VLSFTSIGQK KKFSVIIEGS INVEILSASI VWDDGTFQVR
     TTIVVQILVA SRVKYYSSTT SYKHADKLKR MTYIVYMGDH PKGMDSTSIP SLHTAMAQKV
     LGSDFKPEAL LHSYKNFNAF VMKLTEEEAE RTAEMENVIS VFPNSKKSLH TTRSWNFIDF
     PQNVKRETRE SDIIVGVLDS GIWPESESFS GKGFGPPPSR WKGSCHNFTC NNKIIGAKYF
     NLEHEFAKED IISPRDAEGH GSHCASTVAG NSVNSVSLFG LASGAARGGV PSARIAVYKV
     CWKEHCHDDD ILAAFDEAIS DGVDIISISI GPRIVHYFPY FQDPTHIGSF HAMKRGILTS
     NSGGNEGPSF SSMSNLAPWL LSVAASSFDR KIVTKVQLGN GAVYEGVSIN TFNLKKKLYP
     LIYGGDIPNI AGGHNSSTSR YCIRNSLDKD SVKGKIVLCE ITHGTDIDSL SGIGAVGVIL
     GSNSPQDSAS AFVLPAAILS PWNQRLIHSY ITSTRNATAT IFKSEEINDG LIPFVASFSS
     RGPNPITPNT LKPDIAAPGV EVIAAWSPVS PISDVKGDKR KVQYNVISGT SMACPHASAA
     AAYIKSFHPN WSPAMIKSAL MTTATPMSHV LNPEAEFAYG AGLINPVKAA NPGLVYDISE
     ADYIKFLCGE GYTDEMLRNL TKDHSSCKVQ ASKRAVYELN LPSFALFTNH STFSRAYFRT
     VTNVGSATAT YKARVIASPL LQIQVKPSTL SFTSIGQKKS FSLIIEGITN LDIISASLIW
     DDGSHQVRSP IVVYGRMGM
//
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