ID A0A1S2XGM4_CICAR Unreviewed; 774 AA.
AC A0A1S2XGM4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Subtilisin-like protease SBT1.8 {ECO:0000313|RefSeq:XP_004488082.1};
GN Name=LOC101515370 {ECO:0000313|RefSeq:XP_004488082.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004488082.1};
RN [1] {ECO:0000313|RefSeq:XP_004488082.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004488082.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM
CC symbiosis with AM fungi (e.g. Glomeromycota intraradices).
CC {ECO:0000256|ARBA:ARBA00002076}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR RefSeq; XP_004488082.1; XM_004488025.3.
DR AlphaFoldDB; A0A1S2XGM4; -.
DR PaxDb; 3827-XP_004488082-1; -.
DR GeneID; 101515370; -.
DR KEGG; cam:101515370; -.
DR eggNOG; ENOG502QRTY; Eukaryota.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000087171; Chromosome Ca1.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
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; 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:SF335; SUBTILISIN-LIKE PROTEASE SBT1.8; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523};
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:UP000087171};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..774
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010171490"
FT DOMAIN 26..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..592
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 395..470
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 670..768
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 208..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 555
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 774 AA; 82935 MW; 6BBBA3B7AF3712B8 CRC64;
MGSVSTFFFI LLPLFLSSSI NASKKTYIVH MKDHNKPSVY QTHHDWYTAS LQSLSINTDS
ESSDSDSDSD FDPLLYSYTT AYNGFAVTLN DEQVQSLTRS DSVLGVYEDT VYQLHTTRTP
QFLGLETETG LWEGHRTQEL DQASHDVIVG VLDTGVWPES LSFNDAGLPV IPTRWRGACE
DTPDFNASLC NRKLIGARSF SKGFHMSNGY GKTSNEEPIS PRDRDGHGTH TASTAAGSHV
ANASFLGYAT GTARGMAPQA RVAAYKVCWT DGCFASDILA GMDRAIQDGV DVLSLSLGGE
SVPYFRDTVA IGAFAAVERG IFVSCSAGNS GPARASIANV APWIMTVGAG TLDRDFPAYV
TLGNKKRLSG VSLYSGKGMG SEPVGLVYFK GSNHSANICM AGSLDPALVR GKVVICDRGI
SARVEKGKVV RDAGGIGMIL ANTAESGEEL VADSHLLPAV AVGNTIGDEI REYGSSDRNP
TAVLSFGGTI LNVRPSPIVA AFSSRGPNMI TKEILKPDVI GPGVNILAGW SDAVGPSGLA
GDNRKTQFNI MSGTSMSCPH ISGLAALLKA AHPNWSPSAI KSALMTTAYT HDNSKSPLRD
AAGKSFSTPW AHGAGHVNPQ KAFSPGLVYD ASTKDYITFL CSLNYNPEQI QLIVKRPDVN
CTNKFANPGQ LNYPSFSIMF SSKRVVRYTR ILTNVGEAGS VYNVVVDGPS WVDITVKPSR
LVFEKVGDRK RYTVTFVSKK GVDTSSVRNG FGSILWSNTQ HQVRSPIAFA WTEL
//
