ID A0A1S3DVC3_CICAR Unreviewed; 763 AA.
AC A0A1S3DVC3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Subtilisin-like protease SBT5.3 {ECO:0000313|RefSeq:XP_012567390.1};
GN Name=LOC101512939 {ECO:0000313|RefSeq:XP_012567390.1};
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_012567390.1};
RN [1] {ECO:0000313|RefSeq:XP_012567390.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012567390.1};
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_012567390.1; XM_012711936.2.
DR GeneID; 101512939; -.
DR KEGG; cam:101512939; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000087171; Unplaced.
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; IPR046450; PA_dom_sf.
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:SF768; SUBTILISIN-LIKE PROTEASE; 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; SSF52025; PA domain; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..763
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010229985"
FT DOMAIN 31..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 137..594
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 393..464
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 664..761
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 763 AA; 82550 MW; 1DD7BCF50304834C CRC64;
MKDTMTLSIC HVLISLLFVL LHKPTLAIKQ SYIVYLGSHS XXXXXXATDS HYDFLGSYVG
STEKAKEAIF YSYNRYINGF AAILDEDEAA DVAKHPNVVS IFLNKKYELH TTRSWEFLGL
ERNGGFPNDS LWHKSLGEDI IIGNLDTGVW PESQSFSDEG FGPIPKKWRG FCQVDQNNTD
KFYCNRKLIG ARYFYKGYEA VKGQNASHNS ARDFEGHGSH TLSTAGGNFV NGVNVFGYGN
GTASGGSPKA RVASYKVCWD GCYAADILAG FEAAISDGVD VISMSLGGDP QEYLANGISI
GSFHAVSNNI VVVGSGGNSG PTPSTVSNLE PWMLTTAAST IDRDLASNYV TLGNKKIFKG
ASLSEMNLPP NKMYPLISGA DAKFDNASAA AGLLCTPATI DPQKVNGKIL VCLRGLYDRI
IKGVLASRAG AIGMILANDE ASGGEVIADL HLLPASNVNF TVGNYILNYI NSTKFPVAYI
SKVITRLGVN PTPIMASFSS RGPNSIEPSL LKPDITAPGV NIIAAYSQAV SPTLEAFDKR
RIPYITLSGT SMSCPHVAGL VGLLKSLHPT WSPAAIKSAI MTTATTKDNI GKHMLNSSLI
DEATPFAYGA GHIRPNRAVD PGLVYDLNVT DYLNFLCGHG YTSSKITLFI GRPFECPESF
NLVNFNYPAI TIPYFILGHP LNVTRTLTNV GSPGTYRVLI QAPPECLVSV EPSILRFTKK
GEKREFKVTL TLKSRSNYIN NYIFGKLIWT DGKHRVGTPI AMI
//
