ID A0A1R3HYR0_9ROSI Unreviewed; 1403 AA.
AC A0A1R3HYR0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COLO4_26110 {ECO:0000313|EMBL:OMO75492.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO75492.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO75492.1}.
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DR EMBL; AWUE01019205; OMO75492.1; -; Genomic_DNA.
DR STRING; 93759.A0A1R3HYR0; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
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; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
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:SF769; CO(2)-RESPONSE SECRETED PROTEASE; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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; 2.
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:UP000187203};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1403
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013340148"
FT DOMAIN 33..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 140..603
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 662..727
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT DOMAIN 737..774
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 805..1223
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1283..1402
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 544
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 813
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 875
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1403 AA; 149614 MW; B1095584F375C9E0 CRC64;
MKSLITFVLV LSCFFSVSLL TETGAAAAEK NGVYIVYMGA APSKKGALRD DHAQLVSSLL
KRNKNALVQS YKHGFSGFAA VLSETEAKSL AKKPGVVSVF PDPVLELHTT RSWDFLKLQT
SVVITSNPNS DSDANSTSDS GAIIGILDTG IWPESDSFND KAMGPIPSRW NGTCTQASDF
NTSNCNKKII GARAYDADDH SPIKFHSARD MVGHGTHVAS TAAGSEVQGV SYYGLAAGTA
KGGSPGSRIA MYRVCSPHNG CRGSSILAAF DDAIADGVDV LSLSLGAPSF LKPAINADPI
ALGAFHAVEH GITVVCSAGN DGPDRGTVVN AAPWILTVAA STIDRDFEST IVLGDNTEVK
GEGINFADIK KTPIYPIIYA KSAKKSGEDE TSARNCDLDS MDQEIVKGKI VVCDNDNQLY
ALSEKKDEVK KLGGIGIILI DDDSRTVAST FGSFPATVIS KKDAPKLFSY INSTKNPVAT
ILATTTPTNY KPAPSIAYFS SRGPSTPDIA APGVNILAAW MGNDTVEAPE GKDPPLYNVI
SGTSMACPHV SGIAATVKGK NPTWSPAAIR SAIITTATQT NNMKTLITNE KGEAATPYDF
GAGEVSTTGP LQPGLVYETT TIDYLNFLCY HGYNVTTIKT ISRTIPDGFT CPKESSIDLI
SNINYPSIAI TNFNEKTGRK VNRTLTNVAG EGKTVYTVTI DAPKGLEVQV VPDKLQFTNN
GDKSSYQDQQ VLDPVLYKHG FSGFAAVLSA AEAHSLAEQP GVVSLFPDPV LKLHTTRSWD
FLKFQSSVLI GSYPNSDSNS TSHDSDVIIG IIDSGIWPES ESFNDKAMGP IPSRWKGACE
QSKDFNTSHC NKKIIGARSY EVDDLPRTPR DMEGHGTHVA SIAAGIEVPG VSYYGMAAGT
AKGGSPGSRI ATYRVCSLHY GCPGSSILAA FDDAIADGVD VLSVSLGGPS FEEPDFVKDP
IALGAFHAVE RGITVVCSGG NDGPARGSVV NVAPWILTVA ASTIDRHFES KLVLGDNKEI
KGEGINIADI QKSPVYPIIL AKSAKRRGST DIETSNCDPD TMDPKLVKGK IVLCDNLDSD
YVESERTAEV KKLGGIGIVL IDDALIKVAP NFGTFPGTVI SSKDADKPDI AAPGVNILAA
WIGNDTVSAP EGKNPPKYNV ISGTSMACPH VSGIAAIVKS KNPTWSPSAI RSAIMTTATQ
TNNLRAPITF ANDEAATPHE FGAGEVSLTG PLQPGLIYES TTIDYLNFLC YYGYNISTIK
LIAKTLPDRF TCPKESNIHL IPNINYPSIA ITQFNEKEGE KITRWEVTRT LTNVAGEDKS
IYNVSIDVYS DLYVQVVLDK LQFTRNSDLD VQVVPDKLQF TRNGQKLSYQ VSFSSAKLLQ
NDVFGSITWS NGKYKVRIPF HVH
//
