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Database: UniProt
Entry: A0A2H3IKR2_9EURO
LinkDB: A0A2H3IKR2_9EURO
Original site: A0A2H3IKR2_9EURO 
ID   A0A2H3IKR2_9EURO        Unreviewed;       594 AA.
AC   A0A2H3IKR2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   10-APR-2019, entry version 4.
DE   SubName: Full=Peptidase S8/S53, subtilisin/kexin/sedolisin {ECO:0000313|EMBL:PCG95881.1};
GN   ORFNames=PENO1_071170 {ECO:0000313|EMBL:PCG95881.1};
OS   Penicillium sp. 'occitanis'.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG95881.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG95881.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG95881.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PCG95881.1}.
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DR   EMBL; NPFK01000229; PCG95881.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000218381};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   DOMAIN      200    589       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    275    275       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    279    279       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    490    490       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       532    532       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       533    533       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       567    567       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       569    569       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   594 AA;  64119 MW;  98205332073FB661 CRC64;
     MYTSNMGSCT AQQYKRDPRS VLIVPLVIRK IVEIDTSDIA IPNLLVNNSH GFEQALLAMS
     TPGDPDYGKH FTSYDQMKEM LLPSTAAVSA IREWLTSSGV TDFQEDADWV TIRTSVKIAN
     SLLNANFTWY THDQQSNRAL RTLEYSVPDD ITPYIRMVHP TTIFSQVHAN KAAFRSMSSK
     FGASLAPAAG NTSADTCDSA IIPSCIQKLY HLQNYTADPA RGSKVAFVSF TEQVARYDDL
     AVFESHLAPY AVGQNFTAVE FNGGKNDQHG NTTGEANLDL QYIVGLAAPL PVTEYIVGGR
     GELIPDLTEP DQDHNSNEPF LDFLLEILKV DQEDLPQVIS ISYGDDEQTI PTDYALTVCN
     LFAQLGSRGV SVLLAAGDSG VGSACQTNDA EKRNHFPPQF PSTCPWVTSV GGTNGSHPEK
     AVYFSSGGFS DLFPRPSYQD DAINAYFEIL GDRQAEYFDR LGRGFPDVAA QSVSYVIVDE
     GSAVTTDGTS AAAPAFSAII ALLNDARLEA GLPVMGFLNP WLYGVGRLGL NDIVYGGSTG
     CDGKDRFGGP PNGSPVIPYA SWNATQGWDP VTGLGTPDFA KLKELALGQV CVGQ
//
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