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Database: UniProt
Entry: A0A1V6XIQ3_PENNA
LinkDB: A0A1V6XIQ3_PENNA
Original site: A0A1V6XIQ3_PENNA 
ID   A0A1V6XIQ3_PENNA        Unreviewed;       640 AA.
AC   A0A1V6XIQ3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQE75030.1};
GN   ORFNames=PENNAL_c0074G12014 {ECO:0000313|EMBL:OQE75030.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE75030.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J.,
RA   Nielsen K.F., Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential
RT   of secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(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:OQE75030.1}.
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DR   EMBL; MOOB01000074; OQE75030.1; -; Genomic_DNA.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000191691; 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   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000191691};
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:UP000191691};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    640       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5013252237.
FT   DOMAIN      221    640       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    297    297       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    301    301       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    558    558       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       599    599       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       600    600       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       618    618       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       620    620       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   640 AA;  69696 MW;  C98C0CD7CF1F14D5 CRC64;
     MELFIVLCAL AASAMAVPTA HDYQLHERRD SIPKSWVEGK KLDGNVSLPV RIGLTQSNLD
     YGHELLMDLS NPHSSRYGQY LSIDEVHNLF APTEKSVDDV RSWLESAGIA KDRIVQSANK
     QWIQFDADAE ELENLLHAKY YLYSHAETGR SHVACREYHV PSSVREHVDY ITPGISLREV
     TSVRRSSKQK RFVDGIPPIL EPILLPIEEL LNEAPSLCSQ AITPHCIQQM YNISEGHSAT
     EGNELGIFEG MGDVYAQEDL DLFFSKLYSK IPQGTHPILK SVDGGEAPTD TSRAGPESDL
     DFQISYPIIW PQNSILFQGD DMHYENHYTF RGFLNTFLDA IDGSYCSTIS PLDPPYPDPA
     DGGYKGSLQC GVYDTPKVIS ISYGSAEADL PISYQRRQCA EFMKLGTMGV SVLVASGDSG
     VSGRGGDPTP SNCLGTNGRI FAPDFPATCP YLTAVGGTEI PPGSSPGDHQ EQAVTRFPSG
     GGFSNIYKAP DYQAQAVADY FDKAQPSYPY YESVDNSSFG ENNGIYNRIG RAYPDVAAVG
     DKVVIYNRGM AVSIGGTSAS APVFAAILTR INEERLAAGK STVGFVNPVL YAHPEAFFDV
     TTGSNPGCNT DGFSAAEGWD PVTGLGTPNY PELLRVFMGE
//
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