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Database: UniProt
Entry: A0A1V1T2W5_9FUNG
LinkDB: A0A1V1T2W5_9FUNG
Original site: A0A1V1T2W5_9FUNG 
ID   A0A1V1T2W5_9FUNG        Unreviewed;       722 AA.
AC   A0A1V1T2W5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAW15114.1};
GN   ORFNames=ANO14919_045230 {ECO:0000313|EMBL:GAW15114.1};
OS   fungal sp. No.14919.
OC   Eukaryota; Fungi.
OX   NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW15114.1, ECO:0000313|Proteomes:UP000189293};
RN   [1] {ECO:0000313|EMBL:GAW15114.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW15114.1,
RC   ECO:0000313|Proteomes:UP000189293};
RG   Technology Reseach Association of Highly Efficient Gene Design;
RA   Itoh H., Matsui M., Shibata T.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW15114.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW15114.1,
RC   ECO:0000313|Proteomes:UP000189293};
RA   Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
RT   "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
RT   Inhibitor FR901512.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:GAW15114.1}.
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DR   EMBL; BDMC01000011; GAW15114.1; -; Genomic_DNA.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000189293; 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:UP000189293};
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:UP000189293};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    722       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012188952.
FT   DOMAIN      284    721       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   REGION      200    259       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V1T2W5}.
FT   COMPBIAS    211    238       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V1T2W5}.
FT   COMPBIAS    239    253       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V1T2W5}.
FT   ACT_SITE    361    361       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    365    365       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    639    639       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       680    680       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       681    681       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       699    699       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       701    701       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   722 AA;  79616 MW;  98A2D710BE072473 CRC64;
     MRITQFLLVI GLAAHEIAAN PLYRHAPQSI SPQPSKRVIP HTHIRHEKRT TGQGGSWAKV
     ERAKREALLP MRIGLKQTKL MDGHHLLMDI SNPESENYGK HLSAEEVVDF FAPLESSVQA
     VRTWLAEAGI EAHTISQSAN KQWVQFDAPV DKVEGLLMTN YHVWEHKMTG AKDIGCDEYH
     VPRHIRPHID YITPGIKLMG NGGAQQKRTS TRDAGSDKKL PRLSQPLDSR DIERVMNKRS
     SVRPSSSNQA TGAKFHGPLR FAEPVRPEDI LSGNLTLEQG CDTYVTPDCI RQMYGIPKGT
     TNHAGNKMGI FQSLKQHYTQ QDLDTFFWAF TDDIPNGTYP ELLSVNGGEG ATADLYDAGT
     EANLDFQMAY GLIWPQEPAL FQVDDEWYQQ SQLRSGEYAG FFNNLWNAID GSYCQFEAFG
     ETGNCKRPEC RDPEYPNAHE GGYKGELNCG VYKPTNVISI SYSGAESELP ASYQQRQCAE
     IMKLGLQGST IMIASGDSGV AGFATYANPT GCMGPEHDVF NPQFLATCPY ILAVGSTYLP
     TNRTAGKDAE EATSRFRSGG GFSNIYDAPE WQRDTVERYL SRANVSFEGY EGGGTNYSNA
     REGLGRFNRI GRAYPDVSAN GDRFVISSGG DLLRIGGTSA SCPLWGSIIT LINEARLEAG
     KKPVGFIHPV LYAHPEVFND ITVGDNRGCR TPGFPATEGW DPVTGMGTPN YPKLLELFTS
     LP
//
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