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Database: UniProt
Entry: A0A1V8ULR9_9PEZI
LinkDB: A0A1V8ULR9_9PEZI
Original site: A0A1V8ULR9_9PEZI 
ID   A0A1V8ULR9_9PEZI        Unreviewed;       659 AA.
AC   A0A1V8ULR9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQO24273.1};
GN   ORFNames=B0A51_07975 {ECO:0000313|EMBL:OQO24273.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Cladosporiaceae;
OC   Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO24273.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
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:OQO24273.1}.
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DR   EMBL; NAEU01000340; OQO24273.1; -; Genomic_DNA.
DR   EnsemblFungi; OQO24273; OQO24273; B0A51_07975.
DR   Proteomes; UP000192386; 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:UP000192386};
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:UP000192386};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    659       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012054101.
FT   DOMAIN      230    658       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   REGION      188    217       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V8ULR9}.
FT   COMPBIAS    188    202       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V8ULR9}.
FT   ACT_SITE    307    307       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    311    311       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    576    576       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       617    617       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       618    618       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       636    636       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       638    638       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   659 AA;  70497 MW;  5BE6340886624CE8 CRC64;
     MLGATLNGLA LLLATAAAVP TPANHVLHER RAESLAWVKV TRVHEDVKLP MRIGLIQSNL
     DKAHDYLMKV SHPESEHYGK HYTVDEVTDL FAPAQSSVDA VRAWLESAGI EMDSVSQSTN
     KQWLQFDASA SKAEELLKTE YHEYEHVATG KTGIACDAYH LPAHVQSHVD YITPGVKHIG
     THGSKAALEK RGGWDNGGKG HRKRPHPPPT RPMPPGQMPS AANLTACGTL VTPECIAAMY
     NITQGNKAAP GNELGIFEDL GDVYAQQDLD NFFTRYYPRI RNGTHPKLEG IDGGIAPIAN
     VSQAGLESDL DFQISYPIIW PQNSILFQTD DPVYENNYTF VGFLNNFLDA IDGSYCSYSA
     FGETGNSPLD PSYPDPQPGG YKGQLQCGVY KPTNVISISY GGQESDAPVN YQRRQCNEYL
     KLGMQGISIC VSSGDSGVAG PPGDDNPDGC LGPGGKIFSP DFPASCPYIT TLGATTLPVG
     ASAAADAEVA VTRFPSGGGF SNIYPIPSYQ AAAVSTYLTK HTPSYPSYAC SLNSSACYTN
     GGIYNRAGRG YPDFSAVGDN VVIGGQGRFL RIGGTSASSP AFAAILTRIN EERIARRKST
     IGFVNPALYA HPEVLHDITV GNNSGCGTPG FYAAPGWDPL TGLGTPNYPA MLKLFLSMP
//
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