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Database: UniProt
Entry: A0A168JJW8_CORDF
LinkDB: A0A168JJW8_CORDF
Original site: A0A168JJW8_CORDF 
ID   A0A168JJW8_CORDF        Unreviewed;       581 AA.
AC   A0A168JJW8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Peptidase S10, serine carboxypeptidase {ECO:0000313|EMBL:OAA80541.1};
GN   ORFNames=LEL_00086 {ECO:0000313|EMBL:OAA80541.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA80541.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA80541.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA80541.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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:OAA80541.1}.
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DR   EMBL; AZHF01000001; OAA80541.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168JJW8; -.
DR   STRING; 1081108.A0A168JJW8; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   PANTHER; PTHR11802:SF64; CARBOXYPEPTIDASE 2-RELATED; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:OAA80541.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..581
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007898151"
FT   REGION          540..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  63848 MW;  CC0FBF8E428061CF CRC64;
     MVAIHRLSSL LVGLGTAVAQ FVPAPKGLTN VTGYADVAVR YKQVPTGICE LNPDVKSFSG
     YADVAEDQHS FFWFFEAREV DPREAPLTIW INGGPGSSSM IGLFEELGPC RVDNVGKVYD
     NPHSWSRASN LLFVDQPTQV GFSYSVPVPG MVNDDTGEII VLPNNTCPGN SNGTCGTYSL
     PYANLTANST VNAAPNMWRT LQGFMGAFPQ YARQGVHFAT ESYGGHYGPI FNDYFVKQNE
     KNITGAASID LRSVLIGNGW VHPITHYQAF YNFTVSPGNT YDFSPYNKTI QDKLFDNLYG
     PGKCIDGLEE CARNGDDKQC RTADGFCADN VETFLGRYAN RDEYDIRELN PDTFPYGFYR
     DYLNRADVLD AIGAFTNFTG FSAAVGAAFT STGDDGRGVG AIEALQDLVR HDVNVALYAG
     DADYNCNWLG FQKVAEMVDV PGWSRAGFAN LSTSDGKVHA QVKQSRKFSF TRFYESGHEV
     PFYQPLASLE FFERVVNGRD IATGKVNVTS KCFYRSKGTA ESTFREGNAT VQWEVTPQNL
     TYDTDTNGPG APWPKSGGGN ASPARRGKFA RNFKQAILRR Q
//
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