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
//