ID A0A166YE02_9HYPO Unreviewed; 855 AA.
AC A0A166YE02;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=BBO_08080 {ECO:0000313|EMBL:OAA36801.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA36801.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA36801.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA36801.1,
RC ECO:0000313|Proteomes:UP000076863};
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 -!- FUNCTION: Extracellular serine carboxypeptidase that contributes to
CC pathogenicity. {ECO:0000256|ARBA:ARBA00037356}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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:OAA36801.1}.
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DR EMBL; AZHA01000034; OAA36801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YE02; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF189; CARBOXYPEPTIDASE; 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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 96299 MW; 46CD5573C260ACFD CRC64;
MFWVSGKPGC GKSTLMKHVY HEKRLKDSLM EWADGKRLVL AGCFFYEQGT AIQKSREGML
RTILHQIFST QRDLIPVVFS DFFGDDALPL TPWTWTQLRE ALELTLNNLG DSRICIFADG
LDEYRMLDRI NEYKKGDFTL QFGPSNSDDR WGLSKWIRQL MHILAMDAQV GVYIRGVRHD
EYDMKTFFLF FEARHLNGGP GSSSMMGFCS RRMEWLPSDG KPAHKPTYPH HGSTRMRGEM
RRERRNNNLT MFAKALLLSS IAGLAAAQFP PPVTGVKTLK SKFHENPGLC ETTPGVKSYA
GHVHLPASLL EDIHGVRHEY DTNTFFWFFE ARHDPENAPL AIWLNGGPGS SSMMGLLQEN
GPCLINEDSE TTRHNPWSWN NHVNMLYIDE PNQVGFSYDT PTNFTIVLDS EGDEVRTATD
FSRVDVPELN STARVGTLSS DDKRHTVNTT AEAAHALWHF AQAFFWEFPH YKPNDDRISL
WAESYGGHYG PGFTRFFQQQ NEKILNGTLD DKTAHYMHLD TLGIINGVID ATHREEAGII
FPFNNTYGIQ AYTQEFYDEL IHNFTKPGGC RDQILHCQDV LEDRDRITIQ DERDGGWKAI
CGISEECASP SEKAFRTVDH GRFDITHHKQ DPFPPPHLYG YLSRGEVLEA LGVPVNFTAT
SSAVSGNFGD SADHLKGGFI DAIGYLLDTG VKVHLMYGDR DFACNWIGGE MSSLAVAHAQ
AAGFAAAGYA PMISADGVVV GGLTRQHGNF SFTRVFQAGH MIPAYQPVHA YEIFMRATFN
KDIATGRRDV TDELATEGPG NNWHHRTKPY PAPEPRCYVL EPGTCTEEQW AKVYAGALVK
DYYLVEDNGF ESIEL
//
