ID M3B135_PSEFD Unreviewed; 640 AA.
AC M3B135;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=MYCFIDRAFT_164341 {ECO:0000313|EMBL:EME83103.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME83103.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME83103.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME83103.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB446558; EME83103.1; -; Genomic_DNA.
DR RefSeq; XP_007926422.1; XM_007928231.1.
DR AlphaFoldDB; M3B135; -.
DR MEROPS; S10.016; -.
DR GeneID; 19332165; -.
DR KEGG; pfj:MYCFIDRAFT_164341; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_3_1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000016932; 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 InterPro; IPR029058; AB_hydrolase.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW Signal {ECO:0000256|RuleBase:RU361156};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 17..640
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005140259"
SQ SEQUENCE 640 AA; 71194 MW; 24478DDC3E042CFF CRC64;
MLLSALVLGL FSLVSGQFPP TPEGVTTLQS KFHPGVRVSY KEPGLCETTP GVKSYAGYIH
LPPNALNETH EHNAYPLNIF YWFFESRKDP ENAPLAIWLN GGPGGSSLLG ALSENGPCFV
ANDSKTTYLN PWSWNNEANL LFIDQPVQVG YSYDVPTNIT FNLAGSAEEG GTINPADFTD
GVPEQNNTFL VGTMSSQNVN HTANSTQHAA VAMWHFAQTF FTEFPHLKPK DERISLFTES
YGGHYGPGFM DFFLHQNEKI KKGEISGDGA HYLHLSTLGI INGCIDAPDM MSSNIEMSFN
NTYGVRAISQ DQYEWAMNEF YRTGGVLDDI KKCREMALKT DPHDHGDVAK TNTFCSQAAN
RGENISDSLY VRAGKGARFD ITHEPKDPFP PPFMFGWLNQ PETQKAFGVP VNHSWYSPAV
AAAFESTGDL VKGGQLDQLT YVLEHGVNVA LFHGDRDVAC NWIGGERYSL NIPWAHQAEF
KHAGYTPLVL GSPYTQSGGL VRQYGNLSFT RVYQAGHMVP SYQPEAAYSI FMRALTQRDI
ATGEVDLKEY AATHQAQYST TGPSDTWWMK SDVLPQPPHQ CYILDVSNRC SEEEIEWIKD
GSAIIKDWIV VGRENASDSI DQQRLHYAQP DEQIPLLHDW
//
