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Database: UniProt
Entry: X0IPU7_FUSOX
LinkDB: X0IPU7_FUSOX
Original site: X0IPU7_FUSOX 
ID   X0IPU7_FUSOX            Unreviewed;       539 AA.
AC   X0IPU7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=FOPG_02325 {ECO:0000313|EMBL:EXL86171.1};
OS   Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL86171.1};
RN   [1] {ECO:0000313|EMBL:EXL86171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL86171.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW808.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXL86171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL86171.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum PHW808.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC       peptides. Digests preferentially peptides containing an aliphatic or
CC       hydrophobic residue in P1' position, as well as methionine, leucine or
CC       phenylalanine in P1 position of ester substrate.
CC       {ECO:0000256|ARBA:ARBA00025622}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; JH658807; EXL86171.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0IPU7; -.
DR   MEROPS; S10.001; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   Proteomes; UP000030676; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; 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; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW   Signal {ECO:0000256|RuleBase:RU361156};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           19..539
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5006531768"
FT   DOMAIN          1..100
FT                   /note="Propeptide carboxypeptidase Y"
FT                   /evidence="ECO:0000259|Pfam:PF05388"
SQ   SEQUENCE   539 AA;  60154 MW;  E516B9CD0FF52097 CRC64;
     MRLSTSALVL GAASSAVGLQ EQQVLGGDSK PLVDVNAWTK PLEKFFGEIS SEAKAVWDEV
     TLLAPDAVEA FKKQVLTQPK KANRRPDAHW DHIVKGADVQ SLWVEKNGEK HREVGGKLDN
     FNLRAKKVDP SKLGVDKVKQ YSGYLDNEEE DKHLFYWFFE SRNDPKNDPV VLWLNGGPGC
     SSLTGLFLEL GPASINKKIE LVNNPESWNN NASVIFLDQP VNVGYSYSGG SVCNTVAAGK
     DIYALLTLFF HQFPEYAKQD FHIAGESYAG HYIPVFANEI LSHDDRNINL KSVLIGNGLT
     DGYTQYAYYR PMACGEGGYP SVLSDSECQS MDNALPRCQS LIKGCYESGS AWSCVPASIY
     CNNAMMGPYQ RTGQNVYDIR GKCEDSSNLC YPGLGYIADY LNREEVKEAL GVEVSSYDSC
     NMDINRNFLF AGDWMQPYHQ LVPNVLDKIP VLIYAGDADF ICNWLGNQAW TDKLQWSGQK
     DFSHAKIKNL EHDGKEYGKV KSSGNFTFMQ IYGAGHMVPM DQPEASSDFF NRWLSGEWF
//
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