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Database: UniProt
Entry: A0A0C3JKW4_PISTI
LinkDB: A0A0C3JKW4_PISTI
Original site: A0A0C3JKW4_PISTI 
ID   A0A0C3JKW4_PISTI        Unreviewed;       525 AA.
AC   A0A0C3JKW4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 24.
DE   RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE            EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN   ORFNames=M404DRAFT_131410 {ECO:0000313|EMBL:KIO09768.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO09768.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO09768.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO09768.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR   EMBL; KN831954; KIO09768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3JKW4; -.
DR   STRING; 870435.A0A0C3JKW4; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; A0A0C3JKW4; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000054217; Unassembled WGS sequence.
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; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF452; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW   Signal {ECO:0000256|RuleBase:RU361156}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT   CHAIN           20..525
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361156"
FT                   /id="PRO_5005111115"
SQ   SEQUENCE   525 AA;  57903 MW;  F70645A6B9066A56 CRC64;
     MKALKLTCFV YLSTVLASAL PESQVVLNDL SNLELPADPA VANFEHTTSG GIHGKQFVQE
     EGIIYELVRH QYFAQHQLRV TEPSLCDPSV KQYSGYLDVT DDKHLFFWFF ESRNTPESAP
     LLLWLNGGPG CSSSTGLFFE LGPCSVSDDG LNTTYNPYSW NTHANIIFLD QPVGVGFSYA
     EDGSKVDTSE RAAKDVYAFL ELFLTRFPEY SKQPFHIAAE SYGGIYAPNI ASVIHEENQK
     LPFTSTGLVK INLESVVIGN GLTDSYTQFA SVPEYLCEGP YPIFDDPSGP ECTSLRSKVP
     TCQRLIKACH TFKSRFVCVP AELYCNAQLY GPVQSSGLNP YDARRVCDPE EDGPLCYKQL
     TWIEKYMNTP EVKAAIGVAP QLEFKACNMG VNQGFLLQGD SVRDTPALLP ELVNNGIRLL
     VYAGVADMMC NFIGEERWLE VLGTDFLDEF LDAPTEQWIT SSSKTAVGTV RSAGGGSSRA
     GNITFVAVHD AGHMVPYDQP EAALDLITRW IFDLPLTTDF SASFL
//
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