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Database: UniProt
Entry: R9NW27_PSEHS
LinkDB: R9NW27_PSEHS
Original site: R9NW27_PSEHS 
ID   R9NW27_PSEHS            Unreviewed;       589 AA.
AC   R9NW27;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Potential serine carboxypeptidase {ECO:0000313|EMBL:GAC92699.1};
GN   ORFNames=PHSY_000254 {ECO:0000313|EMBL:GAC92699.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC92699.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; DF238767; GAC92699.1; -; Genomic_DNA.
DR   RefSeq; XP_012186286.1; XM_012330896.1.
DR   AlphaFoldDB; R9NW27; -.
DR   STRING; 1305764.R9NW27; -.
DR   GeneID; 24105565; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000014071; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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   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.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:GAC92699.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..589
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004477800"
FT   COILED          87..114
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   589 AA;  65215 MW;  E7897F88DACBDAD0 CRC64;
     MRSSWLSTAS AVFVCAAALA NAAKLPAPLE QIHYDQAGNL VWNEDADISS AVPSLGRPDF
     SALKLDDVVA AAVPVKQAAQ DVLSESMKEA EDVLTWAENE IERIEHKIEE AIAGTKHTVN
     DWIHTGKVFV DGLEFERLTH PSFPEYSLRL NKQSEAFCDK DVVQHSGYLD ISDSKHLWFI
     FFESRSSPKD DPVVLWLNGG PGCSSSTGLL FELGPCRVTD EGHSVKNNPH SWNNKANLLF
     LDQPVDVGYS YSDNDQVNNS PAAAEDVYAF LQLFFTKFPE YSKLPFTASG ESYAGTYLPN
     IASTIYKKNK NLALARYSNP ELAPKHINLD TVMIGNGLSS PQYQFPSVPE YACGADNKYA
     LFEPGSSTCK TLEQQAATCK SLIESCQKYN SRLTCTPAAL YCWSRLYGPA QETGKNLYDV
     RKDCDRERDG PLCYKDMEYI ETLLNTPSIK KNLGVPESVT FQSCNMNINQ AFLLQGDSMH
     DSAALLPELI EDDIRVLIYA GEADFMCNYM GNLEWMQNLQ TSYLDDFNNG TAKEWTVNGK
     KAGLVRKGGK GAGNVAFAQV YAAGHMVPYD QPEVASDMIN RWLANKPLA
//
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