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Database: UniProt
Entry: H6C205_EXODN
LinkDB: H6C205_EXODN
Original site: H6C205_EXODN 
ID   H6C205_EXODN            Unreviewed;       607 AA.
AC   H6C205;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Carboxypeptidase D {ECO:0000313|EMBL:EHY57831.1};
GN   ORFNames=HMPREF1120_05855 {ECO:0000313|EMBL:EHY57831.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57831.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY57831.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57831.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., 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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; JH226134; EHY57831.1; -; Genomic_DNA.
DR   RefSeq; XP_009158292.1; XM_009160044.1.
DR   AlphaFoldDB; H6C205; -.
DR   STRING; 858893.H6C205; -.
DR   GeneID; 20310494; -.
DR   VEuPathDB; FungiDB:HMPREF1120_05855; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   InParanoid; H6C205; -.
DR   OMA; HYGPIFN; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000007304; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   PANTHER; PTHR11802:SF64; CARBOXYPEPTIDASE 2-RELATED; 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:EHY57831.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003603002"
FT   REGION          545..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  67546 MW;  60DED32C3A3A5F43 CRC64;
     MAWLLSTTAV LLSCASQFGI SFAQFVTPPK NLTSKQGYAN ITVRYKSVPA GICEQDPDVK
     SFSGYADVAP GQHIFWWFFE ARNVDPTTAP LTIWINGGPG SSSMIGLFQE LGPCRVDENG
     TAVDNPYSWS NVTNMIFIDQ PTQVGHSYST PVPAYIDPNS GLLVELPNNT CPDYASDWDC
     GTYSYFNESL TANSTPNAAP NMWRTLQGFM GAFPQYARHD VFFTTESYGG HYAPLFSEYF
     LQQNSKQIQG AHNISLVGAM IGNGWYDPLI QYQAYYNFTV SPGNTYGYDP LNQSVKDQYY
     TNMYGPGNCY DQTVDCNTRK LDTICSLADT FCAQQVENLY DIYLQRDEYD FRYLTPNPFP
     QSYYVDYLNT EAVQTAIGAY VNYTESSNTV GSAFGATGDD DREIGTVEAV RNLVANRNVS
     VTMYFGDADY NCNWLGGQVV ADHVNASGYA DAGFVNISTS DNVVHGQVRQ SGNFAFVRIY
     ESGHLVPFFQ PLVALEMLDR VIHGKDIATG NTAVTKGYVT KGPKVSSFKE GNATVQFTVT
     PPGSIYNTTT NLPQNGTDQQ SPPAKEKRGK YTKRSMGPYR PRQYRKRMMD MLDQQQRRRP
     GRAVGWE
//
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