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
//