ID   PEPS_ARTBC              Reviewed;         529 AA.
AC   D4AQA7;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable serine carboxypeptidase ARB_06414 {ECO:0000305};
DE            EC=3.4.16.- {ECO:0000250|UniProtKB:P52719};
DE   Flags: Precursor;
GN   ORFNames=ARB_06414;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Removes acidic, neutral and basic amino acids as well as
CC       proline from the C-terminal position. {ECO:0000250|UniProtKB:P52719}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; ABSU01000005; EFE34651.1; -; Genomic_DNA.
DR   RefSeq; XP_003015291.1; XM_003015245.1.
DR   AlphaFoldDB; D4AQA7; -.
DR   SMR; D4AQA7; -.
DR   STRING; 663331.D4AQA7; -.
DR   ESTHER; artbc-d4aqa7; Carboxypeptidase_S10.
DR   MEROPS; S10.014; -.
DR   EnsemblFungi; EFE34651; EFE34651; ARB_06414.
DR   GeneID; 9521015; -.
DR   KEGG; abe:ARB_06414; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_12_3_1; -.
DR   OMA; SELYFWF; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..529
FT                   /note="Probable serine carboxypeptidase ARB_06414"
FT                   /id="PRO_0000434921"
FT   REGION          171..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        503
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   529 AA;  59419 MW;  3291ACB822EF881B CRC64;
     MRGLSYFVLA LSAIDAAAAA SLPFLRSLQH VGRRDPAARN LPNYDFSAIP PVEKRQTASR
     LNGKTKKYAV DGTKIPEVQF DIGESYAGLM PISTRKDESR ELYFWYFPSE NPAAKDEITI
     WLNGGPGCSS LEGLLQENGP FLWQYGTLYP VPNPWSWTKL TNMVWVEQYN PTDDNPSRPV
     GTGFSQGKPS VRSQEDVATQ FLGFFRNFVD TFDLHGKKIY IVGESYAGLY VPYIAHAMFE
     KKNKRYFNVE STMIFDPSIN KDEILTQVPA VPFVEHWKGL FPFNETFTKQ IHDMADKCGY
     SSYMKEHLVY PPKGKLPALP KATPECDVWT AIFDAVSLVN PCFDVYQVAT TCPLLYDVLG
     YPGSFEYLPA GANVYFNRTD VQKAINAPLQ KWTECSERPV FVDGKDNSEP SSFTIIPDVI
     EKSPRTIIAH GDLDYVLISN GTLLSIQNMT WGGAQGFSQE PSKPLFVPYH DRGSLSTLSG
     AGVLGRHHTE RKLTYVELYL TGHMGPQYNP SASYRILEYL LGRIDDLSK