ID   A2965_ARTBC             Reviewed;         592 AA.
AC   D4B3C8;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Putative amidase ARB_02965 {ECO:0000305};
DE            EC=3.5.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_02965;
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], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC       ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; ABSU01000033; EFE30174.1; -; Genomic_DNA.
DR   RefSeq; XP_003010814.1; XM_003010768.1.
DR   AlphaFoldDB; D4B3C8; -.
DR   SMR; D4B3C8; -.
DR   STRING; 663331.D4B3C8; -.
DR   PRIDE; D4B3C8; -.
DR   EnsemblFungi; EFE30174; EFE30174; ARB_02965.
DR   GeneID; 9524929; -.
DR   KEGG; abe:ARB_02965; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_14_1_1; -.
DR   OMA; HANDSWA; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..592
FT                   /note="Putative amidase ARB_02965"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434657"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   ACT_SITE        266
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   BINDING         263..266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P97612"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   592 AA;  64011 MW;  BD81D4022E8490CC CRC64;
     MKGPITFLLQ LGAVYTSIAS ACKLSDLPIL SAHGSYGSNQ CIAFGGEQAV IDRLIDPQAC
     DIPKLIEATA DQLQDGLTKG CFTSVDLVKV RITLQTPYRQ GNVLIIVVVQ TYVARIAEVN
     STVRAVTEIN PDALTIAKQM DNERKMGKLR GPLHGLPIVI KNNIFTDDKM SSTAGSYAIF
     GARTSADATV ATKLREAGLV IMGKSGASQW ANFRSLNSTN GWSAYGGQVT AAYIKNQDPS
     GSSSGSGVAS DLGLAFATLG TETSGSIVSP ADKSNIVGLK PTVGLTSRRF VVPISERQDT
     VGPMARSVKD AAYLLQVIAG KDSNDNYTSA IPFDTIPDYV KACDINALKG KRIGVPRNVI
     KIFGSPQTVV DQFNQALAVM KKAGAIIVEN TDFTSFAEFA QSPIPDDILY ADSLTNLPAF
     FKQLKVNPHN ITDLESLRRF TQHHRLEEYP SRDTARWDIA LQKGIKNTDP KFWPMYQKNV
     KFGNEGGILG ALRRHKLDAA VLPTDLSPYI PALIGSPIIT VPMGVYPNGT KVNHDRELVT
     SGPGIPIGIG FMGDLWSEEK LIGLAYAFEQ KTHARPKLKR FIQPKKEVKG IL