ID   A1864_ARTBC             Reviewed;         666 AA.
AC   D4B093;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Secreted protein ARB_01864 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_01864;
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], AND INDUCTION.
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:21919205}.
CC   -!- INDUCTION: Expression is up-regulated in presence of human
CC       keratinocytes. {ECO:0000269|PubMed:21247460}.
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DR   EMBL; ABSU01000023; EFE31245.1; -; Genomic_DNA.
DR   RefSeq; XP_003011885.1; XM_003011839.1.
DR   AlphaFoldDB; D4B093; -.
DR   SMR; D4B093; -.
DR   STRING; 663331.D4B093; -.
DR   EnsemblFungi; EFE31245; EFE31245; ARB_01864.
DR   GeneID; 9526437; -.
DR   KEGG; abe:ARB_01864; -.
DR   eggNOG; KOG4419; Eukaryota.
DR   HOGENOM; CLU_019028_0_0_1; -.
DR   OMA; PLEWGQI; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd07407; MPP_YHR202W_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; -; 1.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR014485; Pesterase_C1039.
DR   InterPro; IPR041823; YHR202W_N.
DR   PANTHER; PTHR11575; PTHR11575; 1.
DR   PANTHER; PTHR11575:SF22; PTHR11575:SF22; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF017316; Pesterase_C1039; 1.
DR   SUPFAM; SSF55816; SSF55816; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..666
FT                   /note="Secreted protein ARB_01864"
FT                   /id="PRO_0000434920"
FT   REGION          323..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   666 AA;  75191 MW;  D74A1AA68CCE80AF CRC64;
     MRFSTLVSLA AWAAAALACD SCSEPGKPAE HKRLVRRMQP EALGALTKPK GPLEWGQINF
     LHTTDTHGWL EGHLKEQNYG ADWGDYSSFV KHMRQKADRL RVDLLLIDCG DLHDGNGLSD
     STSPNGVISN EIFSRVDYDL LSIGNHELYV TDVAYETFAN FSKVYGERYV TSNVQIINKE
     TGEYEYIGSK YRYFTTKHGL KVMAFGVLFD FTGNSNVSKV IKAADLVQES WFIDAVKTPK
     PVDLFIIFGH TPARTDDKFP TLRTLRQKIQ ELRPGVPIQA FGGHNHVRDF VVYDETSTAL
     GSGRYCETLG WLSMTGINSR TFRGSMKPRG VPNPTRRAIK GNATTSTQPY QHPRKGLDLR
     YARRYLDWNR LTFAYHASKS QDRQFDTQKG LKITHDITDA RKQLNTSTVL GCVPETYCMS
     CVPFEAKNNI YQLVIDMLAK VVVKEDRADK PRLLLLNTGG VRFDLVKGPF TKDDEYIVYP
     FKNQFQYLPD VPYSIAKELL DALNKGPYQR RSEEYSPMAP QLSTNEVCAN PSPEFVQLKR
     REAPQPYRPI TRRTIDSSML YPGYVTSDDF GLDGDDTPHS KIPYFKVPID IQANASFPTN
     GSMPTVVDLA FVDYIGAKYV IPALNKLGGK YSASDIQSYK DFGSSSFLRE YALEFWQEGL
     PNCTTN