ID   M28P2_ARTBC             Reviewed;         497 AA.
AC   D4AM42;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable zinc metalloprotease ARB_04732;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=ARB_04732;
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).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000002; EFE35798.1; -; Genomic_DNA.
DR   RefSeq; XP_003016443.1; XM_003016397.1.
DR   AlphaFoldDB; D4AM42; -.
DR   SMR; D4AM42; -.
DR   EnsemblFungi; EFE35798; EFE35798; ARB_04732.
DR   GeneID; 9521926; -.
DR   KEGG; abe:ARB_04732; -.
DR   eggNOG; ENOG502R701; Eukaryota.
DR   HOGENOM; CLU_047420_0_0_1; -.
DR   OMA; NNDMIGN; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; PTHR12147; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..497
FT                   /note="Probable zinc metalloprotease ARB_04732"
FT                   /id="PRO_0000411756"
FT   DOMAIN          411..497
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  54811 MW;  A4AF7951CB05DF6A CRC64;
     MRFLISSLLS GLALLTSLHA FVLALPREYS ISMSNPFHES LFSCPAASWP RVKLGSENTP
     QEPSKDLRKI LSQISPKRIE TTIRKLVSFG TRHTLSTQTN ATYGIGAARE WIESEFQRYA
     NASDGRLTVK VVGYDQQADG NRIPFPVRIS DVVATLKGEG DPERVYVVSG HYDSRNSDPL
     DYKGIAPGAN DDASGVAVSL ELARVMSQRD LPRPKATIVF AAVAGEEQGL YGANFLAQSF
     RNSSTNVEGM FTNDIIGSST ADDGTKEPHV IRLFAQGIPP LNVENQAMRE RRIMIGGDND
     TPARQLARFV KETAENKHTD MEVSVIYRLD RYLRGGDHRP FLEAGYPAAR FTEPNGNYAH
     QHQDIRIDKD PKTGKDIQYG DLPEFCDFDF ISRVGKVNAA ALWNLAMSPG MPRNVRVNTT
     ALSNDSKFSW DPPAGGNALV GGYEIVWRST TAPFWTHKMD VGMVQEATID LSKDNVVFGI
     RARGKNGERG VAVLPFP