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Putative secreted metallopeptidase (EC 3.4.24.-)

 A6334_ARTBC             Reviewed;         687 AA.
D4AQ27;
11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
10-MAY-2017, entry version 29.
RecName: Full=Putative secreted metallopeptidase {ECO:0000305};
EC=3.4.24.- {ECO:0000305};
Flags: Precursor;
ORFNames=ARB_06334;
Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)
(Trichophyton mentagrophytes).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
NCBI_TaxID=663331;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
STRAIN=ATCC MYA-4681 / CBS 112371;
PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
Staib P., Heidel A., Felder M., Petzold A., Szafranski K.,
Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
Monod M., Brakhage A.A.;
"Comparative and functional genomics provide insights into the
pathogenicity of dermatophytic fungi.";
Genome Biol. 12:R7.1-R7.16(2011).
[2]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=21919205; DOI=10.1002/pmic.201100234;
Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
Staib P., Neuhaus J.M., Quadroni M., Monod M.;
"Identification of novel secreted proteases during extracellular
proteolysis by dermatophytes at acidic pH.";
Proteomics 11:4422-4433(2011).
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
ECO:0000269|PubMed:21919205}.
-!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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EMBL; ABSU01000005; EFE34571.1; -; Genomic_DNA.
RefSeq; XP_003015211.1; XM_003015165.1.
ProteinModelPortal; D4AQ27; -.
SMR; D4AQ27; -.
EnsemblFungi; EFE34571; EFE34571; ARB_06334.
GeneID; 9520935; -.
KEGG; abe:ARB_06334; -.
eggNOG; ENOG410ITS6; Eukaryota.
eggNOG; ENOG4110UDA; LUCA.
OrthoDB; EOG092C0WXZ; -.
Proteomes; UP000008866; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008757; Peptidase_M6-like_domain.
TIGRFAMs; TIGR03296; M6dom_TIGR03296; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Hydrolase; Metalloprotease; Protease;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 687 Putative secreted metallopeptidase.
{ECO:0000255}.
/FTId=PRO_0000434675.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 687 AA; 75039 MW; 1CF7624A26EFC302 CRC64;
MLFTSTAVAA LSGALLIQPA LAAPNGLPSH GGSHHGPKDP FEVLDPQNWV NPDNMTWADF
KSPPGTKWND PSRKGSIRNF NIALVNVDYP DKPFTITMAP GSDVFKNPQP GSPNVTRSQV
PAFYRDFLNK PGKLNRGHTL HEYWMEDSNG RFGVDLTTFG VYKMPLKSYQ YGIGESMNAG
ACPIGETCYY EIRDDALGAW RKDIGEEKAK SFELVFILSA GQDESSTWQE FGEIMFQNKE
DVTSAFGPPP GNGTGNMTLP NYAKTRYVEW TSWASASAIW PNAGDGSSTQ AESSGMGTFA
HELSHLLNVG DNYNNPYGKP LRRSYTGPWS MMSRGSFNGP GGPHTRWQVP PLQGGSMGSQ
HTFHDKIRLG LTTKDSALNI SREALANSGL IVARVTARVI APKPGDLIGI HVAMDKDKSP
KCDVNTDPYC DGNGYQNYNV EVIDRMGADS FCPDSGVMLS KTRDKAFSNY QWTIDANPQD
IKQVDFHRPD GTPAMISLGD YRQLADALFH AGTRSGSQYE YTDKANNLQF YIIEPHRDEA
GVLSYTTAVR YVGGKDPHKR GVKLDKNAKI TSSNTKPTDK GVTCSFTLHN TGTYNPAAGK
AKHPQDVTAY LKSDVYRLKA TVEGRGWRVE VPNALATAEF GKTVTVSVAV GAENSAQDKA
KVTLTATSEA DPSKFATAEC KVNKFRN


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