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Database: UniProt
Entry: A0A0D2DXJ3_9EURO
LinkDB: A0A0D2DXJ3_9EURO
Original site: A0A0D2DXJ3_9EURO 
ID   A0A0D2DXJ3_9EURO        Unreviewed;       723 AA.
AC   A0A0D2DXJ3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 37.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=PV06_00483 {ECO:0000313|EMBL:KIW47823.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47823.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW47823.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47823.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; KN847332; KIW47823.1; -; Genomic_DNA.
DR   RefSeq; XP_016268039.1; XM_016400986.1.
DR   AlphaFoldDB; A0A0D2DXJ3; -.
DR   STRING; 215243.A0A0D2DXJ3; -.
DR   MEROPS; M03.009; -.
DR   GeneID; 27352557; -.
DR   VEuPathDB; FungiDB:PV06_00483; -.
DR   HOGENOM; CLU_001805_1_1_1; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06455; M3A_TOP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          217..711
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  82459 MW;  FB04FFDE89CB7995 CRC64;
     MTSAKFRKPP QAPPSFTATP ESVVKDTKEM LAESKKVTDD IVAQIAEKDA TFQNVLLPMA
     HDENLQTLKA HILGFYQSVS TDQALRDAST EAEKLMDDYS IEAAMREDVF KLVDAALKKA
     DKLDPESQRL LEKEHKAFVR NGLNIPAGPK RDRFKEIKKR LSQLGIAFSK NLNEEKGGMW
     FTAQELDGVP EDVLSLLKKE GDKYWLTFKY PDLFPTLKYA TNSETRQKVF VSNENKCNQN
     VPLFQEAILL RDEAARLLGY PNHAAFRIED KMAKTPKTVD DFLHDLRQRL SQGGLDEIET
     LKKMKKADLE SRGEKFDGRY YLWDHRFYDR MMEEKDYQLD QQLISEYFPL QTTIRGMLEI
     FEQLFGLVFV EVVGKDRDSI SPSGKGDDIV WHEEVQVFSV WDDEGEGGGF VGYLYLDLFP
     RNGKYGHAAN FNLQPGFIHT NGTRRYPATA LVCNFSKPTA KKPSLLKHDE VTTLFHELGH
     GIHDLVSRTT YSRFHGTNTV RDFVEAPSQM LENWCWTPSQ LRALSRHYST LSPEYYESWK
     EASGSKTTKP EERIPDDLIQ KLIKTKNLNG ALFNLRQLHF GIFDMTIHEP HDHASLEAMD
     ISETYNALRK DISKIDGPEV LGGGNKWGNG QATFGHLMGG YDAGYYGYLS SQVYSTDMFY
     SVFRKNPMDP KEGRRYRHTV LEKGGSQDEM KTLIEFLGRE PKTDAFYEEL GLTKGTQSGA
     GTT
//
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