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
//