ID M3IN06_CANMX Unreviewed; 680 AA.
AC M3IN06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=G210_1760 {ECO:0000313|EMBL:EMG47786.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47786.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47786.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG47786.1}.
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DR EMBL; AOGT01001372; EMG47786.1; -; Genomic_DNA.
DR AlphaFoldDB; M3IN06; -.
DR STRING; 1245528.M3IN06; -.
DR eggNOG; KOG2089; Eukaryota.
DR HOGENOM; CLU_001805_1_1_1; -.
DR OMA; KNFQSAM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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:UP000011777};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 217..677
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 680 AA; 78879 MW; 41326EBB34577CD7 CRC64;
MSIDFEQIVE TQDFPLWNQS PEQVLEIANA IATNETKLFD QIAAVENPTV ENVLKPFAKH
YNGESFPEGQ ITFYQHVSTD QELRDSSTKG EEIMDNNSIE QWSREDVYKV FQKLYDSVKD
DASLDAESKR YLEKSITAFK RNGLALPEET REKVKKLQVE LNNLRVQFAK NLNEDKGYVL
FTKEELDGIP EDTLNQYEEV DGKLKVTFKY PDIFPVFKHA NVSNTRKVAN VAYGNRCVEN
GPILENIIKI RYEIAKLLGY DTYSDYVLEE RLAKTKDTVL NFLTDLRGKL TPVAENELKV
LKEFKKEDLK ARGLEPEDEF YSWDYNYYNE RLLEKKYKVD HVKIAEYFPL ESTVAKMLGF
YEKIFDIKFV KVNKPDPKAT WHEDVQQYAI YQNVKEGGKA LEFMGWIYFD LHPREGKYGH
AANFGLGPGY LEQDEKTRHT PITVLVCNFT KPSKDKPSLL KHDEVTTFFH ELGHGIHNIL
SKTKYARFHG THVERDFVET PSQMLEYWTW SKNELKELSS HYKTGEPISD ELIDQLISTK
HVNTGLFNLR QLFFGIFDMS LHTVSSQEDL DNLDIFKTWN KLREEVTLLP SDNNTTKGYA
SFGHIAGGYE SGYYGYLYSL VYAADIYYSL FKEDPMNLEN GIRYRDIILK PGGSKEIMDN
LVELLGRKPN SEAFLQEIFG
//