ID A0A166AWR8_EXIGL Unreviewed; 703 AA.
AC A0A166AWR8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=Mitochondrial endopeptidase {ECO:0000313|EMBL:KZV95839.1};
GN ORFNames=EXIGLDRAFT_765912 {ECO:0000313|EMBL:KZV95839.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95839.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV95839.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95839.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC mature size. While most mitochondrial precursor proteins are processed
CC to the mature form in one step by mitochondrial processing peptidase
CC (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC processing by MPP is a required step for a subgroup of nuclear-encoded
CC precursor proteins destined for the matrix or the inner membrane.
CC {ECO:0000256|ARBA:ARBA00025208}.
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; KV425951; KZV95839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166AWR8; -.
DR InParanoid; A0A166AWR8; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000077266; 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:UP000077266};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 228..696
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 703 AA; 79282 MW; F89F81A0CA22E529 CRC64;
MNTVAHIAVQ HVRLSSPPRT RTCNANLAAL FAVGSRCGQV AVHCRRFLLF SSPAIFPIHE
CDILRRQQRR HLDSTFSDVF GALAETESAI FARGEPLTFY QNVSTNSALR DASAAAEVAL
KEYGIEREMR IDLFDAAKDA RASANTLSGE DERLADKILL EGKRAGLDLP EEQRKELESK
NCNEEKGKIA FTPEELEGIP ADVVSGYAKR DDGKLELTFK TPDVMPLFRY AKNPDTRRRA
WEGYESHVAI NAAVFETVLA TRRKIAALLK YDTWADYITE VKMVKTAQGV HDFIADVESK
LLPVGKRDRK QLPALKQKEE GADASEFYVW DWYYYDRLYV ERTLDLADAL VKEYLPVQEV
VPTIMNVYES MLGVEFVPLS NDVEKGDIWH PEVQRFAVWE AGATDASGFV GYTYLDLYPR
EGKYSHAAVW PLVPGFVLAD GKTRNYPVTA MVANLAKPTP DRPALMTHDN VVTFFHEMGH
VFHGLLSRTK YARFRGTSVA RNFVEVPSQM LENRCWVPSV LAKMSSHYKT KEPLSPELID
KIIKSRYVNI GMFMLRQLFF GKYDITVHTS KSASFLPAIH TSHNDLFSCR VGRLYETLGP
PSRRNLARQG ASSRHARTRF LRAPNGRLRR GIYGYAYSLV FAADMYRAVF AKDPLSPEAG
WLYRKQILGP GGSRDEMDSL KAFLGRPPNS EAFLEQLLGS ASQ
//
