ID A0A0D2BXV1_9EURO Unreviewed; 793 AA.
AC A0A0D2BXV1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=Mitochondrial intermediate peptidase {ECO:0000256|ARBA:ARBA00018046};
DE EC=3.4.24.59 {ECO:0000256|ARBA:ARBA00012441};
DE AltName: Full=Octapeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032470};
GN ORFNames=PV08_06155 {ECO:0000313|EMBL:KIW16104.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16104.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW16104.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16104.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal octapeptide as second stage of
CC processing of some proteins imported into the mitochondrion.;
CC EC=3.4.24.59; Evidence={ECO:0000256|ARBA:ARBA00000436};
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; KN847495; KIW16104.1; -; Genomic_DNA.
DR RefSeq; XP_016236320.1; XM_016380493.1.
DR AlphaFoldDB; A0A0D2BXV1; -.
DR STRING; 91928.A0A0D2BXV1; -.
DR GeneID; 27333238; -.
DR VEuPathDB; FungiDB:PV08_06155; -.
DR HOGENOM; CLU_001805_0_0_1; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; cd06457; M3A_MIP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR033851; M3A_MIP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 280..764
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 793 AA; 88523 MW; 3121A23E6301A040 CRC64;
MHKVLRRQPW TCPKCLRRQK RLNSTATGTA SQQNDAFASA YVQSSPARQT DNAQLREVFN
DRVSWRTSEK KSSGLIGNNH LTTPRGFKTF AERSVAQCKR LVERTLAAST VEQYRAIPKD
LDRLSDLLCR VIDLSDFIRG IHPDAAVAAA ATASYSLMFQ YMNELNTTTG LNKQLQKAWD
MPEVRSQWTE EERMVAKLLM KDFAKSGIDL PEKQRKQFVS LSNEIAQIGT DFVNQMEHAR
DQITLSTQQL QGVDPLLIRN LKAWDRAQIP VYSAASKTIL NSANDPETRK QIYVAERTAS
RSTVRKLEQL LLRRAELAKL TGYDSYAQMT LADKMSKTPE SVSNFLDSLN ENNRPQVQKE
LASLLEIKRK LDQGAKSVDP WDHTYLLAKL AQVEASAGPR TSRSRLQESA SAYFSLGHVM
QGLSNLFESL YGVRLVPKET QPGEVWHPEV KRLDVYTDKQ QHIATMYCDL FSRPGKLPNP
AHFTLLCSRE ISEEEVRECQ ERNEPLNNGM PTYLGSNAVS GVTAHHQIPI IALVCGFPDP
SSSAGPSLLS VHSVTTLFHE MGHAIHSILG RTTLQGISGT RCATDFAELP SVLMEYFATD
ATVLKMFARH WQTGAVIPDD MITALADDRT KQAATTGAWN NESQILMAIL DQVYHSEGPV
EALQIGHYNS TAAYHDVWNK YGSVAEPRET AWQGFFGHLY GYGASYYSYL FDRAIARQVW
RAVFKDGADG GAVDRSAGEH FKQEVLRWGG GRDPWLCLEG LMGEGRGVLA EGKEEAMLEV
GRWGVGASSE GSM
//