GenomeNet

Database: UniProt
Entry: A0A0D2BXV1_9EURO
LinkDB: A0A0D2BXV1_9EURO
Original site: A0A0D2BXV1_9EURO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system