ID G0RFE2_HYPJQ Unreviewed; 796 AA.
AC G0RFE2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=TRIREDRAFT_76502 {ECO:0000313|EMBL:EGR50222.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR50222.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR50222.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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; GL985060; EGR50222.1; -; Genomic_DNA.
DR RefSeq; XP_006963737.1; XM_006963675.1.
DR AlphaFoldDB; G0RFE2; -.
DR STRING; 431241.G0RFE2; -.
DR EnsemblFungi; EGR50222; EGR50222; TRIREDRAFT_76502.
DR GeneID; 18488623; -.
DR KEGG; tre:TRIREDRAFT_76502; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_76502; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000008984; 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:UP000008984};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 296..786
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 796 AA; 89956 MW; A8FEB05C9706ADDD CRC64;
MLNSGGSRLR VCTRCCRRVI KARPGHVRWE STAAAAVNDA AAPASGSDSA KLPIDHFTSS
RHDDALLREL FDAPSNSRPF ANFSLKKSQG LFKNRYLTSP DGFLVFAQKS LQRATRIVHR
MLAASTTPEY QRLIRDLDRL SDLLCRVLDM SDFVRMTHPD VRFQQAAADA WSMVYQYMNQ
LNTMTGLSDQ LGEAMSRPEV TSTWSEEERT VAELLKLDFM KSAVNLPKAA RDRFVELSSR
ISDVGSAFVQ GMEPERKEVT LPAHRFYGLY PGLAAQLKIR SNITIPTTGS EAAAALQSVY
DEETRKEIYL AQRTASSRTI RLLETMLKLR AELANLAGFE SHGHMALKDR MMAKSPASVM
QFLLALRHHN APIIQQELNE LTQKKRERLA MQDATLQAWD RDFYMERIRA EMRSRVRFDD
HLTAYFSVGT VIQGLSRLFD RLYGIRLVPR ETLPGETWHP DVKRLDVVSD NGGQVAVLYC
DLFYRPQKSP NPAHFTVRCS REILPDEIDE VGADLNGPDM PAFESAEQAA NDGMETSSQD
GSLKQLPTIA LVCDFPKNDN AREPALLSLY SVETLFHEMG HAIHSILART SFQNVSGTRC
ATDFAELPST LMEHFAVDRT VLSLFARHWK TDKPLPYDLV AERMRVSKRF EGIDTEHQIL
LAMVDQAYHA PEVADRSFDS TATFHDIQRR YAHGPHDPPQ TRWQGFFGHL HSYGSTYYSY
LFDRVLAERV WRVVFRAGQD GAAVGRDNGE RLKERLLKWG GGRDPWTCLA DTLEDERLAP
GNEKSMALVG SWGIRG
//
