ID A0A0G4N657_9PEZI Unreviewed; 918 AA.
AC A0A0G4N657;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=BN1708_008620 {ECO:0000313|EMBL:CRK41962.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK41962.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK41962.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK41962.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-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; CVQH01027194; CRK41962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4N657; -.
DR STRING; 100787.A0A0G4N657; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000044602; 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); 2.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 2.
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; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
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:UP000044602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 287..548
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT DOMAIN 556..905
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 918 AA; 102493 MW; 9E4593E86F30B58C CRC64;
MFKTPTRGLW VCTKCARDSV SRVQRRSWLS AASGAASASH PVDRSAPGAV RDDAILRELF
DSPARTAKAF KASELQPSAG LFKNRYLTSP NGFIVFARRS LQKASKIVDR VLGASSTAEY
KAIVKDLDRL SDLLCRVLDL SDFVRMTHPD PRFQQAAAGA WSLVYQYMNQ LNTMTGLSDQ
LTKALANKDV VASWSEEEKT VADILKLDFT KSAVNLPQRE RDRFVDLSQR ISEVGSDFVS
EMAPEKEEIV LPSSSFYGLY PSIARALTRG GKVRLPSMSA EAQAALRTVK DEDTRRAVFI
ASRTASRRTV HRLDTMLKLR SELAELSGFQ SYAHLALKDR MMAKTPGSVM QFLLALQQHN
KPIVHKEMAD LLAQKQTHLD GMATKVEPWD KDYLMDSVRL DMRLPVRHPD QLAAYFSIGT
VMQGLSRLFS RLYGIRFVPR ETLPGETWHE DVRRLDVVTD AGDQIAVLYC DLFFRKDKSP
NPAHFTVRCS REISESEVEE AAAEVDGGDA GPRFDSAAQA ANDGMESSTQ GGVFKQLPTI
ALVCDFQKHE DWKSPRLYGI RFVPRETLPG ETWHEDVRRL DVVTDAGDQI AVLYCDLFFR
KDKSPNPAHF TVRCSREISE SEVEEAAAEV DGGDAGPRFD SAAQAANDGM ESSTQGGVFK
QLPTIALVCD FQKHEDWKSP SPALLTFHQV ETLFHEMGHA IHSILARTSL QNVAGTRCAT
DFAELPSTLM EHFAADPTVL ALFARHWRID EPLPYAMIAE RLRMSKRFEG FDTENQILLA
MLDQAYHGPE VAGPGFDSTR VYHGLQSRFA AGPTDPPETC WQGFFGHLHG YGSTYYSYLF
DRVLAERVWR VVFAAGADGK AVDRASGERL KENLLKWGGS RDAWRCLSDT LQDERLKEGD
EKAMAIVGSW GIKDDHHA
//
