ID F9XMJ0_ZYMTI Unreviewed; 807 AA.
AC F9XMJ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=MYCGRDRAFT_49589 {ECO:0000313|EMBL:EGP83254.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP83254.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP83254.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001206; EGP83254.1; -; Genomic_DNA.
DR RefSeq; XP_003848278.1; XM_003848230.1.
DR AlphaFoldDB; F9XMJ0; -.
DR STRING; 336722.F9XMJ0; -.
DR EnsemblFungi; Mycgr3T49589; Mycgr3P49589; Mycgr3G49589.
DR GeneID; 13396562; -.
DR KEGG; ztr:MYCGRDRAFT_49589; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; F9XMJ0; -.
DR OMA; ALMFEYM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000008062; Chromosome 11.
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:UP000008062};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 299..781
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 25..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 90106 MW; 1092388AC2F8B874 CRC64;
MKRLGREAWT CSRCIRQSRR SLATSSTARG AAAAATATTA SRAENHHPIS KAAPSTRHDD
KTLRDIFDDP RAWQDFSLRT KYHRSGRNAG LLQNRYLTRP EGFGEFARVT LQKSRKIVAQ
VLAYDSVEGY KRIARDMDRL SDLLCRVIDL SDFIRSVHPD REIQAAATQA YAMMFQYMNV
LNTTTGLDSQ LKKAVSIPEV FQSWSEEERT VADILIRDFA KSAIDLPEAE REAFVRMSDE
VQETGNEFVE NMATETPHLS FDSSKMKGMD PVLARQLTKW GKITLPTEGM PATLATRTVE
DADIRQEIYV ANRTSSKDNI HRLERLLRLR AESAKLAGFD SYARLTLSDK MAKSPESVMS
FLDGLAQVNE PHVRGEMAEL LALKRADAHS SSVFSSEHSL HAWDKEYYTQ KLLNANRSRA
RTPDALSAYF SLGTVFQGLS RLFHRLYGIR LVPRETLPGE TWNSDVRRLD VIDDHQGHIA
VIYADLFERA GKSPNPAHFT LRCSRRIDDE EMQEAAQLSS QPGSPFQTAQ EAVNDGLAVS
YNPRDGNALY QLPTIALICD FAPPSAYSAK GTRPTLLTFR ELTTLFHEMG HALHSICGRT
ALQNVSGTRC ATDFAELPSV LSEYFAAAPE VLALYARHWE TDAPLDASRI AERVELDRSM
QGAETESQIL LAMLDQRYHS SDPLGPSNSS TEVYHDVWSK YSSVPEPAGT SWQGFFGHLF
GYGGTYYSYL FDRAIAGKIW RDVFQRTQGG AVNPAAGQLY REEVLRWGGG RDGWKCVAGV
LREGKGGVLA EGGRGAMEMV GKWGVHT
//
