ID G3J921_CORMM Unreviewed; 792 AA.
AC G3J921;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=CCM_02324 {ECO:0000313|EMBL:EGX94053.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94053.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX94053.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX94053.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(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; JH126400; EGX94053.1; -; Genomic_DNA.
DR RefSeq; XP_006667539.1; XM_006667476.1.
DR AlphaFoldDB; G3J921; -.
DR STRING; 983644.G3J921; -.
DR GeneID; 18164351; -.
DR KEGG; cmt:CCM_02324; -.
DR VEuPathDB; FungiDB:CCM_02324; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; G3J921; -.
DR OMA; ALMFEYM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000001610; 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:UP000001610};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 287..778
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 792 AA; 89671 MW; D4D9DE9FE964E36D CRC64;
MLSSGSTRLW VCTRCVRRRV TRLPQFQQRL RHSTAATAAA DAYKPLVSHG VSPDHDDAVL
RDLFDAPSGT FASFSLKRSQ GLFKNRYLTS PDGFLVFAQK NLDRATRIVN RVLAATSTND
YRAVVRDLDR LSDLLCRVLD LSDFVRMTHP EIRFQQAATD AWSLVYQYMN QLNTMTGLSD
QLNEAISRPE VTDQWTDEEK IVADLLKLDF MKSAVSLPKK SRDRFVELSS QISDVGSAFV
QTMAPEKRKV TLPSHRFYGL YPSLASTLKV RSQISIPTTG SEAAAALQSV YDEGTRKEIY
LTQRTASSRT IGHLENMLRL RAELAGLAGF QSHGHMSLKD RMMAKSPSSV MQFLLALREH
NAPMIQTELN ELQDRKRERL SMPDAELYPW DRDFYMERIR AEMRSKVRHE DQLTAFFSVG
TVMQGLSRLF DRLYGIRFVP RETLPGETWH PDVKRLDVMS DNGEQVAVLY CDLFYRPQKS
PNPAHFTVRC SREILPDEVD EAGADLGSAD MPYFDSPEQA ANDGMEISRG GGPLKQLPTI
ALVCDFPKND NAREPAFLSF YSVETLFHEM GHAIHSILAR TSFQNVSGTR CATDFAELPS
TLMEHFAADP TVLSLFARHW KSDRPLPYDM VAERIKVAKR FEGIDTEHQI LLAMVDQAYH
SPEVSEPSFD STYVFHDIHK RFAHGPLDPP RTRWQGFFGH LHSYGSTYYS YLFDRVLAER
VWRVIFSGGE GGMAVSRANG ERLKENLLQW GGGRDPWTCL AETLHDDRLA AGDEKSMALV
GSWGIKDSAK TK
//
