ID H6C3P4_EXODN Unreviewed; 802 AA.
AC H6C3P4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=HMPREF1120_06271 {ECO:0000313|EMBL:EHY58259.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58259.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58259.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58259.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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; JH226134; EHY58259.1; -; Genomic_DNA.
DR RefSeq; XP_009158720.1; XM_009160472.1.
DR AlphaFoldDB; H6C3P4; -.
DR STRING; 858893.H6C3P4; -.
DR GeneID; 20310910; -.
DR VEuPathDB; FungiDB:HMPREF1120_06271; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; H6C3P4; -.
DR OMA; ALMFEYM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000007304; 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:UP000007304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 283..773
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 802 AA; 89374 MW; A02C3DE624F1BD86 CRC64;
MNKLVRRQPW TCARCLRQQQ RYRSTATGAA TATATLDSSY ESAYLHASPA RSSDNALLRE
VFNKKGKWRT AEKKSSGLIG NKHLTTPRGF QKFAETAVAQ CKRVVERTLA ASTVEEYRAI
PRDLDRLSDL LCRVIDLSDF IRSIHPDSAV AAAASASYSL MFQYMNELNT TTGLNQQLKK
AWDMPEVLSH WNEEEKTVAQ LLMKDFAKSG IDLPEQQRQQ FVSLSNDIAQ VGTDFVNQMD
HAKDHVTFSL KQLDGVDPTL VQGMKSWERV QIPVYSSASK VILNSAKSPA TRRTVYVAER
TASRQTIARL EQLLLRRAQL AKLTGYDSYA QMTLADKMSK TPAAVSDFLE SLNANNRVQV
QKELAPLLEL KRKLDDPNAS SIDPWDHSYL LAKLAQFQAA AGPRTSKSRL RENASNYFAI
GHVMQGLSNL FESLYGVRLV PKETCQGEVW HPEVRRLDVY TDKEEHIATM YCDLFSRPGK
LPNPAHFTLL CSREISDEEV MDSQQRGEPL NDGMPTIMGP SVLKRDPHAR ANYQIPIIAL
VCGFPDPSTS VGPAPSLLSL HSVTTLFHEM GHAIHSILGR TSMQGISGTR CATDFAELPS
VLMEYFATDP AVLKSFARHW QTDAVIPDEL LTALADERTT QAERSGGWNN EAQILMSILD
QVYHSTGPVE ALRTGRYNST AVYHEVWNKY GSVPEPPETA WQGFFGHLYG YGASYYSYLF
DRAIARQVWR TVFKDGQSNA ALDRAAGERF KQEVLRWGGG RDPWLCLEGL IGDGRGVLAE
GGQEAMLEVG RWGVGASSEG SM
//
