ID D4DGJ1_TRIVH Unreviewed; 796 AA.
AC D4DGJ1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 28-JUN-2023, entry version 65.
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=TRV_06295 {ECO:0000313|EMBL:EFE39021.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39021.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE39021.1}.
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; ACYE01000359; EFE39021.1; -; Genomic_DNA.
DR RefSeq; XP_003019666.1; XM_003019620.1.
DR AlphaFoldDB; D4DGJ1; -.
DR GeneID; 9583583; -.
DR KEGG; tve:TRV_06295; -.
DR HOGENOM; CLU_001805_0_0_1; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000008383; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 288..762
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 796 AA; 89393 MW; 6275C2F1E4C5EF3E CRC64;
MLRVLQPRPW TCHRCLLRIN VGTSRCYSVA VPERTRLDPA IAGLSGTKRH DDTNLRLVFD
SNSFWREFSQ RQSASSRRTG LLQNQYLTNP EGFRKFAHIS LHKCQKIVGK VLAASTMEDF
RRMAKDLDQL SDLLCRVIDM AEFMKTNHPD PAIQEAATEA FAFIFEYMNI LNTTPGLHEQ
LKRAIENPEV TSHWSEEENV AATAFLRDFA KSAIHLPPED RHRFVTLSNE ISQLGPDFVK
NMNPETSQLS FSKNQLQGMD PDLLRKLKRW SKVTIPMYGS TPKAALSTVE DAEVRRQIHL
AYRTSSREQI GRLETLLQRR AELAKLSGYQ SYAHMTLSDK MARTPEAVVN FLSSLNASNR
GQLDDELSQL LALKQIESPL ATNLQPWDYS YYMEKYYVKH GRARRSRDTD LLPSFFSLGT
VMQGLSRLFT RLYGVRFVPS ETLPGETWNP DVRRLDVLDE DDNHIAVVYC DLFSRPGKSP
NPAHFTLRSS REISPAEIAE CASLPDSPHP NDGMATGLKP GTNRLYQLPT IALICDFDTP
ASSTPSAKPS LLSEHSVRTL FHEMGHAIHS VLGRTDLQSI SGTRCVTDFA ELPSVLMESF
AMDPQVLRLY ARHWSTDDPL PEDMVQNIHR NRQNRDSIHG GMDNETQIIM ALMDQAYHTT
SAGCHIDSTA ILHAVSSKHS SIPDPADSKT AWQGYFTHLF GYGATYYSYL FDRAIANKIW
TDVFGGGDLS VDRNAGERFK NEVLRWGGGR DGWSCVAGVL GASNPANSNG RLSEGGEEAM
REVGRWGLGK TGSSEP
//
