ID F2PVJ5_TRIEC Unreviewed; 477 AA.
AC F2PVJ5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN ORFNames=TEQG_04923 {ECO:0000313|EMBL:EGE05913.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; DS995743; EGE05913.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PVJ5; -.
DR MEROPS; M16.003; -.
DR VEuPathDB; FungiDB:TEQG_04923; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
FT DOMAIN 49..196
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..392
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 477 AA; 53007 MW; D9F38120ED1C65D6 CRC64;
MASRRLALNF HQAVRSRSAL QAVQRSRRGF ASPVAGTTQS TTLSNGLTIA TEYSPWAQTS
TVGVWIDAGS RAETDQTNGT AHFLEHLAFK GTNRRTQHQL ELEIENMGGH LNAYTSRENT
VYYAKSFNAD VPKTVDILSD ILQNSKLEPA AIERERSVIL REQEEVDKQL EEVVFDHLHA
TAFQGQPLGR TILGPKENIA SIQREQLVDY IKTNYTADRM VLVGAGGVPH EQLVKLAEEH
FGNLPSQPPS SAASAIAAEQ KRQPDFIGSD VRIRDDTVPT AHIALAVEGV SWKDNDYFTA
LVTQAIVGNW DRTMGNSPYL GSKLSTFINH HNLANSFMSF STSYSDTGLW GIYLVSENLT
NLDDLVHFTL REWSRLSYDV SPAEVERAKA QLRASILLSL DGTTAVAEDT GRQIVTTGRR
LSPQEIERVI DGITEKHVMD FAQRKLWDQD LAVSAFGSIE GMLDYQRIRN DMSRDAS
//
