ID   A0A1E4TXU9_PACTA        Unreviewed;      1047 AA.
AC   A0A1E4TXU9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=PACTADRAFT_49825 {ECO:0000313|EMBL:ODV96488.1};
OS   Pachysolen tannophilus NRRL Y-2460.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV96488.1, ECO:0000313|Proteomes:UP000094236};
RN   [1] {ECO:0000313|Proteomes:UP000094236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC       of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000256|ARBA:ARBA00007575}.
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DR   EMBL; KV454013; ODV96488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TXU9; -.
DR   STRING; 669874.A0A1E4TXU9; -.
DR   OrthoDB; 5477696at2759; -.
DR   Proteomes; UP000094236; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000094236}.
FT   DOMAIN          498..750
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
SQ   SEQUENCE   1047 AA;  118878 MW;  9C8CB71518F99129 CRC64;
     MLRGSGSLGV SRVNTKKLLC RASSGQAPRY DVDKMMAKYP IGLEANGFKV QRVVVVPEFS
     LTAVELSHER TGALHLHIDR DDKNNVFGII FKTNPPNKTG VAHILEHTTL CGSEKYPVRD
     PFFKMLNRSL ANFMNAMTAH DHTFYPFATT NKIDYKNLTD VYLDSTLKPL LREEDFQQEG
     WRLENENLKD KESPLIFKGV VYNEMKGQVS NSSYFFWIKF QESIYPSLNN SGGDPTKITD
     LTYWDLLDFH KQNYHPSNSK IFTYGDLKLI DILEKLNKNF KNFGKRSNKN IVKKHMPLLE
     SKNIIIEGPI DTMVPLDKQF KTSITWYAGD PKDVYNTFLL KILSTLLNDG HSAPFYQELI
     EKGIGIDFSI NSGVESMPEI NLFTVGLQGL NEENSNKLEE IINDILIKVI EKGFESKRIQ
     AIIQQLEISK KMESAEFGMN LLYSLIPGWV NDVDPLEMLK FNETIAKLNK DFIKKGDKIF
     IELIEKYLIK KPNFKFSMKP AENFQDLIIK EEQLRLNSKI KNLNDNEKKL LYERALKLEN
     LQNEKEDLKC LPTLTVNDIP TRGDFVKVDV NENNITNSKC YKRFSPKTNG LTYFRALKTL
     GTEIPVDLIP YLPLFTECLT NLGTTDKSMS ELEEEIKLYT GGISSSVSVS SSPFNIDEPI
     LRFVLTGVAQ NKNFNSVLKI WNTLLKETDF EKNLSKLSIL IKSLANDNLN EIISSGHSFA
     KSYSSSKFSS KAVIDESLNG IKQVEFLNKL NKWNEEGLLL EKVVPNLIKL QELIVNKDNF
     RIMLTCDESI ALTNEKLADD FINGLPSRTG KINSDKPTWS SLLLPSTLTK GSRFKNLIEI
     PSQVNFTSLS RPGIPYVTKD GASLQILSQI LTFKKLHKEI REKGGAYGGG SSYDAINGIF
     NFYSYRDPNP TNSLQQFNDV MNNYIDKSFA TTESFALLEE VSDDSLITTR DLDQAKLSIF
     QQIDAPISVR EEGLNYFVHG INDQIRQERR DHLLNADLND IKSAAEKFLV HGEGPTSEVI
     IGTLKDEDSK LISKKSGWNK VKLGVFD
//