ID M7NLU3_PNEMU Unreviewed; 1019 AA.
AC M7NLU3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=PNEG_02221 {ECO:0000313|EMBL:EMR09638.1};
OS Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. muris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09638.1, ECO:0000313|Proteomes:UP000011958};
RN [1] {ECO:0000313|Proteomes:UP000011958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
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}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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:EMR09638.1}.
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DR EMBL; AFWA02000012; EMR09638.1; -; Genomic_DNA.
DR RefSeq; XP_007874205.1; XM_007876014.1.
DR AlphaFoldDB; M7NLU3; -.
DR STRING; 1069680.M7NLU3; -.
DR GeneID; 19895914; -.
DR VEuPathDB; FungiDB:PNEG_02221; -.
DR eggNOG; KOG0961; Eukaryota.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OMA; CVEGPFW; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000011958; 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:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
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:UP000011958}.
FT DOMAIN 457..729
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1019 AA; 117615 MW; 8705CE5EC0391528 CRC64;
MSYFIKNQDF EAHGRRVRSW RSVRTGIQVV LVDIDVPLTK GKFTKLIIIV LNDSGCPHTL
EHLIFLGSKK YPYKGVLDFL ANRSFAQGTN AWTETDHTAY TISTAGTEGF LHIFPIFIDH
ILFPTLTYDG FYTEIHHIDG DGNDAGVVYS EMQGHENTLN DLQLIHSQRA LFPEGIGYRS
YTGGNLKALR VLNVETVRKY HSKYYLPQNL CIIITGKIDV NELFYVLDQI IEPNILNNLT
PNLENWKRPW VDSPKTPPLK KSHTEIVLFP DKDETVGEVL LAWLGPFSTE FLTLTALNLL
GKYLTDSAIS ALQKELVEIE DQFCSDISFS MTIRLPSVIY LNLYSVPTKK LEKIEERVFE
LLNSVRDNPE NFDINRMSTI IHREKLAIMD TNETDLDGIF TNVIITDFLY GSNTKDTLKR
SLQDYEDYEN LKLWTVTEWL QLLDFWFIQN FHICIISKAS AKLSLELEKN EKIRIENQRK
KLGEEGLKKL REQLRISQEK NDAPFPLTVV SDFKIPSVKN INFITSMSAR AGVAKQKINN
THGEQCSDLQ KYIDQDSLEK IPLYLYFNHI NSKFVTIQVY ISSEHVNSDL KPYLGIYLDN
FFLNGVVRSD GTKLTYEEVV RLLENETVDY SASWGVSASF LEIATIQIKV EIQNYKKGIF
LLKDLFYGSI FEPQRLMIFV FKSLNDIPQE KRNGNKICWA LMRMYQLDKN LSTSKAINIL
SQINFLKRLK DELEKEPNKV VEKFKTIQNQ LFKPENMYFQ IISDILNLEH PVLSWKSFIN
HQEKDDINMS RIPYKKIMLT EKGRTPSGIA HIISLSTVEN SYSVHVSKLF SDFNHKDFPA
FILLLSYLNI MEGILWKHIR GAGLAYSVSF KTDIESGFVY YSIYSSPNVF NVWEKTRVII
NDIKNKKISF DENIMINAKS SLVYDIVSID STPFFAAQES FVSQVIKNQP ENKRRQLIDE
ISNITIDELY VLHNKYLVNL FNSKTSDSFI VTTSSKCDEI MQGFSDAGYN ITKKTFNDY
//
