ID A0A673BA91_9TELE Unreviewed; 961 AA.
AC A0A673BA91;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000256|ARBA:ARBA00032857};
GN Name=pitrm1 {ECO:0000313|Ensembl:ENSSORP00005039291.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005039291.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005039291.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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DR AlphaFoldDB; A0A673BA91; -.
DR Ensembl; ENSSORT00005040299.1; ENSSORP00005039291.1; ENSSORG00005016743.1.
DR Proteomes; UP000472271; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:UP000472271}.
FT DOMAIN 443..690
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT REGION 311..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 109170 MW; B2B10468463AF6F3 CRC64;
MIRSINTLAI HLFHCYIQNK WPQSCNNFPV KCFGFPSSFR GQTYTWRLKS TSATERALHY
QPGQKIHGFT VQEVVAVPDL FLTAVKLSHD KTGAQYLHAA REDSNNLFSV QFRTTPMDST
GVPHILEHTV LCGSEKYPCR DPFFKMLNRS LSTFMNAFTA SDYTMYPFST QNTKDFQNLL
SVYLDAVFFP CLREQDFWQE GWRLENENPT DPSSRLVFKG VVFNEMKGAF SDNERLYAQH
LQNKLYPDHT YSVVSGGEPL DIPDLTWDQL KNFHATHYHP SNARFFTYGD LPLEEHLRQI
EEEALSRFDR INPNTEVPPQ PQWSSPREDH VTCSPDALAP DQSKQNTLCM SYLLGENGFE
EERIEAILHK IEIQMKHQST NFGLSLASYI ASPWNHDGDP VELLQISDCV SKFRKALREN
PHFLQDKVQN YFKENTHRLT LSMSPDETYL DKQAKAEEEK LQKKIQALTD SDRKDIYEKG
LELLSAQSKP QDASCLPALK VSDIEPTIAI TPVHLSSAGG VPVQYCEQPT NGLVYFRAMC
SLNTLPEELK PYVPLFCSVI TKMGAGSLDY RQQAQQMELR TGGVSVSTQV IPDSTHMDMY
EQGILLSSSC LDRNLPHMFE LWTDIFSSPH FDDEERLRVL VMMSAQELAN GISYSGHMYA
MTRTGRHLTP AGDLQETFTG MDQVKFMKRI AEMTDLIHVI RILPRIKKHL LNPDNMRCAI
NTTPQKMCDA EGQLESFIKD VCGNRKERKP VRPNIIKVSF NVQLWLYSNS NFLPCQMKTF
FPMPFPVNFI SESIRTVPFS HEDFASLSIL ARMMTAKFLH GEIREKGGAY GGGARMGGGG
LFSFYSYRDP NLVQTLSAFR GGVDWAKLGQ FTQQDIDEAK LSVFSAVDSP IAPSDKGLGQ
FLSGITDEMK QGHRQRLFSV THRNLVDVAE RYLSVGQSTR GVAVLGPETD TIKKDPSWIV
K
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