ID A0A1G4KCI0_9SACH Unreviewed; 455 AA.
AC A0A1G4KCI0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
GN ORFNames=LAMI_0G15676G {ECO:0000313|EMBL:SCV02075.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV02075.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCV02075.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV02075.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family.
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU366005}.
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DR EMBL; LT598469; SCV02075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4KCI0; -.
DR STRING; 1230905.A0A1G4KCI0; -.
DR OrthoDB; 3080668at2759; -.
DR Proteomes; UP000191024; Chromosome g.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:UniProtKB-UniRule.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU366005};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366005};
KW Membrane {ECO:0000256|RuleBase:RU366005};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366005};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366005};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW Transmembrane {ECO:0000256|RuleBase:RU366005};
KW Transmembrane helix {ECO:0000256|RuleBase:RU366005};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 196..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT DOMAIN 40..225
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 228..448
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 396
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 455 AA; 52051 MW; 019FD4F3C946B4E9 CRC64;
MAWIDNLQGF FDKPGIPWKS IVLAFTIGQF SFETYLTFRQ YRALSKKGLP KVLEGEIDEE
TVAKAEDYSR AKAKFAIFSD VFSLVQNLCI MKFDVLPRMW HWGLLLAKRM PTKLAPTSII
GQSLYFVCVL SNISTLLGLP LSYYQHFVLE EKFGFNKLTI KLWFSDLVKS TTLSAVIGMP
LMYAFLKIFE YFPSNFLWYI CSFVLVVQIL ALTLVPVFIM PLFNKFTPLE DGELKTSIEA
LATRVNFPLD KIFVIDGSKR SSHSNAYFTG LPFTSKRIVL YDTLVKDASI DEITAVLAHE
IGHWQKNHLL RMLALSEVHI FFLFTLFTAA YQNKSLYASF GFHSGHLLSQ DPRLVFTQEL
PILVGFMLFN DLLQPLDCVL NFSMMLVSRL HEYQADAYAK GLGYSKDLCR ALINLQVKNL
STMNVDPLYS SYHYSHPTLP ERLDAMDYLS VKKGN
//
