ID G1X9B9_ARTOA Unreviewed; 439 AA.
AC G1X9B9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
GN ORFNames=AOL_s00076g226 {ECO:0000313|EMBL:EGX50261.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX50261.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX50261.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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: 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:EGX50261.1}.
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DR EMBL; ADOT01000124; EGX50261.1; -; Genomic_DNA.
DR RefSeq; XP_011121081.1; XM_011122779.1.
DR AlphaFoldDB; G1X9B9; -.
DR STRING; 756982.G1X9B9; -.
DR GeneID; 22891983; -.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; G1X9B9; -.
DR OMA; FVIEEKF; -.
DR OrthoDB; 3080668at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
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:UP000008784};
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..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT DOMAIN 40..224
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 228..430
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 380
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 439 AA; 50403 MW; 9D8DFDFDFB1ECD8A CRC64;
MDILANLATF FDRPLFPWKK LILGFSVAQY LFETYLSARQ YKVLRKDKIP NQLDGAVEKE
VFDKSQAYGR AKADFGYIKG LYGQLQNVGF IVYDVLPKLW GFTGSLMLTY VPARFNGEIT
HSIIFFFIFN LIVTALNAPI DYYSHFVLEE KFGFNKQTVG LWLTDMIKGQ ALSIVFGAPI
LAGFLKIVQS FGTNFFFYLW AFAVCVQVTM ITIYPLWILP LFNKLTPLEP GKLKTEVEAL
ADKLKFPLKK LYVIDGSKRS AHSNAYFYGL PWAKHIVIYD TLIEKSETEE VVAVLAHELG
HWSLGHTTKL FYIAQFHMFY IFALFSVFIN NRSLYRSFGF HSSHPIIIGF ILFSDVLAPM
DTLVKFFLNM VTRMFEYQAD AFALNLGFGD MLASSLIKLQ VQNLSTMDAD WMYSSYHYTH
PILTERLGAL GWKGQQKKQ
//
