ID A0A0V0VKY6_9BILA Unreviewed; 474 AA.
AC A0A0V0VKY6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
DE Flags: Fragment;
GN ORFNames=T09_15637 {ECO:0000313|EMBL:KRX64155.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64155.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64155.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64155.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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: 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:KRX64155.1}.
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DR EMBL; JYDN01000025; KRX64155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VKY6; -.
DR STRING; 181606.A0A0V0VKY6; -.
DR Proteomes; UP000054681; 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:UP000054681};
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 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 129..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 350..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 383..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT DOMAIN 52..234
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 238..473
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 337
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX64155.1"
SQ SEQUENCE 474 AA; 54555 MW; 0A26058C160DDEE5 CRC64;
LAMFAEAMQS EETLSNLNQQ SEKYAFPEIL FYAFFTVHWI IYLWDLYLSI RQYRTQRNCT
ETPEGLGEIL NDEQFQKARL YKLDKARFSF LTSTVDQLAI TVILLLNMIP KMWAFCGTIC
TKMGADGEII QSVVFSFTTF IISTVFNFPF SVYSTFVIEE RHGFNKQTMK LFICDELKKI
AIMTVLALPV IAVLIAIIKV GGSMFFVYVI IFLTIVSFLL LTIYPEYIAP LFNKYTPLPE
GELRTRLEQL AGKVEYPLKK IFVVDGSKRS GHSNAYLYGF WKNKRIVLYD TLLADDCLPK
EESVDDANAE KNNADEKPVL KQMGMNIDEV VAVLGHELGH WKLWHNVMNI IWAEFNMVVQ
FGLFALLYKK TELYMAFGFY DDYPIIIGLI IIFDFVLAPL NVVLGVIHTY VSRQLEFAAD
DFSAKLGYAK LLQSGLIKLS QDNLAFPVND WLYSCWHFSH PPVPERLAAL RKYD
//
