ID A0A0V0ZN72_9BILA Unreviewed; 533 AA.
AC A0A0V0ZN72;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ste24 endopeptidase {ECO:0000256|ARBA:ARBA00012336};
DE EC=3.4.24.84 {ECO:0000256|ARBA:ARBA00012336};
DE Flags: Fragment;
GN Name=Zmpste24 {ECO:0000313|EMBL:KRY14017.1};
GN ORFNames=T12_4285 {ECO:0000313|EMBL:KRY14017.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY14017.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY14017.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY14017.1};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2};
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:KRY14017.1}.
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DR EMBL; JYDQ01000126; KRY14017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZN72; -.
DR STRING; 990121.A0A0V0ZN72; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRY14017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..237
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 241..475
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 423
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 419
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:KRY14017.1"
FT NON_TER 533
FT /evidence="ECO:0000313|EMBL:KRY14017.1"
SQ SEQUENCE 533 AA; 61336 MW; A8CA02EA854E5BFA CRC64;
LAMFAEAMQS EETLSNLNQQ SEKYAFPEIL FYAFFTVHWI IYLWDLYLSI RQYRTQRNCT
ETPEGLGEIL NDEQFQKARL YKLDKARFSF LTSTVDQLAI TVILLLNMIP KMWAFCGTIC
TKMGADGEVK KIIQSVVFSF TTFIISTVFN FPFSVYSTFV IEERHGFNKQ TMKLFICDEL
KKIAIMTVLA LPVIAVLIAI IKVGGSMFFV YVIIFLTIVS FLLLTIYPEY IAPLFNKYTP
LPEGELRTRL EQLAGKVEYP LKKIFVVDGS KRSGHSNAYL YGFWKNKRIV LYDTLLADDC
LPKDESVDDA NAEKNNADEK PVLKQMGMNI DEVVAVLGHE LGHWKLWHNV MNIIWAEFNM
VVQFGLFALL YKKTELYMAF GFYDDYPIII GLIIIFDFVL APLNVVLGVI HTYVSRQLEF
AADDFSAKLG YAKLLQSGLI KLSQDNLAFP VNDWLYSCWH FSHPPVPERL AALRKKVEIQ
YLGIDLKKSV CITGSRPINV ALAGKYSIQR WQTNVIERIS RNIINQYFRI SCH
//
