ID   A0A024SFM4_HYPJR        Unreviewed;       852 AA.
AC   A0A024SFM4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   02-OCT-2024, entry version 37.
DE   RecName: Full=Ste24 endopeptidase {ECO:0000256|ARBA:ARBA00012336};
DE            EC=3.4.24.84 {ECO:0000256|ARBA:ARBA00012336};
GN   ORFNames=M419DRAFT_129141 {ECO:0000313|EMBL:ETS02977.1};
OS   Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS   (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1344414 {ECO:0000313|EMBL:ETS02977.1, ECO:0000313|Proteomes:UP000024376};
RN   [1] {ECO:0000313|Proteomes:UP000024376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30
RC   {ECO:0000313|Proteomes:UP000024376};
RX   DOI=10.1089/ind.2013.0015;
RA   Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT   "Comparative genomics analysis of Trichoderma reesei strains.";
RL   Ind. Biotechnol. 9:352-367(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the peptide bond -P2-(S-farnesyl or
CC         geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids
CC         with aliphatic side chains and P3' is any C-terminal residue.;
CC         EC=3.4.24.84; Evidence={ECO:0000256|ARBA:ARBA00044456};
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   -!- SIMILARITY: Belongs to the taxilin family.
CC       {ECO:0000256|ARBA:ARBA00009550}.
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DR   EMBL; KI911144; ETS02977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024SFM4; -.
DR   KEGG; trr:M419DRAFT_129141; -.
DR   HOGENOM; CLU_016269_0_0_1; -.
DR   OrthoDB; 3080668at2759; -.
DR   Proteomes; UP000024376; 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:0019905; F:syntaxin binding; 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   InterPro; IPR026183; Taxilin_fam.
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.
DR   Pfam; PF09728; Taxilin; 1.
PE   3: Inferred from homology;
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};
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        565..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        589..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          434..618
FT                   /note="CAAX prenyl protease 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16491"
FT   DOMAIN          621..825
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          38..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..379
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        692
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   ACT_SITE        774
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT   BINDING         691
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         695
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   BINDING         770
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ   SEQUENCE   852 AA;  98377 MW;  AF044668C3728F59 CRC64;
     MDSTEASRLL QARISQLEQD AAGEKDQEME IEREVKRANR DLLQQRSSEL LADMRRLERE
     NQKNKKRGDA LQKERDASRT ELSKTVGLKE KLEKLCRELQ RDNNKMKNEN KELQSTQKRN
     NTAWDEKFAS LLSKLEGYQE EKDTPKKQVV DMEMDELFRV RFKSFIEQYE LRELHFHSLM
     RTKELEVQYH LSRHDREKKN AEAEATKARH LQAQVHAFTK TETELRNQLN VYVDKFKQVE
     DTLNNSNDLF LSFRKEMEDM SKKGKRLEKE NEALKRQKEA TTANIIHMAE ERQEWKKKIE
     AAEKKNEKLM SIIQQMQQQG RKVPPAAAST VEACYPESQG PAVVESRGEG EGEDSEYSDE
     EGEEEGLSEF DDDTEEEPQP SEQSAPVPHR NTATMDFLQR LSQFLDRPLF PWKRLILGFS
     VGQFLFESLL TFRQYRVLQS PKPPAVLAKE VSQETFDKSQ AYGRAKARFS VASGLWGQIA
     NFAFIQLDVM PKLWSWTGDL LLRYAPARFT GEISHSIVFV FAFMLIQQGL SLPTRIYSTF
     VLEEKFGFNK QTPGLFISDM VKTNLLTAVL MPPILAGFLK IIQKTGSQFV FYTWVFTAGI
     QLLMTTLYPT FIQPLFNKLS PLEDGELKTK VNELAARFKF PLHELYVIDG SKRSAHSNAF
     FYGLPWKKHI VIYDTLLEKS EPEEVLAILA HELGHWKLGH TTSLFGISQA HLLYIFSLFS
     VFINNRSLYA SFGFHNERPI IIGFLLFSDA LSPMDTVIQF LLHIVSRTFE FQADAFANSL
     GMRAELATSL IKLHVQNLSS MDADWMYASY HFSHPHLSER LKALDWKGEQ AVTSEKEKEQ
     EGVVKATGRD EL
//