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-DEC-2020, entry version 27.
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).
RN   [2] {ECO:0000313|EMBL:ETS02977.1, 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};
RG   DOE Joint Genome Institute;
RA   Kuo A., Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X in
CC         which C is an S-isoprenylated cysteine residue, A is usually
CC         aliphatic and X is the C-terminal residue of the substrate protein,
CC         and may be any of several amino acids.; EC=3.4.24.84;
CC         Evidence={ECO:0000256|ARBA:ARBA00001213};
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   MEROPS; M48.001; -.
DR   EnsemblFungi; ETS02977; ETS02977; M419DRAFT_129141.
DR   KEGG; trr:M419DRAFT_129141; -.
DR   HOGENOM; CLU_016269_0_0_1; -.
DR   OrthoDB; 422892at2759; -.
DR   Proteomes; UP000024376; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of 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   InterPro; IPR027057; CAXX_Prtase_1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR032456; Peptidase_M48_N.
DR   InterPro; IPR026183; Taxilin_fam.
DR   PANTHER; PTHR10120; PTHR10120; 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   Coiled coil {ECO:0000256|SAM:Coils};
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="Peptidase_M48_N"
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   COILED          89..119
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          191..211
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        51..84
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..379
FT                   /note="Acidic"
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   METAL           691
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   METAL           695
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT   METAL           770
FT                   /note="Zinc; 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
//