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-JUN-2021, entry version 29. 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|ARBA:ARBA00001947}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KI911144; ETS02977.1; -; Genomic_DNA. 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="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 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 //