ID A0A367LAC4_9HYPO Unreviewed; 1088 AA.
AC A0A367LAC4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ste24 endopeptidase {ECO:0000256|ARBA:ARBA00012336};
DE EC=3.4.24.84 {ECO:0000256|ARBA:ARBA00012336};
DE Flags: Fragment;
GN ORFNames=L249_7662 {ECO:0000313|EMBL:RCI11366.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI11366.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI11366.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI11366.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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 -!- 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:RCI11366.1}.
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DR EMBL; LKCN02000010; RCI11366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LAC4; -.
DR STRING; 1330021.A0A367LAC4; -.
DR Proteomes; UP000253664; 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 Reference proteome {ECO:0000313|Proteomes:UP000253664};
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 802..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 827..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..972
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 672..856
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 859..1063
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..478
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 930
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 1012
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 929
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 933
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 1008
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:RCI11366.1"
SQ SEQUENCE 1088 AA; 124449 MW; 35502235DD39CA6B CRC64;
SIKAASSLTT APRVDARRDA AIPFRYVLQR VGRLKSSRAR TPHASRFKAR WTPSLIAVII
LFTVMPASQI ETELANGHEA HAHHTHPPPA AGRKAKGKMA MDSSEASRLL QARISQLEQD
AAGEKDQEIE IEREVKRANR DLLQQVSKMD VMQRIDHLTK RSTELLADMR RLERDNQKNK
KRGDILQKER DANRTELSKT VGLKEKLEKL CRELQRDNNR MKNENKDLQT TQKRNGMAWD
EKYASLLAKL EGYQEEKDTP RKQVVDMEVD ELFRVRFKSL IEQYELRELH FHSLMRTKEL
EVQYHLSRYE REKKNAETES NKARHLQLQV QAFTKTETEL RNQLNVYVDK FKQVEDTLNN
SNDLFLSFRK EMEDMSKKGK RLEKENDALK RQKDTTAANI IRMAEERQDW KRKLEAAEKK
TEKLMSIIQQ MQQQGRKLPP GTSSTVEGCY AGAEGDESDY SDEEDEEALS EFDDDTEEET
QPSSRPVTYG PERPPPPPPP PPPQQQQQQQ HQQQHQQQHQ QQKQASQPAE ATETQVGDDG
STVVTHHKVE GSDKEAKIQA LHELLQRRDS GESVDAGEVT RLVWDLMPRP RVADVAEQRA
GVLPHRRLDV FQPPASFYFA PSPRSIASIP ASMDFLQRLS RFLDRPLFPW KKLILGFSIG
QYVFESILTL RQYQVLLQKK PPAVLAKEVS QETFDKSQAY GRAKARFELI NGLWAQVQNV
AFVQMDILPA LWDWCGGLVA SYAPAVLSGE IGHSIVFVYV FILLQQVLGL PGRIYHTFVL
EEAYGFNKQT PKLFVVDMIK TNVLTAVIMP PILAAFLAII RRTGNQFVFY LWAFSAALQL
FTTTAYPIFI QPLFNKLSPL DEGELKKKVE DLAASQKFPL NDLFVIDGSK RSAHSNAYFY
GLPWKKHIVI YDTLIEKTET SEIVAILAHE LGHWKLGHTT RLFAIAQVHL LYIFSLFSVF
VNNASLYSAF GFHRSHPIVI GFILFSDALS PMDCILKLLL NILSRKFEFE ADDFAKQLGH
RAQLASSLIK LHAQNLSTMD ADPVYATYHF SHPHLSERLK ALDWKPSVAL TSEKDKDKAV
KASGREEL
//
