ID A0A139HBW0_9PEZI Unreviewed; 853 AA.
AC A0A139HBW0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ste24 endopeptidase {ECO:0000256|ARBA:ARBA00012336};
DE EC=3.4.24.84 {ECO:0000256|ARBA:ARBA00012336};
GN ORFNames=AC578_789 {ECO:0000313|EMBL:KXS99944.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS99944.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS99944.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS99944.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the Cyclase 1 superfamily.
CC {ECO:0000256|ARBA:ARBA00007865}.
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:KXS99944.1}.
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DR EMBL; LFZN01000082; KXS99944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HBW0; -.
DR STRING; 321146.A0A139HBW0; -.
DR OrthoDB; 3080668at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004061; F:arylformamidase activity; IEA:InterPro.
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 GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 3.50.30.50; Putative cyclase; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR007325; KFase/CYL.
DR InterPro; IPR037175; KFase_sf.
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; PF04199; Cyclase; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
DR SUPFAM; SSF102198; Putative cyclase; 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:UP000070133};
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 578..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 423..607
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 610..815
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 819..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 682
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 764
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 853 AA; 95569 MW; 9EF9C75DCDBB08CA CRC64;
MESPVPRYVD LPELVPGFRC SWAYFNSLPS KNSEVDHIGT LNFLTPARKV AAAAEIKDGV
SISLDVPIDH FASVSRAFGG RKPPSHSIHV IDESIHEDSI NFNTQVSSQW DGFRHFGLRS
THQFYNGFRS AHFEQSSVLG TNAWTQAGAI VGRGVLVDVY AYFLSEGVEV NPNSGLKITL
KHVLETLRTQ RTLVMPGDIL IFRTGWLKWF NESSEQERYA ELCLRHLPGQ HHFIGLVQAE
DFVAWLWDSQ IAAVAGDQVA LECTPPPKSG VGWLHEHLLA ALGCPIGELV DTESLAKECK
ERGRYSFFLT SAPLHVSGGV ASPFNGVAIF IDGAPTKAHQ IFSISVPQVH VASDVVFIHQ
HTFAARRRRL HSTTTTTTTT LGGMDLLRRF GGLLDNDNIP WKSIIITFGV AEYALETYLA
YRQYQVQQKK TIPKQLKSEI DQETFDKAQS YGRAKAKFQF VTNTWAVVKK LAEIQYNVIP
LLWGISGTLV ARYGRWGLTG EITQSLVFIF ANAWIDTLLG LPFSYYHHFV LEEKFGFNKQ
TVKLWVTDIL KSQAISIAFG VPIGAACLKI IKATGDNFFF YIWVFMLFVQ LGAITIYPTV
IVPLFNKLTP LEAGDLKDRI DALAGRLHFP LGELQVIDGS KRSSHSNAYF SGLPYLKKKI
VLYDTLIEQQ DTKEIEAVLA HELGHWKKNH TAKLLGIGST HLFAIFALFS AFIHNNSLYK
DFGFPTERPI IIGFILFNMV LSPTDHALKL IMNTFTRKFE YQADKFSYDL GYKAELASSL
IKINIKNLSS MDADWMYSAY HHSHPILTER LRALGYSSEH KVSKDKPKVA GEAPDGVKKA
EFASQANGDR KEL
//
