ID   A0A0A1TH35_9HYPO        Unreviewed;       520 AA.
AC   A0A0A1TH35;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-JUN-2023, entry version 39.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=VHEMI04778 {ECO:0000313|EMBL:CEJ88645.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ88645.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ88645.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CDHN01000002; CEJ88645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TH35; -.
DR   STRING; 1531966.A0A0A1TH35; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000039046; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..520
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001979658"
FT   TRANSMEM        501..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..410
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          433..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   520 AA;  54685 MW;  5ECF83EFE51D1657 CRC64;
     MKTTAAALTA ALLATAEANS YVQWEIERRA VGGEEQINRR DTVFRRAAGA VEEPIKNSVN
     AYFASVAIGN PGQKFDLQLD TGSSDIWVPA ASSNTCKSKG GCPGGSYDPK ASSTYKNLGS
     NTFQISYADE SGAAGDYIQE DFTIAGTLVK NMTMGLALRT KEVEYGLVGV GYMRNEASTQ
     APLRKIYPNL PVALQMQGKT NSIAYSLWLN DKTADKGNIL FGAVDSEKFQ GSLSIMDILP
     DERINNYTHF SVPLTSVSAN SSSGNDILTT QETMPITAVL DSGTSLTYLP DDMAKQAWKE
     AGAIYNNSPE FGIALIPCEF GENNKASFTF GFAGPNGPKI EVAMRDMVVP AYKGKARPFP
     NGPYKGKSIC TFGIQNQTAS EDLPVYLLGD TMLRSAYVVY DLVNNQIGIA PTKFNAAKSN
     IVTFDSNGAK IPNGKTIAGG AKKEPTPPTN QFKAQSGFAS GGGSSTSTIG SNGSNSGSGS
     DSSNSSNGKG DGKNAAVTTS ALSGASLLVL LGSVVYAMAF
//