ID R9XMY7_ASHAC Unreviewed; 508 AA.
AC R9XMY7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=AaceriAGR240Wp {ECO:0000313|EMBL:AGO14095.1};
GN ORFNames=AACERI_AaceriAGR240W {ECO:0000313|EMBL:AGO14095.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO14095.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CP006026; AGO14095.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XMY7; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000016920; Chromosome VII.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..508
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004483678"
FT DOMAIN 47..390
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 416..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 317..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 508 AA; 54761 MW; C6ACAE6DC44A2D31 CRC64;
MLSLVSSTFA ILASCFYLNV LAHGAGGRSN AGNAFLLMPL HFNEDHYATD IEVGTPPQKI
SVLFDTGSAD LWVQTANNPF CIGAAHEQEE VHGVAVTPYI DCNGLTIFDA NSSRTLQVLS
NNMYINYVNT FVDGSWAIDR LIICDQDVSG MQFGVVRVSN TEMNGILGVG YERLEAVQGY
AGATNVTYPN LPSTLKQRGV IQKVAYSVFL QATAESDGEV LFGAIDASKY IGNLHTVPVV
NIRSPQQQPN SFHIMLQGMG LHDQALPAGR LCTSKSYPAL LDTGTNGMVV PSAVARCIAA
ALNATFNEDK RVFKIECPTE DDEREFTFNF GELQLVAPLS NFLIPASDMG TEQCEVAIMP
GESDTFTLGL PFLKAVYTVF NLEDNEISLA QANVKPQQPD IIPILEEVPG ARIDSRVSRP
ATSCEARSPT ATAHEGPLAS NQSASGYELH HHSQAPIRRS SLVSRGSVAS KEPINFPDAS
VVTATATARV TRTIAVTQCE QTCLTMIM
//
