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Database: UniProt
Entry: A0A194S7R1_RHOGW
LinkDB: A0A194S7R1_RHOGW
Original site: A0A194S7R1_RHOGW 
ID   A0A194S7R1_RHOGW        Unreviewed;       659 AA.
AC   A0A194S7R1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=RHOBADRAFT_51764 {ECO:0000313|EMBL:KPV76768.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV76768.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV76768.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV76768.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KQ474075; KPV76768.1; -; Genomic_DNA.
DR   RefSeq; XP_018272817.1; XM_018416003.1.
DR   AlphaFoldDB; A0A194S7R1; -.
DR   STRING; 578459.A0A194S7R1; -.
DR   GeneID; 28976451; -.
DR   OMA; DPAHDGN; -.
DR   OrthoDB; 1203010at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF6; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..659
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008265526"
FT   DOMAIN          223..555
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          47..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   659 AA;  67878 MW;  8D72804F28A6910A CRC64;
     MLPPTPLPFP HLVALLLSAL AATASTAAPS PSPTHPSTAT LRSAVPSLEQ PAPEATAARP
     APPGGIHLPL HRRNGHLHHL SRRSRADQED IVRSWAVRER GRLLGKYGQS EARLRRRDGA
     VAASQSPVGV EARRRGVEGG EAAALERRQF GVGGALSSRT TASTTTSATA FRTAGFGTAT
     SGTDSGSGSS TSSGTKTAPT RIPTQSSSVG EVHLVNYDAD LSYYAPIGIG VPAQYLNCIL
     DTGSADLWVA SDYCSSDDGC SSTIPLYNST LSTTALDMNT SFSVKYGSGS AQGEIFQDYV
     SFAGYNVSSQ AFALVESVSE TILGGEISGL MGLGWQPLAA SSVTPFWQNL YQANALPFPG
     FGVSLTRYID VANASAVEPG GSLTFGYLNA SLYSSEINYL DIPAGMESYW VVRMDAVAVN
     GTNATSWAQG DGQMVAIDTG TTLIGGPRDV VASVYAQVEG AKAATGNYNG YYSYPCDNNV
     SIALTFGNIT YNMSAVDFNL GPFGIDAETN RSTCLGAFFN LNFGSGSKIS WVVGAAFLKN
     VYSVYRASPP SVGFALPPNS TSARLPSFPS NSSDPAHDGN LTVAPAGIYG PSGGVSLRTT
     LVPANTVTTA VQAGGSVGQV PSSGAAARFG RASWAVLGVA TAAGLHLVGA AAVGPAGWA
//
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