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
//