ID A0A109FMT9_9BASI Unreviewed; 440 AA.
AC A0A109FMT9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KWU47475.1};
GN ORFNames=RHOSPDRAFT_30902 {ECO:0000313|EMBL:KWU47475.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47475.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU47475.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU47475.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KQ954464; KWU47475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FMT9; -.
DR STRING; 1305733.A0A109FMT9; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000062823; 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:SF51; NAPSIN-A; 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, ECO:0000313|EMBL:KWU47475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..440
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007134808"
FT DOMAIN 136..437
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 440 AA; 46433 MW; E291C7659A7DBABE CRC64;
MLPSASVGAL RTVFTLLTFL SFLSEAAAGP SRLSDSSPGT ARVALTKRGR GGWLVSGLTD
DDGVADLASL KNAVSVASAK YRYGAARIYS QTGHTLAGFS PESFQSWSKL ALAANYRNIK
KRQQAALTNY IDGSFWGGKI EIGTPPQCFD VFDTGSSDAW VPGEGVTGYT IFNVSASSTA
EDTGRDFAIR YGDGSTVEGP VYQDTITVAG LTAKQAWFSP INRMAIRFPE SPVDGIVGMG
LEALSNIGEP PFFQSLVEQG VVAKNVFSFT LGESDEGELY LGGTDSSKYS GEIVTTPVID
QGFWMVQGSA LVDGKQTSEN ANMIIDTGTT LVVVPPAEAD KLFAQVPTAK AWKSGGAYNL
YSYDCAAAFT VQLKFGGVVY HIPEKYFNMG LTELGSTRCV AGFAGADIGL DAWIIGGVFL
QAVMSVFDAT AMTVGFAPLA
//