ID   A0A125PHT0_9BASI        Unreviewed;       727 AA.
AC   A0A125PHT0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KWU42276.1};
DE   Flags: Fragment;
GN   ORFNames=RHOSPDRAFT_21543 {ECO:0000313|EMBL:KWU42276.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42276.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU42276.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU42276.1,
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ954512; KWU42276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A125PHT0; -.
DR   STRING; 1305733.A0A125PHT0; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000062823; 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; 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:SF87; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KWU42276.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          413..724
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          199..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..242
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        615
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        444..449
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KWU42276.1"
SQ   SEQUENCE   727 AA;  78363 MW;  9B9C69D15420B828 CRC64;
     WVCTIKGWVV LESLLLAAQY FAAAWTLRRV VFPILKGLFE NVLSYQVLHG PVHDWIDQIK
     VIFYGCMIYV AVGVCGALGA IFEIMILLWI YALYLIGTAI LNAKTIWSLL QSVRAAEEKF
     GKACNFVFAG KCQGYMEDLK TASLSQTSLL YTYAGAGFVL ACQLLTLVCV LIQIRRIHKK
     TKSWLFTFCG KRLGRKKHRP KDEEENALEK EIPDGRRRRR RRSAAEDRQS SLAHRSRARA
     QRIRVELPPA TFDLPRKTQP RRATNEQRLK FGSLSLTAGS KRRSSAGTSL RPAHRRRARC
     ASWTPFMIDI RAPLTCGLMM AACPARTPST LAIPLFKRAI PKESRLVDAD GVVNFAVLNQ
     TLAGLKGKYH VTQSAAQAHT GRRPFSDGDS QRLARRASTG SDSLTSYQND NLWAGKITIG
     SPAQSFVMDF DTGSSDLWVP SSACSGSGCG THAKYTAKSS STSNAVTGKT LNVQYGDGST
     ASGPVYSDSV TVGGLTATGQ TFGTATTLTG NFGSSPSDGL VGMAYPALSQ LGVSPFFNTL
     WSEGRVAANS FSFRLATQNS AASELYLGGL NSAKYIAGTT GYTPVISQTY WAINTNVAVN
     GQAVSGLGTL AAIADTGTTL IVVPTADAQT FWASVPGAAP YSGGGGYYTF PCNQTPKVTF
     QFPGSTTKWA TPYLNLGTVS YGSNQCVGAI VGQDAGLNAW ILGDSFLKGV YTTFDFSNNR
     VGFSQLA
//