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Database: UniProt
Entry: R9P5A4_PSEHS
LinkDB: R9P5A4_PSEHS
Original site: R9P5A4_PSEHS 
ID   R9P5A4_PSEHS            Unreviewed;       381 AA.
AC   R9P5A4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAC96397.1};
GN   ORFNames=PHSY_003977 {ECO:0000313|EMBL:GAC96397.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC96397.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
CC   -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006547}.
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DR   EMBL; DF238801; GAC96397.1; -; Genomic_DNA.
DR   RefSeq; XP_012189984.1; XM_012334594.1.
DR   AlphaFoldDB; R9P5A4; -.
DR   STRING; 1305764.R9P5A4; -.
DR   GeneID; 24109263; -.
DR   eggNOG; ENOG502S76B; Eukaryota.
DR   HOGENOM; CLU_049918_2_1_1; -.
DR   OrthoDB; 1694531at2759; -.
DR   Proteomes; UP000014071; Unassembled WGS sequence.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.2140.20; -; 1.
DR   InterPro; IPR001447; Arylamine_N-AcTrfase.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR11786:SF0; ARYLAMINE N-ACETYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR11786; N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00797; Acetyltransf_2; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014071}.
FT   REGION          353..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  42861 MW;  970D8AE2D89AEE14 CRC64;
     MPNLRPKHLA SRLTEAQTRT VLSTISFPHF TPTSSLPPPT LTTLSLLHIH FLTTFPFEAL
     SLNYEPGGLM SPHLPDIYSR FVERRLGGGY CLQVNQLYRE MLSALGFRWI GVMGRVFANG
     DWSGLTHTTT LVLLDSHVDS SKKVYYLSDV GFGSSPHRPL LLRDGWEEFG RGGEKFRLVK
     ADVHPSSIFE ESDEQTDDAE VLAIASNQTT WRLQNRKKAD KDWENCYSFS PLECFTPDYI
     ATNKATSHAQ SVPFATTILV VRYLLHLQLV SQSEALVERD GLAKDLYPYH PSVVEQRLIV
     GDRYLVRVGD EVKVDKVISS EEERVGLLKS EFGLLQHVET QVAVNEISGK PSRLKSDEKK
     VKEEHKVEVN GSSTRSTIDT A
//
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