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Database: UniProt
Entry: A0A0J0XFT4_9TREE
LinkDB: A0A0J0XFT4_9TREE
Original site: A0A0J0XFT4_9TREE 
ID   A0A0J0XFT4_9TREE        Unreviewed;       607 AA.
AC   A0A0J0XFT4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Putative long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:KLT39922.1};
GN   ORFNames=CC85DRAFT_330322 {ECO:0000313|EMBL:KLT39922.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT39922.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT39922.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT39922.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ087245; KLT39922.1; -; Genomic_DNA.
DR   RefSeq; XP_018276413.1; XM_018426917.1.
DR   AlphaFoldDB; A0A0J0XFT4; -.
DR   STRING; 879819.A0A0J0XFT4; -.
DR   GeneID; 28987520; -.
DR   OrthoDB; 3109088at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF9; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KLT39922.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT   DOMAIN          63..451
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          502..578
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   607 AA;  65392 MW;  D942F21FCE47F5DC CRC64;
     MAKKQLTYAE CDALITAPGS EFEMITILEN GHQQRVWKNA PPDFRNFFEG VMQKWADRVL
     VNEPVPEPAE YDARQDVTYG QALKNAYDLA AWLRQQGVGR ADRVAIGGLN SSYWLTAFVA
     INLLGGVPVC LNSTLVQDAQ IHCLGLTKPK VVLVDMKDAQ ILSPVRDQLK AKGVGPLYSW
     NDLSHLPAHL TAGVTSLDFS KLKVDQKVVA DVKAKKGCAV KGEDDALILF TSGTTSLPKG
     VLITQRQGMQ HIHTASIPAA RAALRAGAPV SMALGAHAPP PEQLNVLMPV PLFHVTGLLA
     VTVRVFFAGS KLVFQRRWSV PDAVKLCIDQ KIHMISGVPS IATAILQSGL LPKDFQFAAL
     SYGGAAPAKR LAGDVQKRFP AAFINHGWGM TEAAGLHIAI SGQDYIERPD AVGVAIPIGA
     MRIVDKNRKE VPPNTLGVLH IRGGNVAKGY LDNPKANAEA YTDDGWFDTG DVGIINDEGI
     LYLRDRAKDM IIRGGENIAS AEVENGVTQD PRIAEAAAVP VPDNVLGELV AVGVSLAPGA
     SATPESIMEA AEKRLRYPAR PVFVVVWDGD LPHNANGKLL KNEIKEIVQR KWKEQGGKRV
     GPAKARL
//
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