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
//