ID A0A2T4C5E0_TRILO Unreviewed; 893 AA.
AC A0A2T4C5E0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Arginase/deacetylase {ECO:0000313|EMBL:PTB76780.1};
GN ORFNames=M440DRAFT_1234689 {ECO:0000313|EMBL:PTB76780.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB76780.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB76780.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB76780.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ679131; PTB76780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4C5E0; -.
DR STRING; 983965.A0A2T4C5E0; -.
DR Proteomes; UP000240760; Unassembled WGS sequence.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR47558; HISTONE DEACETYLASE HOS3; 1.
DR PANTHER; PTHR47558:SF1; HISTONE DEACETYLASE HOS3; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000240760}.
FT DOMAIN 23..346
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 484..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 96366 MW; 1EC65B86A76876FE CRC64;
MLPSIPFRIH KTDRRLSLLS PAVTNVHGTK WMEEFKMMCE SAESILARGG KELQRPSITR
GPDHAAPETL HEGDLYLCNE SLEAIEGALG AVCEGVDAVF SAGPRRAFVA VRPPGHHCSA
NLPSGFCWVN NVHVGIMHGI LNHGLTHAAI IDFDLHHGDG SQAIAWAHNS RSMAATKNHA
AWKKTSIGYF SLHDINSYPC ENGDDEKIKN ASICIENAHG QNIWNTHLQP WKTTEEFWDL
YETKYSILLD KARSYLKAQA DKLQDAGVNP RAVIFLSAGF DASEWESAGM QRHKVNVPTE
FYARLTQDVV RLAAEEGLCV EGRIVSVLEG GYSNRALTTG IISHLSGLVG KQNVPQRSRL
SFPQGAYDEE DDHIPHSPAS LNPYNPSWWS AGEMDKLESA AALPDITPKK PRVGTPPTYC
TPTHASTARA VDPLRMRRSM STLVNRSTVS SRSPSPSPPE VPWTIAASEL SKLLIPRDRQ
TDSCTFEELN TDATRVRRDR QSAGTPELDR STSRMSLRDR KPRAIDPIQE ENQSRQTRDR
SKTVAAIAAE KATARGQTPQ PIIGMPPKKT NRRLTASAAV PTQRSVSRAA ATNEELPLRP
TTSAGHTAGR PLSVAGNHAQ SSGPSGRITV RRSRPTSSSG EPALRSPMLE AGKETPAEGT
TAPAVSRLDA TIDDMDKITK GIKKIKINLI TQSQKEAREK ARLEAEAAAA AAAATAPGEL
RPSSASTNRS VESGDLKTPN SSVGRRSTIN ATSPDGTMPA LSNASGSTLS TPNLEHFTPR
TLSPEARQVV PNVSSPRSAK ATDEAHGFLQ YQPEGPPPVS VSSQEPLKWL PPSLPAGPPA
VQPGPVKKSS TLFQYGGSGT IPFAKQPTNR SPPSQKAQRQ PSGSARGALP PKK
//