ID A0A0F9XV79_TRIHA Unreviewed; 1405 AA.
AC A0A0F9XV79;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=THAR02_03913 {ECO:0000313|EMBL:KKP03998.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP03998.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKP03998.1}.
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DR EMBL; JOKZ01000091; KKP03998.1; -; Genomic_DNA.
DR OrthoDB; 1331033at2759; -.
DR Proteomes; UP000034112; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.30.2130.10; VC0802-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR009976; Sec10-like.
DR InterPro; IPR048627; Sec10_HB.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR12100:SF1; RECYCLIN-1; 1.
DR PANTHER; PTHR12100; SEC10; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF07393; Sec10_HB; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 448..542
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 514..560
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 155883 MW; 03680E51A2A4EE86 CRC64;
MGSATCDNSS DLGWVVQKFG GTSVGKFPDK IARDIVKANL SRNRVVVVCS ARSTGKKAEG
TTSRLLSVYT KLRNIATPLS SEEKQQELIE QAAGLIQDVC NDHVSAAETF VQDPELRDGL
VAKLKAECQE LIEYIMATKR FNLEINSRSK DRVISFGEKL SCLFMTTLLK DSGVDAEYVD
LSDVLHNDTP SPSLDAGFYK LAVSRFLKKL TACEHRVPVV TGFFGNVPGS LIDGDIGRGY
TDLCAALCAV GLKADELQIW KEVDGIFTAD PSKVPTARLL PSITPSEAAE LTFYGSEVIH
HLTMDQVIRA HPPIPIRIKN VKNPRGNGTV VIPDPILSAA QQLHRSRPSQ RALFKNPRRP
TAVTIKDQIS VINVHSNKRS ISHGFFARVF SILDKQSISV DLISTSEVHV SMAIHADGIR
SEAFETAKRD LAECGDVSIL TDMAILSLVG ADMKNMVGVA GRMFSTLGEH NVNLEMISQG
LIACASTIAT MYRSGGSGPR NRGSILGVLK ATELDARSKL PAEIMVTILN YLPVADQLRC
ARVSHRLREM VYDDTRWVSR LKSMGCWDER EARQRFEESV RRRREAAAAA AAANQANDGK
KNAVASSTIF DATVEQQRRQ RPASELRDGF ETMTIGTSDP AEDPAAYLDV FKRVKSIRGG
ARQEYGKIYK ALAPFYFDLV QAKSHTDPIV FKAFVDPEQQ AQMLANLHKF AGSDWSEGWG
VRDAKLTAMM NIFEAAVLRE FEQGYEFWDV DGRMHRYAHV LHTLNGARTG IELFIQKHPL
FNDRDMVHNP MDCLNQAFTD DITLEPSRRF FEQVLLKVNE QASILERIFP DPAVVFWGLT
EKVAEDIIAE YTTPMFDEAH ERSILSYLKA ISGIFEQTMR FFQSLTPPKG PGEEGEIEKR
AKQLALRVFE PHLDLYLQEE LDFFTKQAEI EVSQWEKKLS EQDSSLESFY MSNINRSAEK
NDFLSSFKKV IMMPVTVLPN FPIGSPFAIN KPTSSPAVTA NGSAVLTPQS SRPQTPGLGN
EIQGRGSSPM PGAKAPTDEL AAKAAIMASK LEGIKSLFSI EVALDLVHKA KSSLGRAAVL
IPLGGQVGGE AKEQCANIFI ALVRILGQRH VKLGFDMAVD HLSQYNPRDV SDHDQKGVAP
LVMFIELVNV GDLISQMIEV FYEQQLAAPK IADKNDFLDP SGLAKKKFEQ MLDESVAAGL
NKGIDVLMDE VEYLQGTLQQ PTDYNPTPRI PVDDGNHRMS HRATLGSMAE LDIGPTPTAR
RIVDLVRSHT NMLIGTTEKS MLDVFNGEVG QRLFTAICKH LKRQRVSTDG AVKLIADMNL
YSDYVRSLRN QDVLPYFAAL RELSQIYLID PGHAKEMATV IADGDRFSGV FRAEEVYEYA
QRRADWYQVR RSVERAMYGM DCLVM
//
