ID   A0A420Y239_9PEZI        Unreviewed;       511 AA.
AC   A0A420Y239;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=HOM3 {ECO:0000313|EMBL:RKU41943.1};
GN   ORFNames=DL546_004909 {ECO:0000313|EMBL:RKU41943.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU41943.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU41943.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU41943.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000709,
CC         ECO:0000256|RuleBase:RU003448};
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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:RKU41943.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QVQW01000065; RKU41943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420Y239; -.
DR   STRING; 177199.A0A420Y239; -.
DR   Proteomes; UP000275385; Unassembled WGS sequence.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-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; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF59; ASPARTOKINASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          448..511
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          316..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  56170 MW;  E7C7ED06E61007C6 CRC64;
     MKDQMVRNSS PNGWVVQKFG GTSVGKFPDQ IAEQVIRPWL ENNKLVVVCS ARSTGKKVTG
     TTSRLLEIFK RLQGIAAATN DESLQHALIE EARRIANDIC EDHLNAVDTF VRDESLRASI
     KADIESECRT LVEYLEVAKR FNLEINSRAK DRVVSYGEKL SCRFMTCLLQ DRGIAAEYVD
     LSDVIHTDSA TRVDANFYRD AAALFRKKIE ACESRVPVVT GFFGNVPGSL LDGDIGRGYT
     DLCAALVAVG LKAEELQVWK EVDGIFTADP TKVPTARLIP SITPSEAAEL TFYGSEVIHH
     LTMDQVIKAV PPIPTRIKNV KNPRGEGTIV RPDPSLAPGQ QLQRSRKPSD PRDRKNPKRP
     TAVTIKDNIS IINIHSNKRS IAHGFFARVF SILNQHRVSV DLISTSEVHV SMAVHTGNGG
     SAEFDQVVKE LADCGDVSVL TDMAILSLVG ADMKNMIGIA GKMFSTLGEH RVNIEMISQG
     ASEINISCVI DASEAERAMN ILHTNLFTFL D
//