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Database: UniProt
Entry: A0A0N0NK86_9EURO
LinkDB: A0A0N0NK86_9EURO
Original site: A0A0N0NK86_9EURO 
ID   A0A0N0NK86_9EURO        Unreviewed;       683 AA.
AC   A0A0N0NK86;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN   ORFNames=AB675_3969 {ECO:0000313|EMBL:KPI37539.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI37539.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI37539.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI37539.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI37539.1}.
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DR   EMBL; LFJN01000023; KPI37539.1; -; Genomic_DNA.
DR   RefSeq; XP_017997502.1; XM_018144068.1.
DR   AlphaFoldDB; A0A0N0NK86; -.
DR   STRING; 1664694.A0A0N0NK86; -.
DR   GeneID; 28735948; -.
DR   OrthoDB; 2021096at2759; -.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04242; AAK_G5K_ProB; 1.
DR   CDD; cd21157; PUA_G5K; 1.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR041739; G5K_ProB.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01027; proB; 1.
DR   PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1.
DR   PANTHER; PTHR43654:SF3; GLUTAMATE 5-KINASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPI37539.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          492..608
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   REGION          618..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  72788 MW;  5229BF3F13298557 CRC64;
     MFPGVAVVTG AAGTGMGQAI AKAFAGEGCN RIAITDINAS LLDKTAAEIK EKYAGVQVLA
     HAGDISDHEF VDGFFTLVVE KFGRIDYAVN CAGIMGNNQS STDTSLDDFD KITNVNYRGC
     WLSSRAELKQ MVQQEPLESH DGRPGERGSI VNIASQLGIV GRPRAPAYCA SKSAVIGMTR
     CDAIDYSEHG IRVNAICPGI IATPMTTGSS SIVDERTHEP ILSILSIIVE TAIRLRRDGH
     KVVIVSSGAI AVGLKRMTIP KRPKHLAQVQ VSFGSNWTIS LMSIWDSLFG HMDQPVAQVL
     LTRNDIADRT QYLNAQNTLA ECLSFGVIPI VNENDTISVS EIKFGDNDTL SAITAAMVNA
     DYLFLMTDVD CLYDKNPRAF PDAQPITVVE DIDRLQADVS SKGSALGTGG MATKITAARL
     ATAAGTSTII TNSSKPGNIS NIIHYLHPDT SSANGISSPA PNVPPLHTRF LPSATPIRSR
     AFWILHGLHP HGSIYIDRGA AAALSTHAGL LPVGIVAVTG TFAQQEAVRL IVVDRTKMGS
     LSPRADTTLE GSISTFSQPA MEFIDYDNGE EIGRAVVNYS STEVARIRGL RSKDIASVLG
     YADSEYVAFR ENVSLREHAN AGSRASRPET PAPQTPTKAA SRTPDASISD LRDLHISKEE
     EGSRTPNAGH ITPAAETPAA SEV
//
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