ID G0W7X0_NAUDC Unreviewed; 554 AA.
AC G0W7X0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=PUA domain-containing protein {ECO:0000259|SMART:SM00359};
GN Name=NDAI0C02210 {ECO:0000313|EMBL:CCD23881.1};
GN OrderedLocusNames=NDAI_0C02210 {ECO:0000313|EMBL:CCD23881.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD23881.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD23881.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE580269; CCD23881.1; -; Genomic_DNA.
DR RefSeq; XP_003669124.1; XM_003669076.1.
DR AlphaFoldDB; G0W7X0; -.
DR STRING; 1071378.G0W7X0; -.
DR GeneID; 11496635; -.
DR KEGG; ndi:NDAI_0C02210; -.
DR eggNOG; KOG1154; Eukaryota.
DR HOGENOM; CLU_025400_1_1_1; -.
DR OMA; GMVRADY; -.
DR OrthoDB; 2021096at2759; -.
DR Proteomes; UP000000689; Chromosome 3.
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 Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 2.
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; IPR002478; PUA.
DR InterPro; IPR036974; PUA_sf.
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; PF01472; PUA; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 2.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 444..544
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 61856 MW; BF30BD98018131A2 CRC64;
MSGFIAGSND TTTASTATPL SPASTLETQS YTIVIKIGSS SLVDNVTREP KLSIMTKVVE
TVSCLKKLGH KVIIVSSGGI AIGLNSMNII NKPQVLSEIQ ALAAIGQGKL ISMWEMLFRQ
YDQKVAQILL TRNDILNWNQ FKNAQNTINA LLNLNVVPIV NENDTLSISE IKFGDNDNLS
AITSVLINAD YLFLFTDVDC LYTENPNQLQ SHLHSQHSST SLASLSSWAS RISLNDQSPA
STSMFNSQMN LQKLTSPDLQ NYNPNIENDT INGPTPILTV FNTKQKNISK LLKNCSTLNK
SGSNIGSGGM TTKIMAAELA TNVGIHTIIM NSIQPLNVLK IINYIELEFD TKKNFKDFNY
KEELNNIIKL NIPLHTKFIA NKKARNNKNL KRKKNKSTQN SYSYSYSYHD DIKDGNDELM
ESIDKNDYIN KREFWILHGL ISKGSIIIDN ESYNDLISST TKEYEGLLPK DIIDIEDNFH
ELECVEVKVG QKLPNGQLNY EIPLKLIGRA RCNYTSLEIN KIKGLKNSNQ IEDILGYADS
KFIANKENLA LLPR
//
