ID C8Z5L2_YEAS8 Unreviewed; 428 AA.
AC C8Z5L2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 13-SEP-2023, entry version 60.
DE SubName: Full=Pro1p {ECO:0000313|EMBL:CAY78801.1};
GN ORFNames=EC1118_1D0_5831g {ECO:0000313|EMBL:CAY78801.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY78801.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY78801.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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; FN393063; CAY78801.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z5L2; -.
DR SMR; C8Z5L2; -.
DR HOGENOM; CLU_025400_1_1_1; -.
DR Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
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 PIRSF; PIRSF000729; GK; 2.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 322..418
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 428 AA; 47162 MW; 0DBAC7CA98051C80 CRC64;
MKDANESKSY TIVIKLGSSS LVDEKTKEPK LAIMSLIVET VVKLRRMGHK VIIVSSGGIA
VGLRTMRMNK RPKHLAEVQA IAAIGQGRLI GRWDLLFSQF DQRIAQILLT RNDILDWTQY
KNAQNTINEL LNMGVIPIVN ENDTLSVREI KFGDNDTLSA ITSALIHADY LFLLTDVDCL
YTDNPRTNPD AMPILVVPDL SKGLPGVNTA GGSGSDVGTG GMETKLVAAD LATNAGVHTL
IMKSDTPANI GRIVEYMQTL ELDDENKVKQ AYNGDLTDLQ KREFEKLKAL NVPLHTKFIA
NDNKHHLKNR EFWILHGLVS KGAVVIDQGA YAALTRKNKA GLLPAGVIDV QGTFHELECV
DIKVGKKLPD GTLDPDFPLQ TVGKARCNYT SSELTKIKGL HSDQIEEELG YNDSEYVAHR
ENLAFPPR
//
