ID A0A1V6PUN4_9EURO Unreviewed; 469 AA.
AC A0A1V6PUN4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE AltName: Full=Seryl-tRNA(Ser) synthetase {ECO:0000256|ARBA:ARBA00034892};
GN ORFNames=PENANT_c033G01900 {ECO:0000313|EMBL:OQD80671.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD80671.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD80671.1}.
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DR EMBL; MDYN01000033; OQD80671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PUN4; -.
DR STRING; 416450.A0A1V6PUN4; -.
DR OrthoDB; 239638at2759; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00414; serS; 1.
DR PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 189..421
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 435..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..100
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 444..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 53716 MW; E4FCB705B28957BA CRC64;
MLDLSDFVTE RGGDIKKIKE SQQKRFAPEE TVDEVIALYE EARRARYEVT QIGSQLNALQ
KEIGMKKKNK EDANELFGQK AELEKRKKQA EEAAVDKEVQ RDRKIRTIGN YVHESVPVSN
DEEDNQVIRT WAPENAQMDR PGCLSHHEVL TRLDGYDPER GVKIVGHRGY CLTGYGLFLN
LALINYGLEF LFNKGYKPNQ PPQFMLRDLM AKTAQLEQFD EELYKVTESE DKTTDKYLIA
TSEQPLSALH DSEWLQDKDL PIKYAGYSTC YRKEAGSHGK DAWGIFRVHQ FEKIEQFVLT
KPEDSWQAFE DMMSTSEEFY QSLGLPYNIV AIVSGALNNA AAKKYDLEAW FPFQKEYKEL
VSCSNCTDYQ SRALEIRYGT KKATDLKKTY VHALNATLCA TERTLCCVLE NYQREDGIVV
PEPLRKYIPG APEFLPYTKD LPKDSTSTKT KSKSKGTDDA TKKMQGLQV
//