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Database: UniProt
Entry: G4UKB9_NEUT9
LinkDB: G4UKB9_NEUT9
Original site: G4UKB9_NEUT9 
ID   G4UKB9_NEUT9            Unreviewed;       555 AA.
AC   G4UKB9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   13-SEP-2023, entry version 49.
DE   RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE            EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN   ORFNames=NEUTE2DRAFT_144186 {ECO:0000313|EMBL:EGZ73468.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73468.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ73468.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000256|ARBA:ARBA00000857};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; GL891217; EGZ73468.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4UKB9; -.
DR   STRING; 510952.G4UKB9; -.
DR   eggNOG; KOG4163; Eukaryota.
DR   HOGENOM; CLU_001882_4_1_1; -.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   NCBIfam; TIGR00408; proS_fam_I; 1.
DR   PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE/PROLINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
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, ECO:0000313|EMBL:EGZ73468.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT   DOMAIN          90..330
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          496..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          5..32
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   555 AA;  62761 MW;  3BDC3022BCE60ADB CRC64;
     MEENKDQSKS ALKKAEKAAQ MAAKKAEKAA KQATLPVVGG KKADDIIGIT VKKSENFSQW
     YQEVVLKAEL IEYYTEISGF FIMRPATMYI WNVIRKWFQE HIDELGVEET NFPMFLSQKS
     LEKEKEHVEG FAPELAWVTK AGDKDLEVPV AVRPTSEAVM YPYYAKWIRS HRDLPFRLNQ
     WNSVVRWEAK QTTPFLRARE FMWQEGHTAH LTEQAAGEEV LQILEFYAGV YEQLLAVPVV
     RGRKTEAEKF AGGYYTTTVE GYIPSNGRGI QGATSHCLGQ NFSKMFDITV EDPAEKGKHI
     HVWQNSWGLS TRVIGVMVMI HGDDKGLVLP PRIAKIQSIL IPVGLTAKMS AEEKDAHMKK
     VDELLATLKK AGVRADVDTR EGYTPAWKFN DWELKGVPLR IEFGPKDAAK DVVSYARRDT
     GEKGTIPIAE LTTKVPELLE TIQQDMYNKA EVSFREHRLK IEKWDDVVPA LDAKNVVLIP
     HCLVPECEDK IKELTTGRSD EAAEGPESQK APSMGMKSLC IPFEQPEGLV KGETKCLNPE
     CSRLAEQWCM FGRSY
//
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