ID C1GF12_PARBD Unreviewed; 656 AA.
AC C1GF12;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000256|ARBA:ARBA00030057};
GN ORFNames=PADG_05848 {ECO:0000313|EMBL:EEH49769.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH49769.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH49769.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH49769.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; KN275963; EEH49769.1; -; Genomic_DNA.
DR RefSeq; XP_010761436.1; XM_010763134.1.
DR AlphaFoldDB; C1GF12; -.
DR STRING; 502780.C1GF12; -.
DR GeneID; 22584699; -.
DR KEGG; pbn:PADG_05848; -.
DR VEuPathDB; FungiDB:PADG_05848; -.
DR eggNOG; KOG2298; Eukaryota.
DR HOGENOM; CLU_015515_1_0_1; -.
DR InParanoid; C1GF12; -.
DR OMA; MEMQYFV; -.
DR OrthoDB; 546660at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.30.40.230; -; 1.
DR Gene3D; 3.30.720.200; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-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; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEH49769.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 160..523
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 122..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 74398 MW; 4B08E4DAF994F5DA CRC64;
MATNSTKTGQ PLDRATLDSL LRRRLFYTPS FEVYGGVSGL YDYGPPGCAL QANVVDLWRK
HFVLEEDMLE VDCTMLTPHD VLKTSGHVDK FADWMCKDPK TGEIFRADHL VEEVLETRLR
GDKEARGQKV EVDEEEEAKR KKKTKETKAV KLDDALVKEY EEVLAKIDNF NGEELGQLIT
KYEIKNPVTG GDVLPPVSFN LMFQTSIGPS GGLPGYLRPE TAQGQFLSFQ KLLDFNQQSM
PFASASIGKS FRNEISPRSG LLRVREFLMA EIEHFVDPDG GKKHPRFHEV QDLELSFLDR
EVQLSGSTKV ERMTIGKAVA DKIVDNETLG YFLARIQLFL LKIGIDESKI RMRQHMQNEM
AHYAKDCWDA ELFTTYGWIE CVGCADRSAY DLTVHKNKTG APLFVRETRS EPLRIEEWQI
DLDKKKFGPR FRKDGKAVEA AVNALSQDLL AKLSLDLTEN GKIEIDVDGV RSGKVELEKD
IINIEKRTRV ENIREYTPNV IEPSFGIGRI LACLMEHVYW SRPDDEARGV LSFPPIVAPT
KVLLVPLSNN PSFQPLVHRL TLKLRRLGVS NRVDDSSASI GKRYARNDEL GTPFGITVDF
QSVKDNTFTL RERDTTKQVR ASEEEICKAV KSLVEGEETW DDIKKRLPEF VSQDAE
//
