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Database: UniProt
Entry: C1GF61_PARBD
LinkDB: C1GF61_PARBD
Original site: C1GF61_PARBD 
ID   C1GF61_PARBD            Unreviewed;       488 AA.
AC   C1GF61;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=PADG_05897 {ECO:0000313|EMBL:EEH49818.1};
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:EEH49818.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH49818.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH49818.1,
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).
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DR   EMBL; KN275963; EEH49818.1; -; Genomic_DNA.
DR   RefSeq; XP_010761463.1; XM_010763161.1.
DR   AlphaFoldDB; C1GF61; -.
DR   STRING; 502780.C1GF61; -.
DR   GeneID; 22584744; -.
DR   KEGG; pbn:PADG_05897; -.
DR   VEuPathDB; FungiDB:PADG_05897; -.
DR   eggNOG; KOG2509; Eukaryota.
DR   HOGENOM; CLU_023797_0_1_1; -.
DR   InParanoid; C1GF61; -.
DR   OMA; GYTPCFR; -.
DR   OrthoDB; 239638at2759; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001628; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEH49818.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT   DOMAIN          208..435
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  55865 MW;  F0195DA7A506E276 CRC64;
     MLDIADFVHG PTPEKISESQ ERLRENQRRR GAPVEAVDEV VALFKIAREA RYEVTQIGEK
     INKVQKEIGK KKKNKEDVSD LIAEKVELGK QKKDADALAT EKELLRDQKL RTIGNYVHED
     VPTSQNEDDN AILSSWAPEG FKEEKPAFCL SHDDILHRLD GFDQKRGTKI FGHRGYCLIN
     YGLLLNLALV NYGLEFLFKK KYTLNQPPYF MLKQFMAKTA QLEQFDEELY KVTENEDKAS
     ERYLIATSEQ PLSALHSGEW LHDTDLPIKY AGYSTCYRKE AGSHGKEVMG IFRVHQFEKI
     EQFVITKPED SWDSFKDMMK NSEEFYQSLG LPYRVVDIVS GALNNAASRK NDLEAWFPSQ
     GTYKELVSCS NCTDYQSRAL EIRYRAKKDS ADEKDCSDEN KKTYVHALNA TLCATERTLC
     CLLENYQTET GIIVPEVLRK YIPGQPTEIL YTKDLVEKSS ADKSKSKNKQ NPGPNNGCVI
     QEMQNLKV
//
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