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Database: UniProt
Entry: A0A165XZU9_9AGAM
LinkDB: A0A165XZU9_9AGAM
Original site: A0A165XZU9_9AGAM 
ID   A0A165XZU9_9AGAM        Unreviewed;       654 AA.
AC   A0A165XZU9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SISSUDRAFT_993829 {ECO:0000313|EMBL:KZT32723.1};
OS   Sistotremastrum suecicum HHB10207 ss-3.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT32723.1, ECO:0000313|Proteomes:UP000076798};
RN   [1] {ECO:0000313|EMBL:KZT32723.1, ECO:0000313|Proteomes:UP000076798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT32723.1,
RC   ECO:0000313|Proteomes:UP000076798};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; KV428301; KZT32723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165XZU9; -.
DR   STRING; 1314776.A0A165XZU9; -.
DR   Proteomes; UP000076798; 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   ECO:0000313|EMBL:KZT32723.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT   DOMAIN          177..531
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   654 AA;  73319 MW;  7E170ED17386179F CRC64;
     MTTVVNKTAH EFDKQRLEAL LSRRFFYAPA FEIYGGVAGL YDYGPPGSAL QANIINEWRR
     HFIIEEGMHE LDTTIMTPAP VFETSGHVAR FADWMVKDTK TGDVLRADHL VKNVLEARLK
     GDLEARGQAA APVKVDEKAK KKKKEVATTV KQLPDETVAE YEKILAQLDN YSGPDLGQLC
     RTHDLRNPDT GNEVGEPQLF NLMFASSIGP TGQHPGFLRP ETAQGHFLNF SRLLEFNNNR
     IPFASAQIGR SFRNEISPRA GLLRVREFTM AEIEHFVDPL DKRHPRFKEV RDIKLGFLSA
     TVQAEGKTNL SFITIGEAVD QQIVANETLG YFVARIYLFL VKIGIDPKRL RFRQHMANEM
     AHYATDCWDA EIHNSTGWTE CVGCADRAAY DLTVHSNRTG HPLVVRQALS EPIITEREVP
     EFDKKAIGKT FGKDTGTVQK VVAELCQEDL VALKEALAKD EAQISRPDGS KIHIPSSVLK
     IERKTIKQNI REFTPNVIEP SFGLGRILYM LLEHNYWSRA QDVERGVLSF PPLVAPTKCL
     VVPLSAREEF EPLTAEVSSK LRKAGVFSRV DDSSVSIGKR YARNDELGTP FGVTIDFASL
     KNRTITLRER DTTDQLIGSV DEVIEVVTEL VLGSLTWEGA SKRLAKYEGV QDVE
//
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