ID A0A139AHQ7_GONPJ Unreviewed; 782 AA.
AC A0A139AHQ7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN ORFNames=M427DRAFT_55781 {ECO:0000313|EMBL:KXS16361.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS16361.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS16361.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS16361.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; KQ965754; KXS16361.1; -; Genomic_DNA.
DR STRING; 1344416.A0A139AHQ7; -.
DR OMA; FHNDMKS; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000070544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000070544};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 49..478
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 87501 MW; 8E05CA5D02089393 CRC64;
MSATPSAAPN PPRDDSVQPP WVKPTVPSGS PSWPGLQVLN SLTRQKDDFV PVKGKTVSWY
VCGPTVYDHS HLGHARTYMS TDIMRRILEG YFGYEVLLVM NVTDVDDKII LRARQTHLFS
EFSAANPTVT AELLGTTTTA LAEFVASSFK VSPATEPLLP PKPTEPDAKD LSQWVEEVWK
RWESLTEDGR RKVVEAEPKF EMRIKAALSA SHSLSTPLST PSSTFLSASR DVLSPHLDRL
YGHTVTDPAV YARFSREWEN EFFADMDALG IRRPDVVTRV SEYVDEIKAF VQGIVDKGFG
YTSPSGSVYF DTLRFHTSPG HFYCKLEPKS RSDLALQAEG EGDLSTGKER EKRNAADFAL
QWGKGRPGWH IECSAMASXI LPHPLDVHSG GTDLRFPHHD NEIAQSEACL GTDQWVNYWW
HAGHLNVEGL KMSKSLKNFI TIKEALATSS ANQMRLLFLA HSWSATIDYK KDSLEEARRK
EDAIKNFLAA SKSLVAEARQ KEAELTDDSA ISGKHNYGKW ETDLMESFLT AQSAVHAALA
DSFDTPNALE AVLVLVSRGN VYLNGKPRDG GRINADVVAK VSKWVRWITE VWGIRWESDG
GRGKLEDELL PYLQILSKFR DGVRELARKR GDSDILALSD KLRDEDLVDL GVQLGDRDDG
TALVTFGDPA SLRASRDEKR AKEAERRRLK EAKLREEQQR EQERLEKGRT PPTELFRGES
NKSESGEALY SAWDEQGVPT HDGSGAELAK TRRKKLQKEW DIQAKLHEKF LAHVSKMPSS
AK
//
