ID A0A091DDG2_FUKDA Unreviewed; 1029 AA.
AC A0A091DDG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00039362};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN ORFNames=H920_10146 {ECO:0000313|EMBL:KFO28285.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28285.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28285.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28285.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of cysteine to
CC tRNA(Cys). {ECO:0000256|ARBA:ARBA00037196}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00036537};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC Evidence={ECO:0000256|ARBA:ARBA00036537};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; KN122776; KFO28285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DDG2; -.
DR STRING; 885580.ENSFDAP00000021287; -.
DR eggNOG; KOG1668; Eukaryota.
DR eggNOG; KOG2007; Eukaryota.
DR Proteomes; UP000028990; 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 CDD; cd10310; GST_C_CysRS_N; 1.
DR CDD; cd15837; TNFRSF26; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR034062; TNFRSF26_N.
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; PF00020; TNFR_c6; 2.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00208; TNFR; 3.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF57586; TNF receptor-like; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KFO28285.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00206};
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:UP000028990};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REPEAT 88..128
FT /note="TNFR-Cys"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DOMAIN 88..128
FT /note="TNFR-Cys"
FT /evidence="ECO:0000259|PROSITE:PS50050"
FT DOMAIN 129..169
FT /note="TNFR-Cys"
FT /evidence="ECO:0000259|PROSITE:PS50050"
FT REPEAT 129..169
FT /note="TNFR-Cys"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT REGION 934..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 89..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DISULFID 107..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DISULFID 110..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DISULFID 130..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DISULFID 148..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DISULFID 151..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 1029 AA; 116587 MW; 3F22DE7A7BD62D48 CRC64;
MGRNWLTIRG RGGSAGVTPG TIGKPLKAGE PIITIAMSTN KQNQQFPGPR SCSDDEYMDV
GLCCKKCPAG YYVEEPCRRP HTQGKCVPCD QGTFTAFSNG LNSCLLCDTC HDDQEMVGEC
SQTRNRKCQC KAGYFYQYPE SSESCMPCDK CPEGIPVLWE CNATSNIACG VADPRNANES
ENTTGVPGFQ RYTSPRAGTS PNSINIATDY RSILSISDEA ARVQALNQHL STRSYVQGYS
LSQADMDVFR QLSTPPADSR LFHVARWFRH IEALLGGPRD KGEPCGLQAS KGRRVQPQWS
PPAGTEPCKL RLYNSLTRNK DVFIPQDGKK VTWYCCGPTV YDASHMGHAR SYISFDILRR
VLKDYFQYDI FYCMNITDID DKIIRRARQN YLFEQYRNQK PLATQLLEDV HAALKPFTVK
LHETTDPDKR QMLERIQHAV ELATEPLERA VHASLVREEV DSLAQVLMEE AKDLLSDWLD
STCGSEVTDN SIFSKLPKFW EEEFHKDMEA LNVLPPDVLT RVSEYVPEIV DFVQKIVDNG
YGYVSNGSVY FDTVKFAASE KHSYGKLVPE AVGDQKALQE GEGDLSISAD RLSEKHSPND
FALWKTSKPG EPSWPCPWGK GRPGWHIECS AMAGTLLGAS MDIHGGGFDL RFPHHDNELA
QSEAYFENDC WVRYFLHTGH LTIAGCKMSK SLKNFITIKD ALKKHSARQL RLAFLMHSWK
DTLDYSSNTM ESALQYEKFM NEFFLNVKDI LRAPVDIAGQ FEKWEDEEAE LNKNFYDKKM
AVHKALCDNV DTRTVMEEMR ALVSQCNLYM AARKAVRRRP NRALLESIAL YLTHMLKIFG
AIKEESSLGF PVGGPGTSLN LESTVMPYLQ VLSEFREGVR KIAREKKVPE VLQLSDTLRD
DILPELGVRF EDHEGLPTVV KLVDKDTLLK EREEKKRVEE EKRRKKEEAA RRKQEQEAAK
LAKMKIPPSE MFLSESDKYS KFDENGLPTH DTEGKELSKG QAKKLRKLFE AQEKLHKDYL
QMVQNGSLQ
//
