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Database: UniProt
Entry: B6QFU7_TALMQ
LinkDB: B6QFU7_TALMQ
Original site: B6QFU7_TALMQ 
ID   B6QFU7_TALMQ            Unreviewed;       798 AA.
AC   B6QFU7;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=PMAA_083370 {ECO:0000313|EMBL:EEA24332.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA24332.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; DS995901; EEA24332.1; -; Genomic_DNA.
DR   RefSeq; XP_002147843.1; XM_002147807.1.
DR   AlphaFoldDB; B6QFU7; -.
DR   STRING; 441960.B6QFU7; -.
DR   VEuPathDB; FungiDB:PMAA_083370; -.
DR   HOGENOM; CLU_013528_3_1_1; -.
DR   OrthoDB; 2140072at2759; -.
DR   PhylomeDB; B6QFU7; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR015273; Cys-tRNA-synt_Ia_DALR.
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; PF09190; DALR_2; 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   ECO:0000313|EMBL:EEA24332.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001294};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          44..477
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   DOMAIN          521..576
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|Pfam:PF09190"
FT   COILED          706..739
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   798 AA;  89793 MW;  4B86541DAE945661 CRC64;
     MATARQQPAW QQPAVSPDAK LPSLKIYNSL TKTKVPFVPV DPNGRKVTWY ACGPTVYDDS
     HLGHARNYVT TDIIRRILRD YFKFDVHFVM NITDVDDKII LRGRQQYLFN KFVSAHPTID
     ATVLDTAKAA YKAYLTKNLR LLDPELPPSK YQAEVEKVYA TVLNGGPLPG NEKPGDDEAK
     TKMHIKTLAS AAKAIAEAEI APPALSETFY TDAQDVFLPY LDQLEGSKID ASDYSIFTKL
     TRKYEERFMR DLRDLNVLDP DELTRVTEYG PQIAQFVERI VENKFAYVTS DGSVYFDIKA
     FEDAGFPYAR LEPWSRSDGK LVAEGEGALT SKTTEKHSPS DFALWKASKP GEPSWSSQWG
     KGRPGWHIEC SAMASDRLGK SIDIHSGGID LAFPHHDNEL AQSEAYWNTH THDQWINYFL
     HMGHLSIQGS KMSKSLKNFT TIREALERKD WTSRSLRIVF LLGNWNSGIE ITEDVINFGN
     SWEDKLNNFF LKMKDLDLLK KSSSGTDQSL GEALEATKAA VNEHLSDSFN TPAAMAAISD
     LVTKFNSADK ATVNPEHVEQ MGKWVTSMVN IFGLNGAAPP DASEIGWSGI DVPEEAKPYL
     YPLSALRDSL REKALSKEGI SVADIKNIIT SQEDSEAPVS ESAKPYAKVL SDFKDTVSAL
     EKPDTIGKEI LGLCDRLRDI DLFDLGIYLE DRENLPALVR PVTKELLQLR EEKAAKLRQK
     QLEKEKREKE AREKAEKGRL SHLDMFRTNE YSAWDDEGVP TRDAAGEEIT KSRAKKLKKD
     WERQKKLHEA WLVANGAK
//
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