ID A0A0L7K677_PLAFX Unreviewed; 483 AA.
AC A0A0L7K677;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000256|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_03053};
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000256|HAMAP-Rule:MF_03053};
GN ORFNames=PFHG_00545 {ECO:0000313|EMBL:KOB58797.1};
OS Plasmodium falciparum (isolate HB3).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=137071 {ECO:0000313|EMBL:KOB58797.1, ECO:0000313|Proteomes:UP000054289};
RN [1] {ECO:0000313|EMBL:KOB58797.1, ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB3 {ECO:0000313|EMBL:KOB58797.1};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Kodira C., Zeng Q., Oleary S., Yandava C., Alvarado L., Wirth D.,
RA Volkman S., Hartl D.;
RT "The genome sequence of the Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC intermediate required for 2-thiolation. It is unclear whether it acts
CC as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC onto the uridine of tRNAs at wobble position. {ECO:0000256|HAMAP-
CC Rule:MF_03053}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03053}.
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DR EMBL; CH671925; KOB58797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7K677; -.
DR EnsemblProtists; KOB58797; KOB58797; PFHG_00545.
DR VEuPathDB; PlasmoDB:PfHB3_060016900; -.
DR OMA; ECTRGED; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR CDD; cd01993; Alpha_ANH_like_II; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_03053; CTU1; 1.
DR InterPro; IPR032442; CTU1_C.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR020554; UPF0021_CS.
DR NCBIfam; TIGR00269; TIGR00269 family protein; 1.
DR PANTHER; PTHR11807; ATPASES OF THE PP SUPERFAMILY-RELATED; 1.
DR PANTHER; PTHR11807:SF12; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 1; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
KW Reference proteome {ECO:0000313|Proteomes:UP000054289};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03053};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03053}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03053};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_03053}.
FT DOMAIN 50..194
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT DOMAIN 431..454
FT /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16503"
FT REGION 233..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 56069 MW; 0EC09EDBBFEF841C CRC64;
MLCEKCNEKN VCMMRPSNKE KLCKECFIES FEEDVHDTIL KKRMFEDNDK ICIAVSGGKD
SSVLAHVLVN LKKKYNYNWE LFLLAIDEGI KGYRDDSLKV VYKLEKLYNL PLKILKFENL
FSYTMDDVVK FIGKKNNCTV CGVFRRQSFE KGALLFNATK LVTGHNADDL AETILMNMCR
GDIDKLAKNI NDLSNADHMN KKYNCTGDSQ NGIKNLENVQ NGPEQVRQKK YKNYENVDNN
DNNDNNDNYD NNDNYDDIIL NDIMSERLNE KCSCINNNLN NDGGKKNKEM QKCEQDYEEK
YNNDNNNNND NNNDNNNDNN NDNNNNNNNN DNNNNNNNNN SNNNNNNNSF FLPRLKPLMW
CYEKEIVLYA FHLKLDYFST ECTYSPNSFR GNLRCFIKDI ELINAQFILN IIHSAEFFYF
NSINQKTLNV CIKCGAYTSN KICKACLIID GLNNYTDNSF LYSNKKKAKK KISIHFDNKK
VEG
//
