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Database: UniProt
Entry: A0A218WEY5_PUNGR
LinkDB: A0A218WEY5_PUNGR
Original site: A0A218WEY5_PUNGR 
ID   A0A218WEY5_PUNGR        Unreviewed;       358 AA.
AC   A0A218WEY5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   Name=NCS6 {ECO:0000256|HAMAP-Rule:MF_03053};
GN   Synonyms=CTU1 {ECO:0000256|HAMAP-Rule:MF_03053};
GN   ORFNames=CDL15_Pgr014295 {ECO:0000313|EMBL:OWM70622.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM70622.1, ECO:0000313|Proteomes:UP000197138};
RN   [1] {ECO:0000313|Proteomes:UP000197138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX   PubMed=28654223; DOI=10.1111/tpj.13625;
RA   Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA   Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT   "The pomegranate (Punica granatum L.) genome and the genomics of
RT   punicalagin biosynthesis.";
RL   Plant J. 91:1108-1128(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWM70622.1}.
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DR   EMBL; MTKT01004609; OWM70622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218WEY5; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000197138; 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   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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
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          91..224
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          293..323
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16503"
FT   REGION          324..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  40460 MW;  94134F629F4B2C3B CRC64;
     MEETAAKPRR SGGGGRQCCI CHERRPALKR PKTLEQIATF LLRLHEKSCC INRSTEMLAL
     KICRECFYAV FEEEIHQVIV ENQLFKPGER IGIGASGGKD STVLAYVLSE LNKRHNYGLD
     LFLLSVDEGI TGYRDDSLET VKRNEVQYGL PLKIVSYKDL YGWTMDEIVK MIGLKNNCTF
     CGVFRRQALD RGAALLKVDK LATGHNADDI AETVLLNILR GDIASLNHVF TYAYFKKLDY
     FSTECIYSPN AYRGFAREFI KDLERIRPRA ILDIIKSGED FRIATSTKMP EQGTCERCGY
     ISSQKWCKAC VLLEGLNRGM PKLGIGRSRG LNSNQMKTDK PTSRTKSIES KQCGSLDF
//
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