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Database: UniProt
Entry: B9H5A1_POPTR
LinkDB: B9H5A1_POPTR
Original site: B9H5A1_POPTR 
ID   B9H5A1_POPTR            Unreviewed;       353 AA.
AC   B9H5A1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 2.
DT   27-MAR-2024, entry version 84.
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=POPTR_005G083500 {ECO:0000313|EMBL:RQO90253.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:RQO90253.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:RQO90253.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC   Nisqually-1 {ECO:0000313|EMBL:RQO90253.1};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
RN   [2] {ECO:0000313|EMBL:RQO90253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nisqually-1 {ECO:0000313|EMBL:RQO90253.1};
RA   Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA   Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA   Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA   Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA   Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA   Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA   Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA   Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA   Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA   Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA   Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA   Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA   Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA   Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA   Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA   Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA   Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA   Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA   Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT   "WGS assembly of Populus trichocarpa.";
RL   Submitted (JUL-2017) 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; CM009294; PNT35600.1; -; Genomic_DNA.
DR   EMBL; CM009294; RQO90253.1; -; Genomic_DNA.
DR   RefSeq; XP_002307125.2; XM_002307089.2.
DR   RefSeq; XP_006382926.1; XM_006382864.1.
DR   AlphaFoldDB; B9H5A1; -.
DR   STRING; 3694.B9H5A1; -.
DR   EnsemblPlants; Potri.005G083500.2.v4.1; Potri.005G083500.2.v4.1; Potri.005G083500.v4.1.
DR   Gramene; Potri.005G083500.2.v4.1; Potri.005G083500.2.v4.1; Potri.005G083500.v4.1.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; B9H5A1; -.
DR   OMA; KPVRGIC; -.
DR   OrthoDB; 5483984at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000006729; Chromosome 5.
DR   ExpressionAtlas; B9H5A1; baseline and differential.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
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; IPR035107; tRNA_thiolation_TtcA_Ctu1.
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   PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006729};
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          61..245
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          288..318
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16503"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
SQ   SEQUENCE   353 AA;  40196 MW;  450F29F0451F12FE CRC64;
     MAENHKKAAG RLCYLCNQRR AALKRPKTLE QICRECFYEV FEEEIHQVIV KNQLFKPGER
     IAIGASGGKD STVLAYVLSE LNRRHNYGLD LFLLSVDEGI TGYRDDSLET VKRNEIQYGL
     PLKIVSYKDL YGWTMDEIVK MIGLKNNCTF CGVFRRQALD RGAALLKVDK LVTGHNADDI
     AETVLLNILR GDIARLSRCT SITTGEDGPI PRCKPFKYTY EKEIVMYAYF KRLDYFSTEC
     IYSPNAYRGF AREFIKDLER MRPRAILDII KSGEDFRIST STKMPEQGTC ERCGYISSQK
     WCKACVLLEG LNKGLPKLGI GRSRGLDNNH RKDVKQSNGT KNIEGKQCGS LDF
//
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