NCSA_HALVD
ID NCSA_HALVD Reviewed; 321 AA.
AC D4GSH6; A0A384KU00; L9UMR4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=tRNA 2-thiolation protein NcsA {ECO:0000303|PubMed:24906001};
DE AltName: Full=N-type ATP pyrophosphatase superfamily protein {ECO:0000312|EMBL:ELY26159.1};
DE AltName: Full=tRNA adenylyltransferase NcsA {ECO:0000305};
DE EC=2.7.7.- {ECO:0000305|PubMed:24906001};
GN Name=ncsA {ECO:0000303|PubMed:24906001, ECO:0000312|EMBL:ADE04813.1};
GN Synonyms=tuc1 {ECO:0000312|EMBL:ADE04813.1};
GN OrderedLocusNames=HVO_0580 {ECO:0000312|EMBL:ADE04813.1};
GN ORFNames=C498_15825 {ECO:0000312|EMBL:ELY26159.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000312|EMBL:ADE04813.1};
RN [1] {ECO:0000312|EMBL:ADE04813.1, ECO:0000312|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000312|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2] {ECO:0000312|EMBL:ELY26159.1, ECO:0000312|Proteomes:UP000011532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000312|Proteomes:UP000011532};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, PATHWAY, INTERACTION WITH CPSF1; EF-1-ALPHA; PAN1; SAMP2 AND
RP UBAA, SAMPYLATION AT LYS-204, DISRUPTION PHENOTYPE, AND PHYLOGENETIC
RP ANALYSIS.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:24906001};
RX PubMed=24906001; DOI=10.1371/journal.pone.0099104;
RA Chavarria N.E., Hwang S., Cao S., Fu X., Holman M., Elbanna D.,
RA Rodriguez S., Arrington D., Englert M., Uthandi S., Soell D.,
RA Maupin-Furlow J.A.;
RT "Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is
RT associated with ubiquitin-proteasome, translation, and RNA processing
RT system homologs.";
RL PLoS ONE 9:e99104-e99104(2014).
CC -!- FUNCTION: Required for thiolation of mcm(5)S(2)U at the wobble uridine
CC position of tRNA specific for lysine (tRNA(Lys)). Probably acts by
CC catalyzing adenylation of tRNA, an intermediate required for 2-
CC thiolation. May also act as a sulfurtransferase that transfers sulfur
CC from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble
CC position. Required for cell growth at elevated temperatures.
CC {ECO:0000269|PubMed:24906001}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000269|PubMed:24906001}.
CC -!- SUBUNIT: Interacts with monomeric and polymeric forms of SAMP2.
CC Interacts with UbaA. Interacts with archaeal EF-1-alpha and Pan1. Non-
CC sampylated protein forms a complex with archaeal CPSF1 of approximately
CC 100 kDa. {ECO:0000269|PubMed:24906001}.
CC -!- PTM: Sampylated at Lys-204 with the archaeal ubiquitin-like protein
CC SAMP2. Polymeric chains of SAMP2 are also linked.
CC {ECO:0000269|PubMed:24906001}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are nonthiolated at the
CC wobble uridine position of tRNA(Lys). No effect on cell growth or yield
CC at 42 degrees Celsius. Transferring the cells grown at 42 degrees
CC Celsius to 50 degrees Celsius results in a slow-growth phenotype.
CC {ECO:0000269|PubMed:24906001}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001956; ADE04813.1; -; Genomic_DNA.
DR EMBL; AOHU01000098; ELY26159.1; -; Genomic_DNA.
DR RefSeq; WP_004044353.1; NZ_AOHU01000098.1.
DR STRING; 309800.C498_15825; -.
DR EnsemblBacteria; ADE04813; ADE04813; HVO_0580.
DR EnsemblBacteria; ELY26159; ELY26159; C498_15825.
DR GeneID; 8925285; -.
DR KEGG; hvo:HVO_0580; -.
DR PATRIC; fig|309800.29.peg.3060; -.
DR eggNOG; arCOG00042; Archaea.
DR HOGENOM; CLU_026481_1_1_2; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 57500at2157; -.
DR BioCyc; MetaCyc:MON-20244; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; IMP:UniProtKB.
DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IMP:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IMP:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IMP:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
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 Pfam; PF01171; ATP_bind_3; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR TIGRFAMs; TIGR00269; TIGR00269; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Reference proteome; Transferase; tRNA processing;
KW Ubl conjugation.
FT CHAIN 1..321
FT /note="tRNA 2-thiolation protein NcsA"
FT /id="PRO_0000454896"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SAMP2)"
FT /evidence="ECO:0000269|PubMed:24906001"
SQ SEQUENCE 321 AA; 36158 MW; 5EA09822D5D04F46 CRC64;
MECDKCGRDA VMHAAYSGAH LCDDHFCASV EKRVRRRIRE DNMLPRDASP ENPQTWVIGL
SGGKDSVVLT HILDDTFGRD PRIELVALTI HEGIEGYRDK SVDACVELAE DLDIHHELVT
YEDEFGVQMD DVVEKDPENM AACAYCGVFR RDLLERFADE LGADKLLTGH NLDDEAQTAL
MNFFEGDLKQ VAKHFDASIG DFEKRRDAGE FIPRAKPLRD VPEKEVALYA HLKDLPAHIT
ECPHSSEAYR GEIQQLLLKL EENHPGTRHS IMAGYEELAE LTAREYRGEG RVDLNDCERC
GSKTAGDVCR KCRLIESIEA V
