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Database: UniProt
Entry: M0A6N8_9EURY
LinkDB: M0A6N8_9EURY
Original site: M0A6N8_9EURY 
ID   M0A6N8_9EURY            Unreviewed;       606 AA.
AC   M0A6N8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=tRNA-guanine transglycosylase {ECO:0000313|EMBL:ELY93542.1};
GN   ORFNames=C482_19129 {ECO:0000313|EMBL:ELY93542.1};
OS   Natrialba chahannaoensis JCM 10990.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=1227492 {ECO:0000313|EMBL:ELY93542.1, ECO:0000313|Proteomes:UP000011693};
RN   [1] {ECO:0000313|EMBL:ELY93542.1, ECO:0000313|Proteomes:UP000011693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10990 {ECO:0000313|EMBL:ELY93542.1,
RC   ECO:0000313|Proteomes:UP000011693};
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).
CC   -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005030}.
CC   -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008906}.
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:ELY93542.1}.
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DR   EMBL; AOIN01000098; ELY93542.1; -; Genomic_DNA.
DR   RefSeq; WP_006169353.1; NZ_AOIN01000098.1.
DR   AlphaFoldDB; M0A6N8; -.
DR   STRING; 1227492.C482_19129; -.
DR   PATRIC; fig|1227492.4.peg.3800; -.
DR   OrthoDB; 115061at2157; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000011693; Unassembled WGS sequence.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   CDD; cd21149; PUA_archaeosine_TGT; 1.
DR   Gene3D; 3.10.450.90; ArcTGT, C2 domain; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR   Gene3D; 3.40.50.10630; Uracil-DNA glycosylase-like; 1.
DR   InterPro; IPR040777; DUF5591.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR029402; TGT_C2.
DR   InterPro; IPR038250; TGT_C2_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   InterPro; IPR004521; Uncharacterised_CHP00451.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   NCBIfam; NF040592; tRNA_mod_ArcS; 1.
DR   NCBIfam; TIGR00451; unchar_dom_2; 1.
DR   PANTHER; PTHR46499:SF2; ARCHAEOSINE SYNTHASE; 1.
DR   PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR   Pfam; PF17884; DUF5591; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF01702; TGT; 1.
DR   Pfam; PF14810; TGT_C2; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF88802; Pre-PUA domain; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          538..605
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   REGION          27..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67604 MW;  DB9A00BECDBF9103 CRC64;
     MTEYFEVHER DGAARVGELR LDFEAVAGDA DSDTDSNPGS APDRTPPQTT PALVDDVLED
     AGSLWSAERE FPEGDDSALT VLPHRSFPGG TADEVQDSFA VDYPDVEFPS VAVISSDHVD
     DHGTDAYAVS DVQSFTGHGA GLVEAVVNVR EEIPTDTALF FSGVATPRNV ALLAYAGVDL
     FDRTAAIVKG TEGRYLTTDE AYFLEDLEEL PCSCPACQQP REAFTREDCV DHNVNALEAE
     LGIVRRRIRD GRLRDYVEGQ ARQDQWLTAA MRELDSQWGY LAERTPILRD AQIDAATEDT
     LRRVEIQRYA DRVTTRYQNR FKNPLVLVPC SAAKPYSESQ SHRQFHDAIQ WRAHLVSMTS
     PIGVVPQELE TTYPAQHYDT VVTGRWSEDE KQFVSEVLRR YLERNEYPKI IAHVPNEGYR
     DIVGRVEEEL DLDITYTVNE HPTDDESLAN LSEALSGELK YSKREREHNT VRAIADYLLG
     DGAGDDLFED IQTTSRYPKI QVRDREDTQL ATMVPQYGTL SFTLAGARRW VDSDAPVKRV
     EIDGFVPHGS VLAPGVVEAD EEIRVGDEVV VEGPKAFGVG RAEMFGREMA ESTRGIAAEI
     RHVEEK
//
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