ID   CTU2B_XENLA             Reviewed;         512 AA.
AC   Q32NV1; Q6NRJ8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2-B {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ctu2-b; Synonyms=ncs2-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2005) 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). May act by
CC       forming a heterodimer with ctu1/atpbd3 that ligates sulfur from
CC       thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
CC       {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH70752.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI08466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC070752; AAH70752.1; ALT_INIT; mRNA.
DR   EMBL; BC108465; AAI08466.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q32NV1; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_03054; CTU2; 1.
DR   InterPro; IPR019407; CTU2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR20882; PTHR20882; 1.
DR   Pfam; PF10288; CTU2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..512
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2-B"
FT                   /id="PRO_0000289179"
FT   REGION          196..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        18
FT                   /note="A -> G (in Ref. 1; AAH70752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="A -> P (in Ref. 1; AAH70752)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  57315 MW;  D67EDDDF40AD49BD CRC64;
     MCEEGETYCP EVKDAKQAKS LGKICMKCKE SSAALLIRAG DAFCKSCFKE YFVHKFRATL
     GKNRVIYPGE KVLLAYSGGP SSSAMVRQVQ EGLSRDAPKK LRFVPGILFI DEGTACGMSW
     EERQQILSEI CSVLQQTKIP FHIVSLEQVF SLPGSVLQRG APEQRPNYKE EVDRFLVQER
     EQGDAGCSEM LERLEVTDSD SPGSSDKMYQ STCSRPPDMH TQKLKQLFAS AKTLTAKQQL
     LHTLRSHLIL HIARTCGYSK VMTGESCTRL SIRLLSNVSL GRGAFLPLDT GFCDSRYGDV
     DIIRPMREYS SKEIAYYNRF FNVLPIFIPA LDTKASENSS IQHLTEVFVN RLQADFPSTV
     STLYRTSEKL NVSIIDADQE TCAKDRCLLC LSPLDTQAGK ASAFSATQLS HHLSQKIPMK
     SNDLANNSDK SCCQGGQGCK EAGYGDTCQS RALQTPSFVH MLCYSCRLTV KDMQSLDVLP
     QYVLHEAEYR CHRTEMRKEI QEFLLEEDDG DS