ID A0AAE0ZBW8_9GAST Unreviewed; 480 AA.
AC A0AAE0ZBW8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=RRG08_026318 {ECO:0000313|EMBL:KAK3765851.1};
OS Elysia crispata (lettuce slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=231223 {ECO:0000313|EMBL:KAK3765851.1, ECO:0000313|Proteomes:UP001283361};
RN [1] {ECO:0000313|EMBL:KAK3765851.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ECLA1 {ECO:0000313|EMBL:KAK3765851.1};
RX PubMed=37816307;
RA Eastman K.E., Pendleton A.L., Shaikh M.A., Suttiyut T., Ogas R., Tomko P.,
RA Gavelis G., Widhalm J.R., Wisecaver J.H.;
RT "A reference genome for the long-term kleptoplast-retaining sea slug Elysia
RT crispata morphotype clarki.";
RL G3 (Bethesda) 0:0-0(2023).
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 NCS6/CTU1 that ligates sulfur from
CC thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03054}.
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:KAK3765851.1}.
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; JAWDGP010004277; KAK3765851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE0ZBW8; -.
DR Proteomes; UP001283361; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:TreeGrafter.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:TreeGrafter.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_03054; CTU2; 1.
DR InterPro; IPR019407; CTU2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR20882; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR PANTHER; PTHR20882:SF14; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR Pfam; PF10288; CTU2; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP001283361};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 52713 MW; 8AFEB804F17AB098 CRC64;
MCNVEDQERN GSENLPVSSS GKSLTGSGCV KCGEPGVLVT RIHDSFCKSC FQVYVVHKFR
SAIGKSKLIR DGETVLVAFS GGGNSSALLH LIQDGLSLRA HKRLRFTPTL LHIDESCISG
VRSDELRQKR EKIRQIMIKS GFPSYWTQLE QSLNIYPELS SKSMSKSKSS ENPASPNSLW
LTDLGQEPAP NQVPDDPPLE ESRKLQDLIK SFKSSTAQED FIHNLRNQLL VAAAQQLGFS
KILTAESSTR LAVHILSDIA QGRGSQVSLD TGISDERNPG VMFMRPVREL NAKELAMYNS
LFGVDTVFMP TLTTKTSIAS SIERLTETFV TGLQADYPST VSNIVRTSGK LGGPDVKRTD
KCSFCQSPLD TDVGKTSALG AVLFSQHMSR PKMVDPKDNK ERVSDGPVYS NGTHTPIASM
PNLKEALCYG CRLSLHEFDG DTSMLPTLIT KRAMWSIQER QKDELSGYLL EEDVEVNGVG
//
