ID A0A698CI91_CAMJU Unreviewed; 338 AA. AC A0A698CI91; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 14-DEC-2022, entry version 9. DE RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000256|HAMAP-Rule:MF_00144}; DE EC=2.8.1.13 {ECO:0000256|HAMAP-Rule:MF_00144}; GN Name=mnmA {ECO:0000256|HAMAP-Rule:MF_00144, GN ECO:0000313|EMBL:EDO9927493.1}; GN ORFNames=GRN34_06195 {ECO:0000313|EMBL:EDO9927493.1}; OS Campylobacter jejuni. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=197 {ECO:0000313|EMBL:EDO9927493.1}; RN [1] {ECO:0000313|EMBL:EDO9927493.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PNUSAC014473 {ECO:0000313|EMBL:EDO9927493.1}; RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance; RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S., RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position CC (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000256|HAMAP- CC Rule:MF_00144}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in CC tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L- CC cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131, CC Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170, CC ChEBI:CHEBI:456215; EC=2.8.1.13; CC Evidence={ECO:0000256|ARBA:ARBA00001042, ECO:0000256|HAMAP- CC Rule:MF_00144}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144}. CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000256|HAMAP- CC Rule:MF_00144}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00144}. 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:EDO9927493.1}. 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; AANIYN010000007; EDO9927493.1; -; Genomic_DNA. DR AlphaFoldDB; A0A698CI91; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule. DR CDD; cd01998; tRNA_Me_trans; 1. DR Gene3D; 2.30.30.280; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1. DR InterPro; IPR046885; MnmA-like_C. DR InterPro; IPR046884; MnmA-like_central. DR InterPro; IPR023382; MnmA-like_central_sf. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; tRNA-specific_2-thiouridylase. DR Pfam; PF20258; tRNA_Me_trans_C; 1. DR Pfam; PF20259; tRNA_Me_trans_M; 1. DR TIGRFAMs; TIGR00420; trmU; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00144}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00144}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00144}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00144}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00144}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00144}. FT DOMAIN 195..257 FT /note="tRNA_Me_trans_M" FT /evidence="ECO:0000259|Pfam:PF20259" FT DOMAIN 267..337 FT /note="tRNA_Me_trans_C" FT /evidence="ECO:0000259|Pfam:PF20258" FT REGION 134..136 FT /note="Interaction with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT REGION 288..289 FT /note="Interaction with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT ACT_SITE 92 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT ACT_SITE 186 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT BINDING 6..13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT BINDING 32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT SITE 117 FT /note="Interaction with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" FT SITE 321 FT /note="Interaction with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144" SQ SEQUENCE 338 AA; 38434 MW; B4464CA0BD45C675 CRC64; MKILVAMSGG VDSTITAYKL KNLGHEVIGC YMKLHGKPNY HEENIKKVEK VANFLQIPYH ILDLQEDFKN KVYMPFVDTY KEGKTPNPCA LCNRFIKLGK LLEFAKSLGC EKLATGHYAR LENNLIKTAV DESKDQSYFL ASADKEALKY LIFPLGEMKK EDVKKFASTI EVLKSFATQK ESSEICFVED TYVQVLDQFM DTKIPGEVLD SSGKVVGKHE GYMHYTIGKR RGFEVRGAHE PHFVLKINPK QNQIIVGTKE ELKISEFNLK NINLFIDAKE LDCEVKIRYR SKSTPCKVEI YEDKSAKIIL KDPVYGLASG QMAVFYDHDK VIASGFIE //