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Database: UniProt
Entry: C7M8W0_CAPOD
LinkDB: C7M8W0_CAPOD
Original site: C7M8W0_CAPOD 
ID   C7M8W0_CAPOD            Unreviewed;       397 AA.
AC   C7M8W0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
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   OrderedLocusNames=Coch_1944 {ECO:0000313|EMBL:ACU93489.1};
OS   Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / NCTC
OS   12371 / VPI 2845) (Bacteroides ochraceus).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU93489.1, ECO:0000313|Proteomes:UP000006650};
RN   [1] {ECO:0000313|EMBL:ACU93489.1, ECO:0000313|Proteomes:UP000006650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC   {ECO:0000313|Proteomes:UP000006650};
RX   PubMed=21304645; DOI=10.4056/sigs.15195;
RA   Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA   Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT   2845).";
RL   Stand. Genomic Sci. 1:101-109(2009).
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}.
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DR   EMBL; CP001632; ACU93489.1; -; Genomic_DNA.
DR   RefSeq; WP_015782956.1; NC_013162.1.
DR   AlphaFoldDB; C7M8W0; -.
DR   STRING; 521097.Coch_1944; -.
DR   GeneID; 29675983; -.
DR   KEGG; coc:Coch_1944; -.
DR   eggNOG; COG0482; Bacteria.
DR   HOGENOM; CLU_035188_1_0_10; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000006650; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; 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:0032259; P:methylation; 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; Adenine nucleotide alpha hydrolases-like domains; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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   NCBIfam; TIGR00420; trmU; 1.
DR   PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR   PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR   Pfam; PF03054; tRNA_Me_trans; 1.
DR   Pfam; PF20258; tRNA_Me_trans_C; 1.
DR   Pfam; PF20259; tRNA_Me_trans_M; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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   Methyltransferase {ECO:0000313|EMBL:ACU93489.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00144}; Reference proteome {ECO:0000313|Proteomes:UP000006650};
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          254..306
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          326..396
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
FT   REGION          95..97
FT                   /note="Interaction with target base in tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   REGION          150..152
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   REGION          348..349
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        200
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            125
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            380
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   397 AA;  45335 MW;  5D0D3F69A38EBAFA CRC64;
     MKRVVVGLSG GVDSSVAAYL LKEQGYEVIG LFMKNWHDDS VTISDECPWL EDSNDALLVA
     EKLGIPFQTV DMSEPYKARI VDYMFNEYEH GRTPNPDVLC NREIKFDVFM KLALSLGADY
     VATGHYCRKE EIEIKGGKIY RLLSGKDENK DQSYFLCQLS QDQLSKALFP VGELQKSEVR
     AIAKAQDLIT ADKKDSQGLC FVGKVRLPEF LQQKLQPKQG DIIEIPNDWK GYTDFDMPRT
     FETYEDELEY LSQRFVYQPE NGKKVGIHQG AHYFTKGQRK GLNVGGTKEP LFIIETDIEK
     NIIYTGQGHT HRGLFRSALF IATPDEHWIR EDLALKIYES KEFMVRIRYR QPLQKAVLYK
     VENGLYIHFS EPQSAITEGQ FAAWYSGDEL VGSGVIS
//
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