ID   A3DJ37_ACET2            Unreviewed;       465 AA.
AC   A3DJ37;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE            EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN   OrderedLocusNames=Cthe_2767 {ECO:0000313|EMBL:ABN53966.1};
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN53966.1, ECO:0000313|Proteomes:UP000002145};
RN   [1] {ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3JWG, ECO:0007829|PDB:3JWI}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 258-465 IN COMPLEX WITH MG(2+).
RX   PubMed=19822745; DOI=10.1073/pnas.0907540106;
RA   Mui Chan C., Zhou C., Brunzelle J.S., Huang R.H.;
RT   "Structural and biochemical insights into 2'-O-methylation at the 3'-
RT   terminal nucleotide of RNA by Hen1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17699-17704(2009).
RN   [3] {ECO:0007829|PDB:4DQZ, ECO:0007829|PDB:4DRF}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-230.
RX   PubMed=22847431; DOI=10.1073/pnas.1209805109;
RA   Wang P., Chan C.M., Christensen D., Zhang C., Selvadurai K., Huang R.H.;
RT   "Molecular basis of bacterial protein Hen1 activating the ligase activity
RT   of bacterial protein Pnkp for RNA repair.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:13248-13253(2012).
RN   [4] {ECO:0000313|EMBL:ABN53966.1, ECO:0000313|Proteomes:UP000002145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145};
RX   PubMed=24295562; DOI=10.1186/1754-6834-6-179;
RA   Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M.,
RA   Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H.,
RA   Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.;
RT   "Global transcriptome analysis of Clostridium thermocellum ATCC 27405
RT   during growth on dilute acid pretreated Populus and switchgrass.";
RL   Biotechnol. Biofuels 6:179-179(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC         S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC         Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.386;
CC         Evidence={ECO:0000256|ARBA:ARBA00034992};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- INTERACTION:
CC       A3DJ37; A3DJ37: Cthe_2767; NbExp=2; IntAct=EBI-16002195, EBI-16002195;
CC       A3DJ37; A3DJ38: Cthe_2768; NbExp=2; IntAct=EBI-16002195, EBI-16002232;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC       {ECO:0000256|ARBA:ARBA00009026}.
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DR   EMBL; CP000568; ABN53966.1; -; Genomic_DNA.
DR   RefSeq; WP_020457915.1; NC_009012.1.
DR   PDB; 3JWG; X-ray; 1.90 A; A=258-465.
DR   PDB; 3JWI; X-ray; 2.20 A; A/B=259-465.
DR   PDB; 4DQZ; X-ray; 2.30 A; A/B=1-230.
DR   PDB; 4DRF; X-ray; 2.60 A; B/D=1-230.
DR   PDB; 4E6N; X-ray; 2.39 A; B/D=1-230.
DR   PDBsum; 3JWG; -.
DR   PDBsum; 3JWI; -.
DR   PDBsum; 4DQZ; -.
DR   PDBsum; 4DRF; -.
DR   PDBsum; 4E6N; -.
DR   AlphaFoldDB; A3DJ37; -.
DR   SMR; A3DJ37; -.
DR   DIP; DIP-60068N; -.
DR   IntAct; A3DJ37; 1.
DR   STRING; 203119.Cthe_2767; -.
DR   KEGG; cth:Cthe_2767; -.
DR   eggNOG; COG2227; Bacteria.
DR   HOGENOM; CLU_042787_0_0_9; -.
DR   OrthoDB; 626362at2; -.
DR   EvolutionaryTrace; A3DJ37; -.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.1610.20; Hen1, N-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR024026; 3'-RNA_MeTfrase_Hen1_bac.
DR   InterPro; IPR026610; Hen1.
DR   InterPro; IPR024740; Hen1_N.
DR   InterPro; IPR038546; Hen1_N_sf.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR04074; bacter_Hen1; 1.
DR   PANTHER; PTHR21404; HEN1; 1.
DR   PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR   Pfam; PF12623; Hen1_L; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3JWG, ECO:0007829|PDB:3JWI};
KW   Metal-binding {ECO:0007829|PDB:3JWG};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ABN53966.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002145};
KW   RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..241
FT                   /note="Hen1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12623"
FT   DOMAIN          290..382
FT                   /note="Methyltransferase type 12"
FT                   /evidence="ECO:0000259|Pfam:PF08242"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3JWG"
FT   BINDING         365
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3JWG"
SQ   SEQUENCE   465 AA;  53576 MW;  6BAD46C5FAA7D220 CRC64;
     MILTITYTQP PATDLGYLLH KNPSRPQTFE LNHGKAHIFY PEATSERCTV ALLLDIDPID
     LARGKKGSSG EGGLFDYVND RPYVSSSFMS VAISRVFGTA MSGKCKEKPE LAAIKLPLKA
     KIMMLPCKGG EEIIYRLFEP LGYKVDVEGY MLDEKFPEWG KSRYYTVSLE GEVRVRDLLN
     HIYVLIPVLD SEKHYWVGED EIDKLFQHGE GWLVDHPEKE LITGRYLIRK KRLVNQALKR
     LLEASDVVDD ENEDDEPLKN EETEKKLNLN QQRLGTVVAV LKSVNAKKVI DLGCGEGNLL
     SLLLKDKSFE QITGVDVSYS VLERAKDRLK IDRLPEMQRK RISLFQSSLV YRDKRFSGYD
     AATVIEVIEH LDENRLQAFE KVLFEFTRPQ TVIVSTPNKE YNFHYQNLFE GNLRHRDHRF
     EWTRKEFETW AVKVAEKYGY SVRFLQIGEI DDEFGSPTQM GVFTL
//