Y241_ARCFU
ID Y241_ARCFU Reviewed; 139 AA.
AC O29998;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=S-adenosyl-L-methionine-binding protein AF_0241;
GN OrderedLocusNames=AF_0241;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=17588214; DOI=10.1007/s10969-007-9018-3;
RA Forouhar F., Kuzin A., Seetharaman J., Lee I., Zhou W., Abashidze M.,
RA Chen Y., Yong W., Janjua H., Fang Y., Wang D., Cunningham K., Xiao R.,
RA Acton T.B., Pichersky E., Klessig D.F., Porter C.W., Montelione G.T.,
RA Tong L.;
RT "Functional insights from structural genomics.";
RL J. Struct. Funct. Genomics 8:37-44(2007).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17588214}.
CC -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC {ECO:0000305}.
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DR EMBL; AE000782; AAB90992.1; -; Genomic_DNA.
DR PIR; A69280; A69280.
DR RefSeq; WP_010877752.1; NC_000917.1.
DR PDB; 2NV4; X-ray; 2.20 A; A/B=1-139.
DR PDBsum; 2NV4; -.
DR AlphaFoldDB; O29998; -.
DR SMR; O29998; -.
DR STRING; 224325.AF_0241; -.
DR EnsemblBacteria; AAB90992; AAB90992; AF_0241.
DR GeneID; 24793773; -.
DR KEGG; afu:AF_0241; -.
DR eggNOG; arCOG00761; Archaea.
DR HOGENOM; CLU_013458_2_0_2; -.
DR OMA; QIQYFAR; -.
DR OrthoDB; 117039at2157; -.
DR PhylomeDB; O29998; -.
DR EvolutionaryTrace; O29998; -.
DR Proteomes; UP000002199; Chromosome.
DR CDD; cd09281; UPF0066; 1.
DR Gene3D; 2.40.30.70; -; 1.
DR InterPro; IPR023370; TrmO-like_N.
DR InterPro; IPR023368; UPF0066_cons_site.
DR InterPro; IPR040372; YaeB-like.
DR InterPro; IPR036413; YaeB-like_sf.
DR InterPro; IPR036414; YaeB_N_sf.
DR PANTHER; PTHR12818; PTHR12818; 1.
DR Pfam; PF01980; TrmO; 1.
DR SUPFAM; SSF118196; SSF118196; 1.
DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1.
DR PROSITE; PS01318; TSAA_1; 1.
DR PROSITE; PS51668; TSAA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..139
FT /note="S-adenosyl-L-methionine-binding protein AF_0241"
FT /id="PRO_0000155620"
FT DOMAIN 3..133
FT /note="TsaA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT BINDING 16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT BINDING 20..22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT BINDING 58..59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT BINDING 113..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17588214,
FT ECO:0007744|PDB:2NV4"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:2NV4"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2NV4"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2NV4"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2NV4"
SQ SEQUENCE 139 AA; 15809 MW; A4EF98224A1FA841 CRC64;
MILKPIGVVK SPFKTQNDAP RQGRFSDAVS EIAIFDEYAD GLHKIENLRH IIVLYWMDKA
SRDKLRVVPP GETEERGVFT TRSPSRPNPI GLCVVEILEV ERNRLKVRWL DALDGSPVID
IKKYSPEIDC VNQLEGQQP
