ID A0A0D6KU52_9CYAN Unreviewed; 334 AA.
AC A0A0D6KU52;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Methyltransferase domain protein {ECO:0000313|EMBL:EKF03282.1};
GN ORFNames=FDUTEX481_02741 {ECO:0000313|EMBL:EKF03282.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF03282.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF03282.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. gTMT family. {ECO:0000256|PROSITE-ProRule:PRU00914}.
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:EKF03282.1}.
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DR EMBL; AGCR01000024; EKF03282.1; -; Genomic_DNA.
DR RefSeq; WP_045869388.1; NZ_JH930358.1.
DR AlphaFoldDB; A0A0D6KU52; -.
DR STRING; 1188.FDUTEX481_02741; -.
DR PATRIC; fig|1188.3.peg.2762; -.
DR HOGENOM; CLU_039068_7_0_3; -.
DR OrthoDB; 9769602at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025774; MTs_g-TMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44068:SF11; GERANYL DIPHOSPHATE 2-C-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR44068; ZGC:194242; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51581; SAM_GTMT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:EKF03282.1};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00914};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:EKF03282.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..193
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REGION 97..106
FT /note="SAM motif I"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 157..165
FT /note="SAM motif II"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 184..193
FT /note="SAM motif III"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
SQ SEQUENCE 334 AA; 37116 MW; 1693B3DE9CD1BC3F CRC64;
MSTLLVYFVI GSLIVLLIGI AAYFVTARKY QSSATVANSY DQWTLDGILE FYWGEHIHLG
HYGSPPRRKD FLAAKSDFVH EMVKWGGLDK LPPGTTVLDV GCGIGGSSRI LARDYGFAVT
GITISPQQVK RAQELTPQEL NAQFAVDDAM ALSFPDASFD VVWSIEAGPH MPDKAVFARE
LIRVLKPGGI LVVADWNQRD DRQKPLNFWE KPVMRQLLDQ WSHPAFSSIE GFSELLAATG
LVEGEVITAD WTQATLPSWL DSIWQGVVRP SGFLRFGLSG FIKSVREVPT FLLMRLAFGA
GLCRFGMFRA VRANSRTELR DRNFVQENPS SLVG
//
