ID B2UN25_AKKM8 Unreviewed; 433 AA.
AC B2UN25;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=PUA domain containing protein {ECO:0000313|EMBL:ACD05636.1};
GN OrderedLocusNames=Amuc_1818 {ECO:0000313|EMBL:ACD05636.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05636.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC {ECO:0000256|ARBA:ARBA00038091}.
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DR EMBL; CP001071; ACD05636.1; -; Genomic_DNA.
DR RefSeq; WP_012420850.1; NZ_CP071807.1.
DR AlphaFoldDB; B2UN25; -.
DR STRING; 349741.Amuc_1818; -.
DR PaxDb; 349741-Amuc_1818; -.
DR KEGG; amu:Amuc_1818; -.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_0_2_0; -.
DR OrthoDB; 9805492at2; -.
DR BioCyc; AMUC349741:G1GBX-1937-MONOMER; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 52..105
FT /note="RlmI-like PUA"
FT /evidence="ECO:0000259|Pfam:PF17785"
FT DOMAIN 222..382
FT /note="S-adenosylmethionine-dependent methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF10672"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 48543 MW; A5ADD175F691B815 CRC64;
MNDFHNSRDS RPRPVYRDRR SQPGRPRTAP KKNLFANKSP EGSEQWLKPW VELKYFTYNP
AVFPRMLGSV SGEIAPGSLV NVYDKNGELF GAGFWNESSR TPLRMVYHGK DVFAERDLDA
ALERAVKLRR EVLRLDETTN AYRVLHGDSD GLGGLVVDRY ADVLSLEVST LAVWQRLNRW
LPLLHRLCGT KRHVVQVDEG IARMEGIRAE EAPASPAPVR LVKIVENGIT YEVDFAQGHK
TGFFCDQRDN RLKFASLVKG ATVLDLCCYS GGFSIAAKML GGAAEVTAVD LDEKAVAMAK
RNGNINRQRI DFVHADAFVY ARQMVRNGRL FDAVLLDPPK FIVGRDGYEE GIKKYHDLNM
LGLQCVRPGG LFVTCSCSGL LSPAEFEHTV IKAAQRQGRK LQIMAMTGPG WDHPFLSTYP
EGRYLKVLWA IAL
//
