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Database: UniProt
Entry: Q2VZ09_MAGSA
LinkDB: Q2VZ09_MAGSA
Original site: Q2VZ09_MAGSA 
ID   Q2VZ09_MAGSA            Unreviewed;       820 AA.
AC   Q2VZ09;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Predicted SAM-dependent methyltransferase {ECO:0000313|EMBL:BAE53166.1};
GN   OrderedLocusNames=amb4362 {ECO:0000313|EMBL:BAE53166.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE53166.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE53166.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE53166.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2VZ09; -.
DR   STRING; 342108.amb4362; -.
DR   KEGG; mag:amb4362; -.
DR   HOGENOM; CLU_018174_0_0_5; -.
DR   Proteomes; UP000007058; 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; cd21153; PUA_RlmI; 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   ECO:0000313|EMBL:BAE53166.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAE53166.1}.
FT   DOMAIN          434..499
FT                   /note="RlmI-like PUA"
FT                   /evidence="ECO:0000259|Pfam:PF17785"
FT   DOMAIN          600..763
FT                   /note="S-adenosylmethionine-dependent methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF10672"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  89195 MW;  D302A286C90EDFA4 CRC64;
     MRQRVHRLDR HHRTFEGRHA VERHRGDQET HDRIGPQLVP GTRQGHQAVD HAAPRGHPQH
     HREGHAQGLR PIGQSGVVQV VRTGPDVQED QRPEVHDRQT VGVHRTLGPL RHEVVHDAEE
     AGGQEEAHRI VAVPPLGHGV LHATEHVVAL HPAAAEQGGR NRDVVAEVQH GDGQDHGEEE
     PVGHIDVGFL TLHDGAGEGD QVGHPNHGEP QVDPPFRLRV FLALAEAQNI GQSGDDDQRL
     EIPENETTKA GTAEQAGTAG PLHDVQRGGE KNVTAERKDH RGSMNGTQAP ERSPLEIEVQ
     NGKGQLQGDE VARQEAHDAP ENRGDRELLD HVVAIGRGFS VDAHAELLFR PEKGPPEASG
     RIHGDTMPPG PMAAGWFFAS SVRTMPTEAR AAIDIYQSMA IFRRFRPLAI MIPRRKVPAM
     TQTHPDQPAA RPVIRLAKGR SKRLRAGHPW VFSNEIEMGA EAKALPPGSL VTLMDAGDER
     LGVATFNPHS LIAARVLSRR AADTVDVDFL AERLRAALAL RDTLFPTPHY RLVHSEADRL
     PGLIVDRYGD VLAVQTNTAG MERLLPVLLD ALQMVLAPRA VVLVNDSPVR KLEGLEPHHD
     VAFGQVDGPV ELEENGCRFV ADLTGGQKTG WFFDQRDNRA FVARLAKGRR VLDLYTYAGG
     FAVQAAKAGA TQTIAVDRSE HSLALADQAA RLNGVEVQTV RAEAFAEMER LALAGERFGL
     VVADPPAFVK SRKDLGAGAK GYRKMARLAA ALVEPGGFLL CASCSHHMPV ETFAEEIGHG
     LHLAGRSGRI LRSAGAASDH PVHPWLPESA YLKAQVFQLD
//
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