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Database: UniProt
Entry: A0A395HF41_9EURO
LinkDB: A0A395HF41_9EURO
Original site: A0A395HF41_9EURO 
ID   A0A395HF41_9EURO        Unreviewed;       543 AA.
AC   A0A395HF41;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:RAL06073.1};
GN   ORFNames=BO80DRAFT_460328 {ECO:0000313|EMBL:RAL06073.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL06073.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL06073.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL06073.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ824419; RAL06073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HF41; -.
DR   STRING; 1448316.A0A395HF41; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_460328; -.
DR   OrthoDB; 5489391at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF037959; MFS_SpdSyn; 1.
DR   PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000313|EMBL:RAL06073.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW   Transferase {ECO:0000313|EMBL:RAL06073.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   543 AA;  60132 MW;  B2808BD2EE0E7914 CRC64;
     MFSLAGLLQQ PTTRQLLAGT ALLFLTAFYS PLTVLMLTPV YGSAPAHIFH PYGLALIGAA
     GWFLKDQIQR LTGRQALYLV PVIAFWVPTV QSFLFASSSV LGNPFGAVVT EVISYYPLVL
     LSVACAGKLV QAGLDLGRHG EAVVEHVPLV VTYVIYKTGE KFAKLFLAKF IGTTFFFSRA
     GLQLLLPALY SAIAPSKLLL LAIPSLLFSM TSNVHMNSGA LNSYLNDEGF DLLARQDSST
     GYISVLDNLG DGFRVMRCDH SLLGGQWTKM PQNYNPAVMD PIYSVFTMLE AVRLIETDHG
     EPRVDANSKA LVIGLGVGTT PSALIHHGIE TTIVEIDPVV HKFATEYFHL PSNHIAVIED
     ATTFVKRTPP AQYDYIVHDV FTGGAEPLEL FTLEFLENLG ALLKDDGVIA INYAGDISLY
     PAALTVRTIQ HVFPTCRIFR EASDSDLTTD FTNMVIFCKK SAATPLTFRN PVPADFMGSK
     FRQTYLVPKQ EIDISRFEPI EKGGRRFLLS KETHLLHKYQ DRAALEHWNI MRHVLPDLVW
     ENW
//
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