ID S7Z542_PENO1 Unreviewed; 348 AA.
AC S7Z542;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Velvet complex subunit laeA {ECO:0000256|ARBA:ARBA00041581};
GN ORFNames=PDE_00584 {ECO:0000313|EMBL:EPS25650.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS25650.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS25650.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionyl-[protein] + S-adenosyl-L-methionine = S-adenosyl-
CC L-homocysteine + S-methyl-L-methionyl-[protein];
CC Xref=Rhea:RHEA:60560, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:15592,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:142742; Evidence={ECO:0000256|ARBA:ARBA00036003};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561;
CC Evidence={ECO:0000256|ARBA:ARBA00036003};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000256|ARBA:ARBA00038158}.
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DR EMBL; KB644408; EPS25650.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z542; -.
DR SMR; S7Z542; -.
DR STRING; 933388.S7Z542; -.
DR eggNOG; ENOG502QQMC; Eukaryota.
DR HOGENOM; CLU_010595_2_0_1; -.
DR OrthoDB; 2241530at2759; -.
DR PhylomeDB; S7Z542; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43591:SF30; PROTEIN-METHIONINE METHYLTRANSFERASE LAEA; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 40019 MW; 3E187D63A29493C2 CRC64;
MDIYTITDRN PVDKDGDRRT GRFLSNGSVA SQRSQASRAS ESSPPVIISN RKIPERYPPY
KENNRLYHSY RKGTYMLPCD DEEQDRLDIF HKLFTVARVS DGLIYAPHPK NSRILDLGCG
TGIWSIEVAN KYPDSFVVGV DLAPIQPQNH PSNCDFYAPF DFESPWALGE DSWDLIHMQM
GSGSVASWPS LYRRIFSHLR PGAWFEQVEI DFEPRCDDRS LSNLALRHWY TALKRATEST
MRPLAHSSRE TIRNLQEAGF TEIDHQMVGL PLNPWHSDEH ERKVASWYNL AISESVETLS
LAPFSRVYNW PLEKIKRLAT DVKTEAFNKD LHCYNILHIY QARKPSAA
//
