LAEA_COPC7
ID LAEA_COPC7 Reviewed; 402 AA.
AC A8N374;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Secondary metabolism regulator laeA {ECO:0000303|PubMed:31496254};
DE AltName: Full=Methyltransferase laeA {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:C8VQG9};
GN ORFNames=CC1G_00498;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN [2]
RP INDUCTION.
RX PubMed=26510163; DOI=10.1371/journal.pone.0141586;
RA Muraguchi H., Umezawa K., Niikura M., Yoshida M., Kozaki T., Ishii K.,
RA Sakai K., Shimizu M., Nakahori K., Sakamoto Y., Choi C., Ngan C.Y.,
RA Lindquist E., Lipzen A., Tritt A., Haridas S., Barry K., Grigoriev I.V.,
RA Pukkila P.J.;
RT "Strand-specific RNA-seq analyses of fruiting body development in
RT Coprinopsis cinerea.";
RL PLoS ONE 10:e0141586-e0141586(2015).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31496254; DOI=10.1021/acs.orglett.9b02861;
RA Tsunematsu Y., Takanishi J., Asai S., Masuya T., Nakazawa T., Watanabe K.;
RT "Genomic mushroom hunting decrypts coprinoferrin, a siderophore secondary
RT metabolite vital to fungal cell development.";
RL Org. Lett. 21:7582-7586(2019).
CC -!- FUNCTION: Methyltransferase that performs automethylation (By
CC similarity). No other methyl-accepting substrate has been identified
CC yet (By similarity). Acts as a global regulator for secondary
CC metabolite gene expression (PubMed:31496254). Negatively regulates the
CC production of coprinoferrin, a structurally novel acylated tripeptide
CC hydroxamate siderophore (PubMed:31496254).
CC {ECO:0000250|UniProtKB:C8VQG9, ECO:0000269|PubMed:31496254}.
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:0000250|UniProtKB:C8VQG9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60561;
CC Evidence={ECO:0000250|UniProtKB:C8VQG9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VQG9}.
CC -!- INDUCTION: Moderately expressed during the development but expression
CC is induceded in the mycelium stage. {ECO:0000269|PubMed:26510163}.
CC -!- DISRUPTION PHENOTYPE: Leads to the production of coprinoferrin.
CC {ECO:0000269|PubMed:31496254}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AACS02000001; EAU92279.1; -; Genomic_DNA.
DR RefSeq; XP_001829319.1; XM_001829267.1.
DR AlphaFoldDB; A8N374; -.
DR EnsemblFungi; EAU92279; EAU92279; CC1G_00498.
DR GeneID; 6005747; -.
DR KEGG; cci:CC1G_00498; -.
DR VEuPathDB; FungiDB:CC1G_00498; -.
DR eggNOG; ENOG502S6PS; Eukaryota.
DR InParanoid; A8N374; -.
DR OMA; KWGRDIR; -.
DR OrthoDB; 1047281at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Sporulation; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..402
FT /note="Secondary metabolism regulator laeA"
FT /id="PRO_0000452733"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 46935 MW; 07040E04FABBABF5 CRC64;
MSLKYYLNDL SDSDSESESE CAEGSSPQDE QNGFYDYRSP PDSADTSIFE DTGRSSSERP
MSPTEVCSTD FEEKVPFSSE LVVIPESMLK KREEYGRFFS NFKKAIYHLP ADEEEWDRQE
RLHQSFIEMF GRKYPPELSE ILKSDEYYEK RCLDLGCGTG CWIKEVARDF PYCEAVGVDL
VVVPDTRDFP PNLRCEMDDV NLGLQHFFGR FDVVHARLLS SGIKDYQLLI ENIARTLRPG
GLVELQEYDF HIYDCNRRRF ELSTNELAPP WWPRWMTFFN EAIRKMQGDV DAATHLLKWV
RTHPGFEQVR YEERWIPIIP GNLDPLEPMY ARLQADVSVY LRSGRPLLLK SGLSEMEVDI
LENNAIREFY ESETTQYTRL QCVCARRNNA VLDHLPPSYN FR
