RLMA_ASPFU
ID RLMA_ASPFU Reviewed; 600 AA.
AC Q4WX78;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 23-FEB-2022, entry version 100.
DE RecName: Full=Transcription factor rlmA {ECO:0000303|PubMed:27473315};
GN Name=rlmA {ECO:0000303|PubMed:27473315}; ORFNames=AFUA_3G08520;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
RX PubMed=19715768; DOI=10.1016/j.fgb.2009.08.005;
RA Valiante V., Jain R., Heinekamp T., Brakhage A.A.;
RT "The MpkA MAP kinase module regulates cell wall integrity signaling and
RT pyomelanin formation in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 46:909-918(2009).
RN [3]
RP FUNCTION.
RX PubMed=21883519; DOI=10.1111/j.1365-2958.2011.07778.x;
RA Jain R., Valiante V., Remme N., Docimo T., Heinekamp T., Hertweck C.,
RA Gershenzon J., Haas H., Brakhage A.A.;
RT "The MAP kinase MpkA controls cell wall integrity, oxidative stress
RT response, gliotoxin production and iron adaptation in Aspergillus
RT fumigatus.";
RL Mol. Microbiol. 82:39-53(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=27473315; DOI=10.1534/g3.116.031112;
RA Rocha M.C., Fabri J.H., Franco de Godoy K., Alves de Castro P., Hori J.I.,
RA Ferreira da Cunha A., Arentshorst M., Ram A.F., van den Hondel C.A.,
RA Goldman G.H., Malavazi I.;
RT "Aspergillus fumigatus MADS-Box transcription factor rlmA is required for
RT regulation of the cell wall integrity and virulence.";
RL G3 (Bethesda) 6:2983-3002(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27393422; DOI=10.1111/mmi.13462;
RA Valiante V., Baldin C., Hortschansky P., Jain R., Thywissen A.,
RA Strassburger M., Shelest E., Heinekamp T., Brakhage A.A.;
RT "The Aspergillus fumigatus conidial melanin production is regulated by the
RT bifunctional bHLH DevR and MADS-box RlmA transcription factors.";
RL Mol. Microbiol. 102:321-335(2016).
RN [6]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
RX PubMed=32005734; DOI=10.1128/aem.02347-19;
RA Rocha M.C., Fabri J.H.T.M., Simoes I.T., Silva-Rocha R., Hagiwara D.,
RA da Cunha A.F., Goldman G.H., Canovas D., Malavazi I.;
RT "The cell wall integrity pathway contributes to the early stages of
RT Aspergillus fumigatus asexual development.";
RL Appl. Environ. Microbiol. 86:0-0(2020).
RN [7]
RP FUNCTION, AND INTERACTION WITH HSP90.
RX PubMed=33010083; DOI=10.1111/cmi.13273;
RA Rocha M.C., Minari K., Fabri J.H.T.M., Kerkaert J.D., Gava L.M.,
RA da Cunha A.F., Cramer R.A., Borges J.C., Malavazi I.;
RT "Aspergillus fumigatus Hsp90 interacts with the main components of the cell
RT wall integrity pathway and cooperates in heat shock and cell wall stress
RT adaptation.";
RL Cell. Microbiol. 23:e13273-e13273(2021).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RX PubMed=33705521; DOI=10.1093/genetics/iyab036;
RA Rocha M.C., Fabri J.H.T.M., da Silva L.P., Angolini C.F.F., Bertolini M.C.,
RA da Cunha A.F., Valiante V., Goldman G.H., Fill T.P., Malavazi I.;
RT "Transcriptional control of the production of Aspergillus fumigatus
RT conidia-borne secondary metabolite fumiquinazoline C important for
RT phagocytosis protection.";
RL Genetics 0:0-0(2021).
CC -!- FUNCTION: Transcription factor; part of cell wall integrity (CWI)
CC signaling pathway composed of pkcA, the bck1-mkk2-mpka MAPK cascade and
CC the downstream rlmA transcription regulator (PubMed:16372009). The CWI
CC signaling pathway regulates cell wall integrity and pyomelanin
CC formation (PubMed:19715768). CWI controls also oxidative stress
CC response, gliotoxin production, iron adaptation and asexual development
CC (PubMed:21883519, PubMed:32005734). Finally, CWI is constitutively
CC required for A.fumigatus to cope with the temperature increase found in
CC the mammalian lung environment, during infection (PubMed:33010083).
CC Positively regulates the phosphorylation of mpkA (PubMed:27473315).
CC Involved in tolerance to oxidative damage and transcriptional
CC regulation of genes related to oxidative stress adaptation
CC (PubMed:27473315). Finally, CWI is constitutively required for
CC A.fumigatus to cope with the temperature increase found in the
CC mammalian lung environment, during infection (PubMed:33010083).
CC Directly regulates the expression of regulators of conidiation,
CC including flbB, flbC, brlA, abaA, and rasB, as well as genes involved
CC in cell wall synthesis and remodeling (PubMed:32005734). Specifically
CC associates with the target fumiquinazoline (fmq) cluster genes
CC promoters at conserved motifs (5'-TAWWWWTA-3') during conidiation to
CC supplement mature conidia with fumiquinazoline C (PubMed:33705521).
CC Controls also the DHN-melanin production via binding the promoter of
CC pksP (PubMed:27393422). {ECO:0000269|PubMed:16372009,
CC ECO:0000269|PubMed:19715768, ECO:0000269|PubMed:21883519,
CC ECO:0000269|PubMed:27393422, ECO:0000269|PubMed:27473315,
CC ECO:0000269|PubMed:32005734, ECO:0000269|PubMed:33010083,
CC ECO:0000269|PubMed:33705521}.
CC -!- SUBUNIT: Interacts with hsp90. {ECO:0000269|PubMed:33010083}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- INDUCTION: Expression is induced during cell wall stress
CC (PubMed:27473315). Also induced during asexual development
CC (PubMed:32005734). {ECO:0000269|PubMed:27473315,
CC ECO:0000269|PubMed:32005734}.
CC -!- PTM: Phosphorylation during asexual development.
CC {ECO:0000269|PubMed:32005734}.
CC -!- DISRUPTION PHENOTYPE: Exhibits an altered cell wall organization in
CC addition to defects related to vegetative growth and tolerance to cell
CC wall-perturbing agents (PubMed:27473315). Results in attenuated
CC virulence in a neutropenic murine model of invasive pulmonary
CC aspergillosis (PubMed:27473315). Leads to reduced conidiation during
CC asexual differentiation (PubMed:32005734). Reduces conidial pigment
CC DHN-melanin formation (PubMed:27393422). Strongly decreases the
CC production of fumiquinazoline C (PubMed:33705521).
CC {ECO:0000269|PubMed:27393422, ECO:0000269|PubMed:27473315,
CC ECO:0000269|PubMed:32005734, ECO:0000269|PubMed:33705521}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000002; EAL92725.1; -; Genomic_DNA.
DR RefSeq; XP_754763.1; XM_749670.1.
DR SMR; Q4WX78; -.
DR STRING; 746128.CADAFUBP00003974; -.
DR EnsemblFungi; EAL92725; EAL92725; AFUA_3G08520.
DR GeneID; 3512174; -.
DR KEGG; afm:AFUA_3G08520; -.
DR VEuPathDB; FungiDB:Afu3g08520; -.
DR eggNOG; KOG0014; Eukaryota.
DR HOGENOM; CLU_024080_1_0_1; -.
DR InParanoid; Q4WX78; -.
DR OMA; HKGPADF; -.
DR OrthoDB; 1192094at2759; -.
DR PHI-base; PHI:6647; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..600
FT /note="Transcription factor rlmA"
FT /id="PRO_0000453188"
FT DOMAIN 1..61
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 71..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 64379 MW; 3C93CE422897A9CD CRC64;
MGRRKIEIKA IKDDRNRSVT FLKRKGGLFK KAHELAVLCS VDVAVIIFGH NKKLYEFSSC
DMRETLGRYQ YYGPPHEHKG PEDFNGKRDD DDDEDETTPA PEEMQPTTQN PPAVVPAHIP
SHPGFQHVNH APSASPPISN GIPFDPRHGT PQPQGASRPS SRNHLRRVSS NLGPQQHHGT
PPPPPQNGFA YIPNPSMYHP NANPNIAQQP RPPQFAHYGP QQPLPPHAIP PHPMPQPVPP
HHQAPQHLPQ HPHPLAQQTP AMGLSQPPHA SIPQVAQPFL PEQGRNSIPP AFPTEQSQPP
RPVSLPDVSS ADQMVGPLKV ETSPSPPHQR SLSSKSRSIF TPIDDRGSVL ARHFGLGPPT
CESPRTESAD VKAEAKQNDS KEIKPPAQPV APPPPPRTTA DAARSQSAPD IKPPPRTNSG
QLPSKRPQLK VQIPSENSDR GSATADSSSS TGNQTVTPAK ANPDTNHSGV VLPPPSPSAG
AILSAGATGP PNPFARPPPP GTASQNSNAY NSNNNIETPI SALPSRFVSD ALLPSPSSFF
PEWGFGRSGP DTNMLPSPLT FPTPAVQTGP GFAREDEQEK KRKSPDSGPS IEGTAKKSKT
