MBZ11_METRA
ID MBZ11_METRA Reviewed; 557 AA.
AC E9EPV1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=BZIP-type transcription factor MBZ1 {ECO:0000303|PubMed:25673695};
GN Name=MBZ1 {ECO:0000303|PubMed:25673695}; ORFNames=MAA_01736;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25673695; DOI=10.1074/jbc.m114.630939;
RA Huang W., Shang Y., Chen P., Cen K., Wang C.;
RT "Basic leucine zipper (bZIP) domain transcription factor MBZ1 regulates
RT cell wall integrity, spore adherence, and virulence in Metarhizium
RT robertsii.";
RL J. Biol. Chem. 290:8218-8231(2015).
CC -!- FUNCTION: BZIP-type transcription factor that functions as either an
CC activator or a suppressor, and which contributes to the regulation of
CC fungal growth, conidiation, cell wall integrity, and virulence
CC (PubMed:25673695). Plays a key role in virulence against insects by
CC mediating cell wall integrity, cell surface hydrophobicity, and
CC adherence to hydrophobic surfaces (PubMed:25673695). Exhibits negative
CC regulation of subtilisin proteases, but positive control of an adhesin
CC gene (PubMed:25673695). {ECO:0000269|PubMed:25673695}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25673695}.
CC -!- INDUCTION: Highly expressed during infection structure appressorium
CC formation. {ECO:0000269|PubMed:25673695}.
CC -!- DISRUPTION PHENOTYPE: Alters culture pigmentation and leads to defects
CC in cell wall integrity, adhesion to hydrophobic surfaces, and topical
CC infection of insects. {ECO:0000269|PubMed:25673695}.
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DR EMBL; ADNJ02000001; EFZ02154.2; -; Genomic_DNA.
DR RefSeq; XP_007817925.2; XM_007819734.2.
DR AlphaFoldDB; E9EPV1; -.
DR SMR; E9EPV1; -.
DR EnsemblFungi; EFZ02154; EFZ02154; MAA_01736.
DR GeneID; 19256022; -.
DR KEGG; maj:MAA_01736; -.
DR HOGENOM; CLU_020078_1_0_1; -.
DR PHI-base; PHI:4554; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Repressor; Transcription; Transcription regulation;
KW Virulence.
FT CHAIN 1..557
FT /note="BZIP-type transcription factor MBZ1"
FT /id="PRO_0000435640"
FT DOMAIN 264..327
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 171..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 289..296
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 61342 MW; 0EBC4F8DB35F2667 CRC64;
MSTSSQTIDV DALLDFSACD GSYNSPSLSP STASKPTFAS PVTAAVSTPS LPSTTQTLSG
PSHNYDMYRQ QTGFVPGALT NTMAVNQTNN TGYQDFGSLD YLSSFSPEND VFDFNASPSQ
GTMEMEFESP ADSQFFPTVN PSSIQHDTSA LSQTSSVGRL WPGAHSQAAL AKAQAQQRQQ
QQQQQLIQQT QRQTSPKSRG KAPQPTDPIV EQKITQLLNS MRAKPASNEP ESQSVLNNLP
KSKKDEEEMD EDERLLASEE GKKLSSKERR QLRNKVSARA FRSRRKEYIS QLEAEIANKV
NENGDLRSQN RALMDENKRL SDLTRMLLSS PSFSTFLDNL SANPTGLPQG SPVKIEQNPQ
QEQNQVPKDV NAYNSQFSSQ QQIGMAMIPE QTMDFSLLSL GNTYNFQPQV FVVDTPEVPN
AIDASVLSGK TSNFVEESFS SDDEKVEVPV IERPLKTKAI ETPEAPVDEE FESDPEFALF
HSEPATTTTT PKDIDTENLT GIDLFGGIES EKMFARYELV NATEEEATAA FAMARVQRIS
ASIDSVVSRL ELLTMDI
