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ATFB_ASPFU
ID   ATFB_ASPFU              Reviewed;         328 AA.
AC   Q4WVQ7;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Basic leucine zipper (bZIP) transcription factor atfB {ECO:0000303|PubMed:27706915};
GN   Name=atfB {ECO:0000303|PubMed:27706915}; ORFNames=AFUA_5G12960;
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27706915; DOI=10.1111/cmi.12681;
RA   Pereira Silva L., Alves de Castro P., Dos Reis T.F., Paziani M.H.,
RA   Von Zeska Kress M.R., Riano-Pachon D.M., Hagiwara D., Ries L.N.,
RA   Brown N.A., Goldman G.H.;
RT   "and MpkC dependent.";
RL   Cell. Microbiol. 19:0-0(2017).
CC   -!- FUNCTION: Transcription factor that acts as a key player in the
CC       regulatory circuit that integrates secondary metabolism and cellular
CC       response to oxidative stress (By similarity). Regulates the genes
CC       involved in development, as well as osmotic, oxidative, and cell wall
CC       stresses (PubMed:27706915). Participates in the caspofungin paradoxical
CC       effect (CPE), where fungi grow beyond the minimum inhibitory
CC       concentration of caspofungin (PubMed:27706915). Plays a role in
CC       virulence (PubMed:27706915). {ECO:0000250|UniProtKB:A0A0F0IP79,
CC       ECO:0000269|PubMed:27706915}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- INDUCTION: Expression is induced in during osmotic stress and repressed
CC       in the absence of the mitogen-activated protein kinase sakA
CC       (PubMed:27706915). Expression is also highly induced at low and high
CC       caspofungin concentrations (PubMed:27706915).
CC       {ECO:0000269|PubMed:27706915}.
CC   -!- DISRUPTION PHENOTYPE: Increases sensitivity to osmotic and oxidative
CC       stresses, but also to cell wall-damaging agents such as Congo red or
CC       iprodione (PubMed:27706915). Shows increased resistance to low
CC       caspofungin concentrations, but is more sensitive to higher caspofungin
CC       concentrations (PubMed:27706915). Leads to attenuated virulence
CC       (PubMed:27706915). {ECO:0000269|PubMed:27706915}.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000003; EAL91319.1; -; Genomic_DNA.
DR   RefSeq; XP_753357.1; XM_748264.1.
DR   AlphaFoldDB; Q4WVQ7; -.
DR   SMR; Q4WVQ7; -.
DR   STRING; 746128.CADAFUBP00005927; -.
DR   EnsemblFungi; EAL91319; EAL91319; AFUA_5G12960.
DR   GeneID; 3510880; -.
DR   KEGG; afm:AFUA_5G12960; -.
DR   VEuPathDB; FungiDB:Afu5g12960; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_888511_0_0_1; -.
DR   InParanoid; Q4WVQ7; -.
DR   OMA; HAQCGDE; -.
DR   OrthoDB; 1519076at2759; -.
DR   PHI-base; PHI:6909; -.
DR   Proteomes; UP000002530; Chromosome 5.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..328
FT                   /note="Basic leucine zipper (bZIP) transcription factor
FT                   atfB"
FT                   /id="PRO_0000444006"
FT   DOMAIN          163..226
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..202
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          205..219
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          250..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  36651 MW;  E35C38003674A1CB CRC64;
     MLPEQSAFGR SAMPGSDAVN PGPSPFAPPP NSFSGDFLGL SLPDEEHLWG MSPLSSSMPS
     WNGKNEQMFS NPNLERDLKH SHVRNGQPTP PPYGDNKTHT VGDLYSLSQC QFSNGAQNFQ
     THNDRRSFCE QSAINSNGGS SKRRKVRDAK MTQAEYNEQQ QEKAKREKFL ERNRLAASKC
     RQKKKEHTQL LESRYREQSD KKEQLVSEIA RLRSEILGLK NEVLKHAQCG DEPIKLHLAQ
     MVKKITYNDT TAPDLTDVPD AASSSEGPMT PRPQQALSFG FDDPLHLEPS RADGSTDHSV
     RRDSEASVLT ENSYAFSTDE SFDDLINV
 
 
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