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HXNR_EMENI
ID   HXNR_EMENI              Reviewed;         865 AA.
AC   C8VJW0;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Nicotinate catabolism cluster-specific transcription factor {ECO:0000303|PubMed:29212709};
GN   Name=hxnR {ECO:0000303|PubMed:29212709};
GN   Synonyms=aplA {ECO:0000303|PubMed:4581274}; ORFNames=ANIA_11197;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=4581274; DOI=10.1111/j.1432-1033.1973.tb02928.x;
RA   Scazzocchio C., Holl F.B., Foguelman A.I.;
RT   "The genetic control of molybdoflavoproteins in Aspergillus nidulans.
RT   Allopurinol-resistant mutants constitutive for xanthine-dehydrogenase.";
RL   Eur. J. Biochem. 36:428-445(1973).
RN   [4]
RP   IDENTIFICATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF PRO-219; TYR-226; ASN-227; TRP-228; PHE-230; ASP-237; ALA-238; PHE-239;
RP   PHE-565; LYS-603; THR-607 AND ARG-639.
RX   PubMed=29212709; DOI=10.1098/rsob.170199;
RA   Amon J., Fernandez-Martin R., Bokor E., Cultrone A., Kelly J.M.,
RA   Flipphi M., Scazzocchio C., Hamari Z.;
RT   "A eukaryotic nicotinate-inducible gene cluster: convergent evolution in
RT   fungi and bacteria.";
RL   Open Biol. 7:0-0(2017).
CC   -!- FUNCTION: Transcription factor that specifically regulates the
CC       expression of the hxn gene cluster that mediates the degradation of
CC       nicotinate and related metabolites (PubMed:4581274, PubMed:29212709).
CC       {ECO:0000269|PubMed:29212709, ECO:0000269|PubMed:4581274}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:29212709}.
CC   -!- INDUCTION: Expression is induced by nicotinate and 6-OH nicotinate and
CC       is subject to nitrogen metabolite repression mediated by the GATA
CC       factor areA (PubMed:29212709). {ECO:0000269|PubMed:29212709}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the inability to use nicotinate, 6-OH
CC       nicotinic acid, and 2,5-dihydroxypyridine as sole nitrogen sources
CC       (PubMed:29212709). {ECO:0000269|PubMed:29212709}.
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DR   EMBL; BN001306; CBF82382.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VJW0; -.
DR   SMR; C8VJW0; -.
DR   EnsemblFungi; CBF82382; CBF82382; ANIA_11197.
DR   VEuPathDB; FungiDB:AN11197; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_005733_1_1_1; -.
DR   InParanoid; C8VJW0; -.
DR   OMA; IRRSNCC; -.
DR   OrthoDB; 319562at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..865
FT                   /note="Nicotinate catabolism cluster-specific transcription
FT                   factor"
FT                   /id="PRO_0000443341"
FT   ZN_FING         8..32
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         41..63
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          74..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           77..87
FT                   /note="Nuclear localization signal(NLS)"
FT                   /evidence="ECO:0000303|PubMed:29212709"
FT   MOTIF           285..289
FT                   /note="Nuclear export signal (NES)"
FT                   /evidence="ECO:0000303|PubMed:29212709"
FT   COMPBIAS        74..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         219
FT                   /note="P->A,L: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         226
FT                   /note="Y->D,L,S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         227
FT                   /note="N->D: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         228
FT                   /note="W->R,S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         230
FT                   /note="F->I,S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         237
FT                   /note="D->Y: Leads to constitutive activator activity; when
FT                   associated with Pro-238."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         238
FT                   /note="A->P: Leads to constitutive activator activity; when
FT                   associated with Tyr-237."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         239
FT                   /note="F->S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         565
FT                   /note="F->S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         603
FT                   /note="K->N,E,T: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         607
FT                   /note="T->P,S: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
FT   MUTAGEN         639
FT                   /note="R->C: Leads to constitutive activator activity."
FT                   /evidence="ECO:0000269|PubMed:29212709"
SQ   SEQUENCE   865 AA;  94673 MW;  A5E16296A17BCEBE CRC64;
     MKAKMKKHAC TYPGCSKAFT RAEHLRRHSL NHETISNSQG YTCQRCMTHF SRADLLSRHL
     DRHAKKDAEA GGFGKGVLET RKRMRRAEDG SIVLRPPKRP SRHQQKTGPP VGAPLSSSGS
     VSAGSGRSSR SPDVSLHAAQ APVSPPRSAS DPVSVSGVSI DDDGTDPDPM LAPMMPGGPF
     EPYVEPIPGQ FDAADGSWGG FDALGDGMML DTATDFNLPF AATGNYNWLF DVSSLDDAFH
     HLELPLGPDL VPFANSHGNY ASVNTMELSG AGAENVQDSM LNLDLDIDLN GLPAGFVHDQ
     GPDGSSASVL LQAASFVERG NINGSDPKRD FPDLDWMAGA PPIESTVPLR PQLSEDARRG
     ILTLIAQSPP VDIHGQPLNL DSPLLSLSAL QSYSDLFFSR FNTTYPLIHS ATFDPNKTEP
     VFLASILSMG ATYSSREAHQ LAVGIHDGLR NQLFCHGAFS PQPDELWVLQ AMLLIDCFGK
     MRAGPKQRER AQLFHCVLIK LIRRSTCCSI RADTHSDPGL GGLELEDAWK RAMDAEQRKR
     LAFQCFMWDT EHSVLFSQSL CMSAFEIRSS LPCSPAAWEA HTAEEWSRHA SRDTEHAFLP
     VLKGYITPGS VSRPRDLNRF SRMVVLHGLM SISADLKRRD QTTLRAETPE RVGAWTPRMG
     RAYDLWKADF DADCLNMKLG PVQVSADETR RFTSLKAAAM ALYRAASLAL HVEVLDLQIA
     AGASHILGRV VKQHDRERSR VMLSRWLSGP SPAATTASRH AAALLQDAVL SLHDWDQTDA
     FHFPWCLYLA TLTVWAFHAR EGCVPKPTDL SSLIVAMTTS NAADLEGLAG QYDTRPLIRA
     MAQQLATVRW AVVHDAMKVL LNLGV
 
 
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