ID A0A0M9ESS5_FUSLA Unreviewed; 1396 AA.
AC A0A0M9ESS5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Amidase signature enzyme {ECO:0000313|EMBL:KPA39149.1};
GN ORFNames=FLAG1_07994 {ECO:0000313|EMBL:KPA39149.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA39149.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA39149.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA39149.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPA39149.1}.
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DR EMBL; JXCE01000215; KPA39149.1; -; Genomic_DNA.
DR OrthoDB; 2322629at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR40626:SF22; C2H2-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR40626; MIP31509P; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 603..630
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 631..659
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 653..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 153976 MW; B914043E0B719D67 CRC64;
MSVFFKEIQP GNPIQKGDVE ALLDPLELTI RPEDSADYQL LLAAVHDCAE RISSLPDYQP
IPDTERFPRQ DVRLAENHEQ VFGHAWAHRF TIHGDKTSRS SLAGKLVCLK DCIAVAGVPQ
FFGSDAFPAW TPSTDATVVT RSLEAGAVIT GTATCENFCN STSSFTSAQG IIDNPRKAGY
SAGGSTSGGA ALVTGGLADI AIGTDQGGSI RVPASLCGCV GFKPTHGLVP YTGISSGDQI
DDHAGPLTRT VDEIAACLDA IAGYDGIDDR SLGAASHGSF GFLESLNGAS LQGVRIGVLK
EGYDNSLVQP GVKKAFFETV NRLESLGAIV EEISIPIHKE GPSIWTIQQR ISGSAGILGQ
ANGRRGLYLT EFEQARLPWT ASQFEKLFPS TKNTVINGLY LQRTFPGLYS KTVNIGRQIR
DAYEIKFKEY DAIIMPTTPF VAPRHGSRES VLKSFEPSIG MTNNTAIFNV TGQPALSLPV
GWSQAVDDES VMLPVGLQIV GGLWEEKKVL RIAKALESSF DWEAGGKSTP AEAGDILNEP
HSQQLQDKLG TTPSAFVLPC LLLHLQRSIG VEMTREMVLD AYSRSTSPNK RQKVGHNGGA
NLRMCHHCGR RFKRTEHLER HVRTHTKEKP FLCHCGASFA RRDLLTRHQR IAEHEGDAPS
PGSVLGPGAL TQSRQNSISG EQVDLAAAVS LSGHNVDPWF CARAQQAMQV PVTMTVDEQT
QRPPNIDAGQ FVPNFLSPQM LDSGVDFDTH FREFTSFLDG VGLSAEWSPF FGDRDRHLDP
VDPELRNEEN ETASPQQGAP TRAGTPFSSW LPSAPTGNRI NNYVSDTDNP RAVDPETRPF
KVTEEQRSKV KAFIQDFSHL LDPAFCVPSR HALTRYIASF FEGFHSHMPF IHVPTWQITE
HSPELIFGIA AIGAQYCFER KASERLFFAG KALVLERLRR NAELFDISAI PRIHTVNSAK
QSGRDSNAPD KESQVETIRA LVTLMGFATW EPKAAMVQES FVLQGILTQA LRNAGLEDVD
ELVSSTPSNH PHDSNALWHD WRTWAKQESC RRSKLICFSF LHTHSIAYNV YPTLRSNEVG
LRLPCSTKEW KAPNAASWRA AAREVEEPQL FFREALSLLL KNKSESAPLF PIPTPLGNYV
LLHGLLQRIH IVRDLSLPIT SSSAFLPSEE VEKLERGLRS WTSCWQQAPE STLDPNNENG
PIPFTSSSLL ALAYVRIYLH LGPFRQLETR DPQLIAEAIA SSPDIERSDG IIAALLYAAH
MIGIPVRLGV DRVARSQAFF WSVRHSLSGL DCAVLLSKWL SKLAETVSES PLSDSEDRIL
HWVRCIVEEA YTVVDFEQSH DQEIANLLDF TDPQNLSLAV LKIWAHFFKS NTQWLFINII
GVGLEKYREI LIQKKI
//
