ID   B8MX14_ASPFN            Unreviewed;      1286 AA.
AC   B8MX14;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Zinc finger protein, putative {ECO:0000313|EMBL:EED56906.1};
GN   ORFNames=AFLA_076010 {ECO:0000313|EMBL:EED56906.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56906.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED56906.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; EQ963472; EED56906.1; -; Genomic_DNA.
DR   RefSeq; XP_002372518.1; XM_002372477.1.
DR   EnsemblFungi; EED56906; EED56906; AFLA_076010.
DR   VEuPathDB; FungiDB:AFLA_003155; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_002406_3_2_1; -.
DR   OMA; NHIYTHQ; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          1180..1213
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1231..1258
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1259..1286
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          342..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1286 AA;  147219 MW;  CA403ED24AD4E4F6 CRC64;
     MDERHRPLRR NDFEVAIICA LPLEANAVLC SLDEIWHDAH NMYGRAVGDG NAYDFGRSGR
     HSVVVVTLPG MGKVPASTAA SYLRMSFSSI KLVLLVGVCG AVPRTDRTEI ILGDVVISQS
     IVELDRGRQY PNGFKRKDTI LDSHGRPNED ILGLLQRWKA TLHLKNLQKK TLENLKTLLQ
     HPYSEARYPG ETEDKLFEPD YIHRHHFGCG ICNIPAAPDS VCEAALTAAC DELQCDESKL
     VPRTRLHERD TDGEIPTPLI HFGLIGTADT VQKSAAHRDK HAESEGVIAF EMEGAGVWNK
     FNCLIIKGVC DYADSHKNKN WQNYAAAVAA SVAKEILGQY VSHDQPSQPG TPNGSSGYST
     QLSMISRGRA TKQFKEGLAK KQLDTFKATD LRALKKELKK IQDEQGQSHS LRNLRRLERF
     IQATEQIGTV LEDILGTSEE MCLVWGPVKA LLQVAKGNVD LFDTLLEAYE DIGSELPNLG
     VYRELFKHHV GLQRILARVF ALLLEFHENA LRLYSGRALR TVFRPLWKDF ETTLFDVIVR
     ETGSHRIMIE DKTMALYSHP GHCTMDAQEV RDHLESTSNN MRLSKQEHQK AREKMYDEVR
     CWIAGAAGVS GVEDVADVVG AETESDHNNI CRDRSFYPGS GSWILENEKV KKWLSPEPEQ
     SSNSMLWING RPGTGKTYLA SVVIETCLED SSSVTCYFYC KEKVKSRNSA IAVLRGILLQ
     LARQHRELIP YCYAKIKSSG SLMLSDLSTA NGILEVFCER IPRLNVVIDG VDECEEQRKD
     LIDIFRILVR KNEIYAKGKL RVLFLSRPMN EVKNALPEAE MLALEPDHNR QDIQKYCERR
     KREFQKFGFD NEYLKDVVQI ICTRADGMFL FAKLVMNNLK EQPTREDFRI ETTAAILPSE
     IDQAYARIME RLARDLGSKQ YEYTELLLGW LVCSKRPLKW TEIQVALSID IKTWGHTSEV
     NPDRRLEDDV QELCGSLVQV LKGNRVELVH STARLPDISA QRLRENALRG DFGFQDYAVS
     AWFLHVGTLI EKKHDLLEGI FDSQDRVARI SRELEHFASF YQESFPLYDN NILEQAWIDC
     EFFRQYHFHN NLVRIWNHIC CAQREDLESR NSVSIPLLKE TLARNRQLLE NLSTEDTVTL
     SRVYDEYPFR CPKVLCFYFH EGFKNALARD NHVDHHNRPY RCTVGTCEMN GMGFAEKSRL
     TAHMKRFHPE ERDLGETFTP YNRTRSVGAR YECPVCNKRL VRKNILEDHQ RIHTGEKPFR
     CSECGKGFAR NYDKKRHEKI HEKRRR
//