ID   A0A0L1IZN2_ASPNO        Unreviewed;      1334 AA.
AC   A0A0L1IZN2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Zinc finger protein {ECO:0000313|EMBL:KNG84885.1};
GN   ORFNames=ANOM_006877 {ECO:0000313|EMBL:KNG84885.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG84885.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG84885.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG84885.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KNG84885.1}.
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DR   EMBL; JNOM01000183; KNG84885.1; -; Genomic_DNA.
DR   RefSeq; XP_015405808.1; XM_015552133.1.
DR   STRING; 1509407.A0A0L1IZN2; -.
DR   GeneID; 26808681; -.
DR   OrthoDB; 1785483at2759; -.
DR   Proteomes; UP000037505; 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; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          1228..1261
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1279..1306
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1307..1334
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1334 AA;  152567 MW;  945C7A1DB059F9F1 CRC64;
     MDERHRPLRR NDFEIAIICA LPLETNAVLC SLDEVWRDAH HTYGRAGGDN NHYSYGRSGK
     HSVVVVTLPK MGKVNASSAA SYLRMSFTSI KLALLVGICG AVPRKADGTE IVLGDVMISE
     ILVVLDYGRQ YPNGFKRKNT ILDTHGRLNE DVWGLLQRWK TAFHLKYFQE KTMEHLKALL
     QHPDSMAKYP GATEDKLFEP DYIHSHHFGC WVCNMSGVPG SVCEASVTAT CDELQCDESR
     LVPRTRLHER DTELEIPTPL IHFGSIGCAD TVQKSAEHRD QYAKSEGVIA FEMEGAGVWD
     KFNCLIIKGV CDYADSHKNK KWQDYAAAVA ASVAKEVLAQ YVSHDQPSQP GTPNGSSGYS
     TQPSIVSRSR LDLQMVPDSL PKDMFHRVTK HFEEGLEKEQ LDAFKATDLR ALKKELKKIQ
     DEQGQSHSLR NLRRIERFIQ AMEQIGTVLE DILGTSKDMS LIWGPVKALL QTAKGNVDLF
     DTLLAAYESI GDQLPMLGAY REFFKSYVGL QRILARTFAL ILEFHENAIR LYSGRALRTV
     FRPLWKDFEA IFVLILGEIG SHRTLIEDKT MALYSHPGYY PMDAQEIRNH LESTSNNMHL
     SKEKQKIVRE KMYDEVRCWI AGAAGVSGVE DVADAKGAET ESDHNNICRD RSFYPGSGSW
     ILENEKVKKW LSPEPEQSSN SMLWINGRPG TGKTYLASVI IEACLGDSSS LTCYFYCKEK
     VKSRNSAIAV LRGILLQLAR QHRELIPYCH AKIKSSGSLM LSDLSTAHGI LEVFCERISR
     LNVVIDGVDE CEEQRKDLID TFRILVRKNE IYSKGKLRVL FLSRPMNEVK NALPEAEMLA
     LEPEHNRQDI QKYCECRKRE FQKFGFGNEY LKDVVQVICT RADGMFLFAK LVMNNLKEQP
     TKEDFRTETT AAILPSEIDQ AYVRIMERLK RDLGSKQYEY TELLLGWLVC SKRPLKWTEI
     QVALSTDIKT WGRSSEVNPD RRLEDDVQEL CGSLVQVLKG NRIELVHSTA RLFIIQKSNI
     RISAAECDLA LRCLRYLSLD IFRPDVSASR LRENALSGDF AFQDYAVAAW FLHIGTLIEK
     KHDFLEEGIN GQDRVARISR ELEHFVGFYQ ASFSVDGSSI LEQVWIDCAF FQQYPFYNNL
     VRIWNHICCG QRGDLESRNN VSIPLLKGTL ARNRKLLEDL STDDTVVLSR LNDEYPFRCP
     KVLCFYFHEG FKNAIARDKH EDHHNRPFRC TVENCTMNGM GFAEKSRLTA HMKRFHPEER
     DLGETFTPYE RKRPVGARYE CPICKKRLVR KNILQDHQRI HTGEKPFRCS ECGKGFARSY
     DKKRHEKIHE KRRR
//