ID A0A0A2JWZ1_PENEN Unreviewed; 1176 AA.
AC A0A0A2JWZ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 32.
DE SubName: Full=Zinc finger, NF-X1-type {ECO:0000313|EMBL:KGO56675.1};
GN ORFNames=PEX2_076280 {ECO:0000313|EMBL:KGO56675.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO56675.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO56675.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO56675.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NFX1 family.
CC {ECO:0000256|ARBA:ARBA00007269}.
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:KGO56675.1}.
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DR EMBL; JQFZ01000161; KGO56675.1; -; Genomic_DNA.
DR RefSeq; XP_016598381.1; XM_016744898.1.
DR AlphaFoldDB; A0A0A2JWZ1; -.
DR STRING; 27334.A0A0A2JWZ1; -.
DR GeneID; 27680318; -.
DR HOGENOM; CLU_005714_2_1_1; -.
DR OrthoDB; 1412at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd06008; NF-X1-zinc-finger; 6.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 7.
DR SMART; SM00438; ZnF_NFX; 9.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 905..969
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 127589 MW; D64595253F0A4869 CRC64;
MSTPGVSSQT SAAFSAMATP QPETSIPAGP RPPRSSRPSR RRGRGSAKRD GQQQTPAGEP
QSQAAPQAHP TQSQPQPNTT PQPSQQDGPS SSRRGGNREG RGRRQRNPPR QGQNQNGGHE
SQETRPEMRT RGMRARGFEA QLTRPDQAEN GPLLDGAGHL HDQSLRADVP DFVPGMPSSQ
QRQPAESTPS AKGKGKARQP RAPPPPKVTA KSTADDLATR IHEDISHNLY ECPICCSELG
RRSKVWSCEL CWTVFHLSCV KKWSTNEGAA AQRASAQEDG QDSPTPRAWR CPGCNLSQQN
FPTSYSCWCE KEVDPRPLPG LPPHSCGQTC SRPRKNCPHP CDTTCHAGPC TPCTAMGPIQ
DCFCGLNSSQ KRCQDTNYED GWSCGEICGE LLPCGEHTCP LPCHEGLCGG CEVSIDARCY
CGKLQTEMLC KSKDDEEDSR IVREDGSEDE WTGCFGCGET CNRPYDCGKH SCQKNCHPQD
PHPAHCPQSP DVIVNCACGK TPLSEIPGYT PRTSCEDPIL NCQKPCGKTL PCGHACEKLC
HVGSCGACLR NVHIKCNCGR TNNLTICHQG QNEPPQCPRM CKATLHCGRH ACTERCCPGE
QRANERQAAR RKLRPHLRPA DEDIEAEHIC TRICGRMLKC GRHTCPELCH KGACNTCREA
VFEEIPCNCG RSVLYPPQPC GAKPPACNFP CERPKRCGHP QAAHTCHTDE ENCPKCPFLT
EKACLCGKRV LKNVPCWLTD ARCGQVCGQL LKCGSHFCRK DCHRPGDCED ATKPCSHPCG
KTKTMCGHPC TEQCHAPYAC PEKTPCSSKI AVTCSCGRLR QERRCNAAKA VTSKGQVQSP
PRHPELTPLV CDDECTRLER NRSLAGALGI DINQTTTLQT ITAQNLPYSE ETLNQYVQLA
CSVPLSTLQT YESNLHALAA ADKPTRSFRF QPAKSTLRAF AHSLAADWGF VTESHDPEPH
RHVFVLKPVA WTPPLFGMGS GSTIGIGGMS VRECVKLRER ERSKEQEARR VAALEAKATR
EAAKVQASTG DGGWAQVASK SKGGSGAGSR AGTPVQNSWV SKSIYAALDG DGAKKERLVL
RSGVGVGKSL RAKTPAPEVV DDWEEAEEKE EKEEAGQQDQ GQEISVREDP EGKPELAPET
EAPADDGPTQ AEATGAEATQ AEATQAEAPI TDDVPV
//
