ID   A0A179FN34_METCM        Unreviewed;       594 AA.
AC   A0A179FN34;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=CCCH zinc finger domain-containing protein {ECO:0000313|EMBL:OAQ66429.1};
GN   ORFNames=VFPPC_07981 {ECO:0000313|EMBL:OAQ66429.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ66429.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ66429.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ66429.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ66429.1}.
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DR   EMBL; LSBJ02000004; OAQ66429.1; -; Genomic_DNA.
DR   RefSeq; XP_018143516.1; XM_018286760.1.
DR   AlphaFoldDB; A0A179FN34; -.
DR   STRING; 1380566.A0A179FN34; -.
DR   GeneID; 28850754; -.
DR   KEGG; pchm:VFPPC_07981; -.
DR   OrthoDB; 232322at2759; -.
DR   Proteomes; UP000078397; Chromosome 4.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR21099:SF2; C3H1-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21099; RAD201; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          1..25
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         1..25
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          114..155
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        188..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  61841 MW;  71B33A216D6D3C43 CRC64;
     MAICKFYQQG NCKFGSSCRF EHPGAGNNRN QPQNRFGALS SGAGGGGSGP LQNAFDRYNI
     AVDTIEKDLT SEAPQWILSA YAPGRNAPEQ LFGGYPREQS FEEMRLHYMM GKAAGNEQQA
     LNQAQELYQN AQQQMQNAAR NAQDAARFIV EAENKHPNRL DICQEGSQGA PFGEFEVGKR
     PVGMAQPAQA NPFSTGSSTT SPFGGGSSQP TPSAFGQPAA LGQRPNPFGT QAFGQPAQPS
     SGFGQPSQPA SGFGQQSSSQ PQASPFGQPS QPSQPSQPSA PAFGQPSQPT SAFGQASALG
     AKPSPFGAPA FGQSAQPANS QPSAFGQVGQ MGSQPNPFAS GGAANKSSSP FGSVGTANNN
     TQAPAAANPF ASSNTSQNNA TPNPFGSNTS NQAGNAAQSS PFGQQPAQSQ SPFGQGAKPN
     PFASTTTADS QPASNPFAQN TQNQPNGAFG ANASSPFSQG ASQQQNPFAS SNQPQQVAAP
     ATGGGNPYPP DSTKQHPSLE SYASKNMDGS LAAFRGKPVT YKEGKPGIRA FDGTWTRIWF
     PGGAPGYYKD TELPTDAYDE QSKNQWASFA QTGTFANGIM PDLPPPRECT RWDF
//