ID A0A1V6R0G0_9EURO Unreviewed; 841 AA.
AC A0A1V6R0G0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=PENSOL_c023G11839 {ECO:0000313|EMBL:OQD94944.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD94944.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD94944.1}.
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DR EMBL; MDYO01000023; OQD94944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R0G0; -.
DR STRING; 60172.A0A1V6R0G0; -.
DR OrthoDB; 2210730at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF14529; Exo_endo_phos_2; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 387..402
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..116
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 94514 MW; 523CE2ABF8249987 CRC64;
MRTTEPPDLD EHGDSPPRLS RPKRTTRPPN KYSREQEIDS EQRKTRSQQK NRTQIEPEAQ
RDATTADDSS TESEDLSTTN LVKELVKLRE EIRRRDELHR EELQKVQEEF RKAREEFGAA
LAGVRHELQT VTDRPPTPQS HTEACAQNNH DEILREIQSL RDAISPSVPT GSPSYADVAR
TPPLSHPSNI RTLSTSNTTP TTVTDTLYCT IDTSKMAEND NERISAGPIR AAVESEIRTM
EGHTHWRCRA VTVDPKNTNR IRIACRDEYE HQLVKKVAEA KIGAGARVLR DELYPIKVDS
VNKAAVLDEK DEIRAEAVAA FSEENEATVA KIAWLSRKDS AKAYGSMVVY LTKGTDARRL
LADGFFHAKG ESGVTSTFEY RPRPMQCYNC QEIGHKAFQC KNTQKRFRSA FHAGDLMNRS
AEIVGNSTHH DMNKTIRIIQ LNVRKQGAVH DSLMNDEDTR GAVALAIQEP QARRIQGRLL
TTPMGHHKWT KMVPSTWREG RWAIRSMLWI NKDVEAEQVP IESPDLTAAV IRLPERLIFM
ASVYVEGGDA SALDDACDHL RKAVARVRRD TGAVVEVMIV GDFNRHDQLW GGDEVSLGRQ
GEADPIIDLM NEFALSSLLK RGTKIWHGGG QSGDCESTID LVLASDNLTD SMIKCAIHGT
EHGSDHRAIE TVFDAPWSAP KHSERLLLKN APWKEINATI ASALTATPSG GTVQQKTDRL
MTAVSEAVHA LTPKAKPSPH AKRWWTADLT QLRHIYTYWR NHARSERRAG RKVPHLERTA
QSAAKQYHDA IRKQKKKHWN EFLADNDNIW KAAQYLKSGE DAAFGKLPQL VRADGTTTTD
H
//
