ID A0A135LC90_PENPA Unreviewed; 876 AA.
AC A0A135LC90;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Zinc finger, CCCH-type {ECO:0000313|EMBL:KXG46585.1};
GN ORFNames=PGRI_054410 {ECO:0000313|EMBL:KXG46585.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG46585.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG46585.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG46585.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(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:KXG46585.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHQR01000069; KXG46585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LC90; -.
DR STRING; 5078.A0A135LC90; -.
DR OMA; YWREGKC; -.
DR OrthoDB; 2729045at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46557; SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10-RELATED; 1.
DR PANTHER; PTHR46557:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10; 1.
DR Pfam; PF18345; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
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 849..876
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 849..876
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 98..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 96705 MW; 3FF012175C617509 CRC64;
MLQNTIDLTN DYPDSDPNVT INPQFLNSTP QAFSQQQSSL ASNFLQGIPA DFQRQGSEQA
RLFNYYQHDL SVQSHMTPNG NPVLSPRGLS VPEVVITNKK GAHNNQQTKK TGQTRAVSIS
ESESSDESDL EIEAPDEPSP IPAVRPTEPE AAAQYDTLQA VWSPRNKWPG TDKIKNAMVA
YKDLVKSLRD AWKEQVQAMK LAENQDDNQK ATKLKEKVIS QRRTMDKIAT TTLEMGHPII
VEKLGEHPMI VAALYSFLVD RFQAADFAGT LTINLLTLFS RFSSLTEDLM QKTNLSKLLP
KFLKKGSQQV KDLTQKILDN AAACTKRKQE SEKPAKEESN PKALLADQSK GDAGVKRPRE
ADSNLQPGAK RMAVANTLKD VNKLTSGNGQ AKGAQSSKPT GAAVLRPKPN IVAPKPTSLF
GTLSSASKRP GTTNADRAAA AAAAKPTAAP EKEKASAFKP SFSFGDIMAD LSKPKQAPTP
KPAEDQPPET EAERTKRLRK EERRKLRVTW RPDDTLTEVR LFTHDPDEEL GPGDGSLRSR
GDVKGEGSVL KLHKDMDELE EEDLGGIRET IFQDGYILSM IDFDFEEPKD GSFVKRGGPQ
LPTSPEREAQ EHREATTLMV FYTSPADMPD TPKEPPAPDP DEIVPEVLPF GELPDMVKVR
QERYYSYMNP KPAPTQQPQQ PTPGDGGFDI SNLLKIIQGV PGQVQPVPPI QATQPGVMPD
LERTINMFRQ QQPQSQIPPP PPVPTSQPQG LDFNAILNVM KQMQTPAAYS QPQQSHPAMA
PNLGAMFAQF GGQNQQAGAL PFQQHGHDYE DPERKRGREG GYYDDQSNSE SWSRSKRTRV
GANEAKPYKV GLVACRFWAE GKCRKGDNCT FRHDPL
//