ID A0A2H3IGH6_9EURO Unreviewed; 451 AA.
AC A0A2H3IGH6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE SubName: Full=Zinc finger, HIT-type {ECO:0000313|EMBL:PCG92932.1};
GN ORFNames=PENO1_086120 {ECO:0000313|EMBL:PCG92932.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG92932.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG92932.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG92932.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(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:PCG92932.1}.
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DR EMBL; NPFK01000339; PCG92932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IGH6; -.
DR STRING; 290292.A0A2H3IGH6; -.
DR OrthoDB; 2029831at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR InterPro; IPR039723; Vps71/ZNHIT1.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR13093; ZINC FINGER HIT DOMAIN CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13093:SF0; ZINC FINGER HIT DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..447
FT /note="HIT-type"
FT /evidence="ECO:0000259|PROSITE:PS51083"
FT REGION 168..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49370 MW; 381C7E1FDBD1F497 CRC64;
MSTMLRPVIS SLRAGRVLAT SQAPAMFSTS SHLRTDISSS ALPKQRPVGA FRGGLFGFLL
GSVAAGVSVY YYILKEYRVS NELLTEDIYH HEDDIKTNNA NIALPTSIHP PSRPPTNFLP
HPINKVIINI TTQPNFDTKM PLVEVLGTSR SHATPGWAYV PETALQKSST TLTTSRKRGI
REPGRTGTDL TSRQNHATIR HLAELDRENH RDNVHIPVPV RKDAIQRDNG RGARAKTTSN
VRRIMQSQKT FKNYLDDEEA ALAHSTATTT GGVAAVPVVV GAAAGVSKVA RVAARRSLTP
AVAAASSTTQ DTLTERQKRA LARKTTSTDT PATKKQKSER TNEEVHGDDM QIDTPEQIQE
GLLKTPHDND HLLKSYIPLP PSDRLMAALL AEPPLRYHAA RAAPSATNKP ARQFCTICGY
WGKIKCKNCG VRTCGLECYK VHEDSRCGAF F
//
