ID A0A2H3IIP7_9EURO Unreviewed; 968 AA.
AC A0A2H3IIP7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Zinc-finger domain of monoamine-oxidase A repressor R1 {ECO:0000313|EMBL:PCG92877.1};
GN ORFNames=PENO1_086330 {ECO:0000313|EMBL:PCG92877.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG92877.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG92877.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG92877.1,
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PCG92877.1}.
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DR EMBL; NPFK01000341; PCG92877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IIP7; -.
DR STRING; 290292.A0A2H3IIP7; -.
DR OrthoDB; 1387875at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR PANTHER; PTHR12480:SF6; 2-OXOGLUTARATE AND IRON-DEPENDENT OXYGENASE JMJD4; 1.
DR PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000313|EMBL:PCG92877.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000313|EMBL:PCG92877.1};
KW Zinc-finger {ECO:0000313|EMBL:PCG92877.1}.
FT DOMAIN 154..334
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 538..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 110781 MW; 2E1FA3D021EE5D32 CRC64;
MPAQRPQAAF EPIPPNIDVP ALVESTPNFE WVIRIHCDAI YEQGLENFEK LVRLHVITGG
KPLVVEGYDS RFEKWIFAEQ WLRDNLSSKA ENARNLTAKT NIPLSIGHYL SNMPMLAEQI
TPQNFTEPTR QRIYLKDIDC PDVWHEKLKD IIPPFLFYMN ESTLDPDVLS SQDFAKAGDL
MSSLPGPMRA ENLMCYIGHE GTYTPCHQEM CATLGHNIMV ETSTGSFEYG KRTKPGSSIW
FMTETKDHHL VSEYWSSILG HDIDLEDHFA QISAWKAAPF TTYVVEQRAG DFILIPPLAP
HQVWNRGTRT MKVAWNRTTV ETLELALEEA LPRARTVCRD EQYKNKSIIY FTLDKYSGLL
AAAERLNTKT TKVRQLQKDF RKLYTMFTAI MLSESFSNEF PEEKRVEFLP YDSNVTCSYC
RCNIFNRFLT CPHCVGKFAS GEDDCYDVCM ECYAMGRSCG CISNLQWVEQ FPWQELVQKH
ETWGKQICRM QNLREDKYSS LTTERMRLGH RTLAEVCQLE LKRRPWVDIT KHTFDEREGF
DSQDDEDDQG SGDERRVKKR KVHPRDKLSK EHARCHICKT LEPTWKLASC QTCSLHYCYG
SLFRAFEIKP QEPMQTYRWE CPRCRKICSC GACRRKFTTQ PYEPKGLALG HDTKKIADPR
SVEALVNFSH SNIGWLKKAG DGTADSTRRL QRHQAEAEQA KMQEAFAFQD DDALFVQQPM
QNGYSNAEPA FHDGIPIDPA LGGPPTAPAH NFDIYDPSVH LPELAARVHQ LTQSSAVQGL
MRSEEEMFRD AAAIRFEMPS GNGLPIDLTQ DITTDGHASY AIDPSLLQST NGGENGALPR
AANHIPVVQS KSRPRKMKSK LVVRLRLGQE HMHAIAQTYK DQPTPNTTMI ITSDILTFHS
EPLPTPENPK KKRRRGEKDD DFKVWRKGRN PPRTSDTDHH AENGDKRRRA ARIANYYEDS
DLELSDGV
//