ID A0A2H3ITL1_9EURO Unreviewed; 457 AA.
AC A0A2H3ITL1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Homeodomain {ECO:0000313|EMBL:PCG97986.1};
GN ORFNames=PENO1_060310 {ECO:0000313|EMBL:PCG97986.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG97986.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG97986.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG97986.1,
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 ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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:PCG97986.1}.
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DR EMBL; NPFK01000172; PCG97986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3ITL1; -.
DR STRING; 290292.A0A2H3ITL1; -.
DR OrthoDB; 5401018at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR PANTHER; PTHR24208:SF166; LIM HOMEOBOX TRANSCRIPTION FACTOR 1 ALPHA, ISOFORM B; 1.
DR PANTHER; PTHR24208; LIM/HOMEOBOX PROTEIN LHX; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 136..197
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 138..198
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 49517 MW; 8089BA502BBD895F CRC64;
MSLSSGAPIF APSAATPVKD CAASSAANTQ GDPSGATTLP KPVESGQFST QFASTNAFVE
RAAVQDEKGG VVSEQNRPAE SWGARSSNMS ASQTAQAGRE HENHGEENDE DLGEDFSNGE
EGDGGQGRSA GDGGDNSKKT KRFRLTHNQT RFLMSEFTRQ AHPDAAHRER LSREIPGLSP
RQVQVWFQNR TQMLQQPYSS RHSANTSPTS PATTRSSFSG PKPLAVNNIK RNPGDEYPIS
PASAYGNYVN SPALSEPFSP TNNTGHPATL PRVPGVHPPH SHEYNRSHSF SSSYAGWQYP
QRLHMPPSES GIKTEQTMNP LHRPTASYPG LAGTIPEGAP LPPAMAYQAG QPSHTNEQYP
PSTESAYHTP VGYRHVLSLQ TGQLPPPQEY QVSPFTPSYN FDSFYQYTHE NSSTVSLPAS
YMRSSQQSAY EPASGTYSYE NQDMSHRLSA TQPGGTR
//
