ID A0A421DB53_9EURO Unreviewed; 1729 AA.
AC A0A421DB53;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=PHD type zinc finger protein with BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CFD26_104546 {ECO:0000313|EMBL:RLL99303.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL99303.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL99303.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL99303.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:RLL99303.1}.
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DR EMBL; NIDN02000034; RLL99303.1; -; Genomic_DNA.
DR STRING; 1245748.A0A421DB53; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 75..116
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 163..256
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 462..512
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 604..770
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1336..1385
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1729 AA; 194451 MW; 9789E337326C83AB CRC64;
MVAPASTGAI STGVQPPANR QPTRSSSTHP SHSHNVPLSA RRSAPLDLST VERRGQPNAP
REPSKRIRPH GLQEAPTFRP TEEEFKDPLE YIRKIAPEGK KYGICRIIPP ENWQPPFAID
TERFHFKTRR QELNSVEGGM PPRSATSAAG STPQPSSDPD SGTRANLNYL DQLAKFHKQH
GTNLNRFPSV DKRPLDLYKL KKAVEIRGGF DQVCKMKKWA EIGRDLGYSG KIMSSLSTSL
KNSYQRWLQP YEEYLRVVKP GVQQQLELEH GGPYTPSPNQ SPMAKKPVLY DHISPSATPQ
APPSIPAAGG LQGTPKEIEA TPDKPTPPVE SAPPRPVTSG FTPVNAGGGG FTAVNRSPSF
VAVNSGPVVK KEAENGSLTP QSVAEHPQSS TPVPNGNGSH PMKRAISHES GSQTEGGETD
GSGRRSKRLR KDAPPPTVAG SHMSLLRPAP PRTRKSDSRK IGDKCEVCGK SEDRPSILVC
DSCDQGYHRN CLDPPLTTIP EYDWHCPKCL VGTGEFGFEE GGVYSLKQFQ EKANSFKKNY
FASKMPFDPV LNTHRRESED DVEREFWRLV ESLTETVEVE YGADIHSTTH GSGFPTIERN
PLDPYSTDPW NLNVLPFHGD SLFRYIKSDI SGMTVPWVYV GMCFSTFCWH NEDHYAYSAN
YQHFGATKTW YGIPGSDAEA FEEAMRQAVP ELFEGQPDLL FQLVTLMPPD QLKKAGVNVY
ALDQRAGQFV ITFPQAYHAG FNHGFNFNEA VNFAPADWEP WGAMGVERLQ AFRRHPCFSH
DELLLTAAAR DTSITTAKWL GPALQRTCHR EVADRAAFIR RHREIAPHNC AVGSSDPSAS
GECQLKFVVE EEDLPEDDYQ CQYCKAYTYL TQFRCHKSGK TVCLLHAETF DCCGDSPSQR
LLGPDHTLRY RVSDDTLKAL VQKVQERARI PEAWGQKLDK VLEDEPKPQL KVLHSLLSEG
EKIPYHLHGL QDLAAFVQRC DKWVEEATNY ITRKQQNRRK NEKAWRKSTS KAAQLEERDR
EVRRIENMYA LLAEADKLSF DCPQMAALEE KTREIEKFRQ DVNVALMNPH IRSIQEVEEL
VESARNFNVE IPEVEGLEHV LRQMRWNDEA RRKRDQYMTL KECQELVQAG EQLGLSETNE
HLNHFKELCR HGETWEAKAK ELMSVESVHY QQLEALSAQA LRFPVSPETL SAVDAILTKQ
REAQKKIQSL YERSKNPDFR KRPKYKEVRE LMESLEALNS RPTGAIDLER EQKRHEDWMR
KGKKLFGKAN APLHILKSHM EYVEKRNSYC FDLEDRCRPP VEPSSRDNTP DGLLENHTTT
TTTASMWGGG KSRKRDVFCI CRHSEAGMMI ECEVCHEWYH GKCLKIARGK VKEFDKYTCP
ICDWRQKIPR DAARPKLEDL QDWQAEIPGL PFQPDEEQIL ENIINQATTF RDFIQNFTNA
ACTTTEEVPT LIFYLRKIEG AEVLLAYETN FFRQEIHKWA PVAPEPPPIL EQSLSTRKPR
PTKQQKIMAQ LGVERPEDLP PHLRTKQPNH TKRKSLDSQT PRPASLQPTP HTSGEDSNRT
GPALTPMTDA QNPPYPFSAN YSLPASDSTP AFAPGPSAFL PHVSAHSPSF PPRSPSPHHG
LDSALFSSPR FSRDPTEGPP GVDVGNQDPF DSSPRHNLDD VFADLTNQDA EPEPEPEPME
NTHANEALEA LNASNGGDHS DATQDDDSHD TGVDGDMNGQ ADEDTAESS
//
