ID B8NFX6_ASPFN Unreviewed; 1483 AA.
AC B8NFX6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=PHD finger and SET domain protein, putative {ECO:0000313|EMBL:EED50643.1};
GN ORFNames=AFLA_134050 {ECO:0000313|EMBL:EED50643.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED50643.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED50643.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; EQ963478; EED50643.1; -; Genomic_DNA.
DR RefSeq; XP_002379419.1; XM_002379378.1.
DR STRING; 332952.B8NFX6; -.
DR EnsemblFungi; EED50643; EED50643; AFLA_134050.
DR VEuPathDB; FungiDB:AFLA_005746; -.
DR VEuPathDB; FungiDB:AFLA_005747; -.
DR eggNOG; KOG1286; Eukaryota.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_249535_0_0_1; -.
DR OMA; PNEDEHI; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43341; AMINO ACID PERMEASE; 1.
DR PANTHER; PTHR43341:SF34; TRANSPORTER, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 825..955
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 644..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 161273 MW; A47FA676455C0DB8 CRC64;
MVLSIDSTEE VATFKSICTA HIPLAPFECV RRILYCVDAL RPNARFSDRT PSYTIFTSDC
TMAIGPTLGT GLFIGSGQAL AAGGPASLLG SYIFISVLVY CVSTAVAEIA AHLPSQTGTM
VNHTYRYASS HLGFSLGYLR WFSIAALVPF EITNAMVNLG LWNPGARLAI RISIVTAVVF
FFNMLPEKAF KRSEAAFTAL KLVTTIGLII ISGYLAVRGV PESAARGFRY WHEPGAMNEY
LTDGHLGRLL GLVQCILCST ISFIFSPELI VQRAEQVDSE SVRNALDMTR IDCFHLFALY
ILSSLAITVS SPSDEPLLTN HGIGAGLSPY IVGIRRSGIP ILPTVATALI FLSSVASGRS
FLYISSRTLC SLAETGHGPE LFKVRNDYGV PYISVIISAL FSGFAYLSLA MSASVVFNLL
MYFITTSGYI SWLFSCVIYF QFRRTTALQG FTPANQTRIQ PYGAYFGIAA CTFLPLANAL
LLAAPSWIVA RNSIPAYIAV SIFLLLYFGH LMKSIVTQRR LQSEELRKQG CGDMLEKCTA
RPQGSTVGWR GLTSQAVPQS GSYALDPKVG VATEPYPVTV SLNSPAVNGA VSDSAAPEEE
EPYTIKCICA FEDDDGNTVF CEGCETWQHI ECYYHGRDVP EVHNCVDCEP RPLDGRRATE
RQRRLREQSD GGDRKAKRSG TKSQKKKTKD GEQVNGTHNR SESSTRDQPP AKKAKTNHRA
SGSVGSLAGV PSLPPDSRKR TTTSMSPTKP SGPSIPLYSN EFLHLYDQDN HHVDTDSNLF
VNLELATHLA TWVNEPGALA RASNGRSAQD VFTWSGGALD RSHWPSLATE TIRDANVDID
GIHPTWKILK TRDPVRKDEI VGEITGKIGP LWKYCVEASN RWQELRHPEP FVFFHPQLPL
YIDSRHEGNI LRYARRSCRP NVTIRTFITN EVEYHFCFVA KEDIAADSEI TAMWYLDPQL
FESTNGVVKQ EFSDNAQDVA AMCISNVLSH FGGCACVAPP NCLLANVDRR RHPKALDTNS
KQTSSKRKKT KSKSNISPPA SNSRAGSEAT KNLEEDDQTD TLSTSGSARG QTRSRDLTPT
LQTSTEGVVF GEAELSARDK RKIAAVEKKF QQLEQDQQAS HRRKKRASGQ STQTTPVIGS
ASAQASYFTH LSGRDRQSHS PTSAISPGSL PGGRHGSPRK ASNHGTPSLR SRLGRPQYVD
SATQTELDVC DSPSPSTTPS RRPNFVPFTQ RLLKRCYADR IRLEKSSQQF FVSPSSQSKH
ATHLMSPVSS PRAGPLTVTT PSVTGDRDDM EMKDAVSPMG TPGWQQETSP LSGRSSIKPP
LPPPWPSTAA HNSRIPGGKG NSHRVDLRVS LPATIPSLPP ANSPGSGAPA VISSPSTSDT
AIPGSSVTAP SPVKKKLSLG DYLIRRGTLT TPTSEKSQTQ ATPMPPPKSP TTQPHMNREL
STVGNNEHAQ PRAIGEGGST KSSDVPMKDV SGPTQASQLS SLS
//
