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Database: UniProt
Entry: A1D6M0_NEOFI
LinkDB: A1D6M0_NEOFI
Original site: A1D6M0_NEOFI 
ID   A1D6M0_NEOFI            Unreviewed;       861 AA.
AC   A1D6M0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=PHD transcription factor, putative {ECO:0000313|EMBL:EAW21364.1};
GN   ORFNames=NFIA_065280 {ECO:0000313|EMBL:EAW21364.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21364.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS027690; EAW21364.1; -; Genomic_DNA.
DR   RefSeq; XP_001263261.1; XM_001263260.1.
DR   AlphaFoldDB; A1D6M0; -.
DR   STRING; 331117.A1D6M0; -.
DR   EnsemblFungi; EAW21364; EAW21364; NFIA_065280.
DR   GeneID; 4589813; -.
DR   KEGG; nfi:NFIA_065280; -.
DR   VEuPathDB; FungiDB:NFIA_065280; -.
DR   eggNOG; KOG1632; Eukaryota.
DR   HOGENOM; CLU_011451_0_0_1; -.
DR   OMA; CVNIDPR; -.
DR   OrthoDB; 124870at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR037869; Spp1/CFP1.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR46174; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR   PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          495..546
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          672..699
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        10..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  95452 MW;  B04DA69FF752DDB5 CRC64;
     MAGHATAPAE PSQVNGSIGL DPSTTNPYET NPELIPPTDP FLSRSPQYGR YAPHVDDFKP
     RYDGWYQAEP DATSYWEEIV RTSCTPENSM NVPGTREVYA AGSVLIKVDQ EPAAGAAAER
     YSNVNTNELS AARRAQDALQ ELDVAVPIIY FCGTIDGKNV TVESRIPGVS LEVAWKYLTI
     EQIGAFKQQC RRIIQRLAIV EPAPDSASYV CGELNSQSPP GVEDSERDIL FQDRKGTEQL
     HLVHNDMIRS NIVVKDGRIV GILGWRQCGF FGFERAKQIH RQFRIPERPV IDNGGVNVTQ
     VWADLYDDIP DVGGTNGLPD HHTAAAPEVK VEPLQPSLDK YPPSNEAEIL PALAQLDGTL
     LPEEHPTPRK VADLKSELAS RASSTDRSSP SGSTKAAGRR KPGPGASKKG TAKKQATKKR
     KIDELASEDA ESRRSNTPSS TRASKTPGIK KQGSVSVAGS PAPEGKKRKK SAKKAKVEKQ
     EEEEEPEEDS SEDDGVFCIC RKGDDHTWMI ACDGGCDDWF HGKCINIDPK DADLIDKYIC
     PNCKAEGKGW TTWKPMCRLK GCRKPARVTG KNPSKYCSDE HGREFMRRRI QQLNKTPGDP
     AKKEWEELGS RGGVLTTGDL HAVVMAVSSA EEFRKLGERI ISPPPDEEDP VTGARSSKKL
     GLDVDPEGLT YSHDEASKLE QLRKQREELL HRRDILNTRS TFMTLIRQRS KSIVEKLKQT
     DPKGGWKDIC GFDTRLAWSD EEFDDWRLSR LGAKALEEGT PEALASSYPD AVDADGDTAM
     NGTKTEDEDE DELAKLSRGV CTKKRCERHK QWVKVHQSEL LFEENKLKQD LATCEKEAQN
     VVERAVLRMW AEKENAQNGS E
//
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