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Database: UniProt
Entry: A1CIG2_ASPCL
LinkDB: A1CIG2_ASPCL
Original site: A1CIG2_ASPCL 
ID   A1CIG2_ASPCL            Unreviewed;       828 AA.
AC   A1CIG2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   SubName: Full=PHD finger domain protein, putative {ECO:0000313|EMBL:EAW10667.1};
GN   ORFNames=ACLA_051390 {ECO:0000313|EMBL:EAW10667.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10667.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10667.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
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).
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DR   EMBL; DS027054; EAW10667.1; -; Genomic_DNA.
DR   RefSeq; XP_001272093.1; XM_001272092.1.
DR   AlphaFoldDB; A1CIG2; -.
DR   STRING; 344612.A1CIG2; -.
DR   EnsemblFungi; EAW10667; EAW10667; ACLA_051390.
DR   GeneID; 4703753; -.
DR   KEGG; act:ACLA_051390; -.
DR   VEuPathDB; FungiDB:ACLA_051390; -.
DR   eggNOG; ENOG502RATP; Eukaryota.
DR   HOGENOM; CLU_015602_0_0_1; -.
DR   OMA; ECLKPGH; -.
DR   OrthoDB; 1333597at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0031213; C:RSF complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15556; PHD_MMD1_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR028938; Rsf1-like.
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; PTHR14296; REMODELING AND SPACING FACTOR 1; 1.
DR   PANTHER; PTHR14296:SF3; REMODELING AND SPACING FACTOR 1; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 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   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          431..487
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          188..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          291..427
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        202..216
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..562
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  92834 MW;  5AE909E7A8760CA0 CRC64;
     MVSRKRTRSE ADAAPEQPAE EHGLLKRLRD CWEFACLMQF ITIFGHLMKI DEDFGIEDLE
     TECLKPEPSQ KLMEIGLCLL KWVSSHRGLT FDNFDEYTRR QYNAKAPHLP NPFGYDEAPN
     KFSEFDVFLK LRVLHQLTLW TFWNPDRIRE KMPQQKESEQ TEWRIEEVGY DREGRYYYVL
     DDNRLYRRTD PDIPPSKPAK AKPKSRSARA ARASKRRKVS TAAAAEESDG ENDKANDDIA
     NDPFKAMKWE CIAVTLTDYQ KFLDPIRKTK DADEKILRDT IVEKVLPVIE KEEEALERKR
     AKREKELFNL QLLAGAKRSG RLAQKAERER QEREAAEAAR KHEIDLAEAH KEEARLKKME
     EERRTRMMTR EQRIKDRERK RLLHEAELER IAKEQEKLER GESRASERHL KAELEKQRKN
     LEELQAEDQW IFDCSGCGVH GENLDDGSHS VACEKCNVWQ HSKCLGISQE AAERDDFHFV
     CQDCKRREEE SKFPKLPPLK FRLGSSPIQD HKASDIVDTG SSMPSTETGP ATSVTQMGSP
     SKPPRKPSTH EPSVPVSPSR PPSSPLKGIN GSTLPSRELP PKLPPLSQAT NLPPISRGFP
     NGGSSHSRRP SSSHSAQSTT LSSPIRNRPS MSPTQGNHDV GPLAGFPSTA PSDGSAPWTP
     YGQHQASRPD AGAHASFSSI PSGRPSFSAA TPGGSRSSPP QSSHGVPFSG ISPTKQSPRP
     MTSGSIAGAP VLPPIQRLEP SPKLMGRSSP DAPIPPPVKC MTPEQEERRQ REHAMMIQNQ
     SHAFSNGQHS AMSSPSLNRI PPLGPSALSR NIGPQSSTAR TDQKTNGN
//
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