ID F2SUP4_TRIRC Unreviewed; 1786 AA.
AC F2SUP4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=PHD finger and BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TERG_06192 {ECO:0000313|EMBL:EGD89956.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89956.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; GG700654; EGD89956.2; -; Genomic_DNA.
DR STRING; 559305.F2SUP4; -.
DR VEuPathDB; FungiDB:TERG_06192; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_001514_0_0_1; -.
DR InParanoid; F2SUP4; -.
DR OMA; WVMDEPP; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04710; BAH_fungalPHD; 1.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR029617; Snt2.
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; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 310..428
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 625..800
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 1070..1120
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1178..1295
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1786 AA; 194850 MW; 4E65880D95C356D5 CRC64;
MAAAAAQHRG RDRDTSTTTT TTTTTTATAL LATTSSSSSS SAAAAKTTAM AAAAADRSKD
KDRGDMGEAA SSETASSATT PAPAPAPYST RSRNRPRINY AEDTELDAEL EKPLMAPVSA
SAAAGAGAAG SAATSNSTAK GTPGRKPKDR DAAAQTTSSS SSNTRIASPA SNSERPPGMS
TRRAAAVAAS NGTAAARDKN SESHGHAASA SAASTTTTAT ASTSAIPGTS TFSANPNTVV
VSSKKRKQPG SSTTVQNVVP ANGAGHPSKR FIAAGSRNSE EAVTTSMMTF RSSRAMLRNG
KLKADDGTLL APNDIDHVYL ICEPPGEPYY LARIMEFLPS KDNPSGPIES VRVNWYYRPR
DIQRKTNDLR VVFASMHSDA CPLTSLRGKC TIKHRTEIAN WDQYMKAKDC FWFERMYDRY
IHRYYDVIPT SHVINVPQHV KQVLDERWKY VLVEIGRRKE LTSAVKTCKK CQQYAANNDS
VDCAVCHNTY HMLCVRPVLQ KKPARGFAWA CGPCSRAQEK KLEARNTPMV GESRTNNDTE
PELVEEEEEE QPPADADTAA ATQRSSPANE LQQQQQQQQQ QQQHVLKPAT AEQISQAKLW
QFRYLGIHCR VEDALDYDDR IYPRASSRLG SRHQANVVPW YGHPVEYFKP AETKRKYVRS
GPKKEVKLSK EALAAQEADR AERASRPKWV QEVPPGYIAR GEDEPITVDG KKFHTAELQF
KMPDASQLSS VRGEDDAPGS HLSVEEREKF IDEYMDKAKE VATSKGIPDY STNYLDKALA
LLYEENFNVE PALARLKALH RYNDLKEPYL KPEEVKLFEA GVAKYGSELR SITKHVGTVK
HRHIVRFYYM WKKTPKGRQI WGNYEDRKGK KLAKKADSAA KLLDDVADDY DDSAFDNDKA
MEKRRGFTCK FCNTRSSKRW RRAPAVPPGF TVPAEQSGKR EKGNRLTVSL SPYHSESDVR
INQTTATIAA SIGVHVTTEV VKETASNPPE PQQQQNQHHQ HQQPAKKKTK TADKDANAAN
AVMADAPPPA PPPPQQQQQQ QQTSSRKRAA EKVVQEAPPP LAPEPPRPKV LPCAVCKKMD
PMGDQHLSCR DCRLTVHRDC YGIDASRPAA KWICDMCAND RNPTVSTSYE CVLCPVTETE
HELMEPPKTT HKKKSERERE KERLEREMVN EAIKLYRQRQ EAAGKPVGPR EPLKRTAGNN
WVHVICAIWF PEIKFGSAKD LEPAEGIESI SQESFKDRCK ICKTENGACV SCRASTCNAR
FHVGCAHQAG YNMGFDITPV KSSRKDVVST ATMGEETGVV APAIWCPHHN VQTIVHEMGE
SKGSTEGNAL QIYARTFKQA DLTLTGTARK AAYVQHSSPS GAGKRAAAAA MTNGVGTSTA
PTASLGQGQH QHDEVNGTWN AEQSNTGHGK DDIPKKCFRC QSVASPKWWR RAQPHQPPHQ
QQPVNGLGPL DLIRWPTSMH HANDTNGDIP DRIVYECHKC HLKKHLTPPT LTPVLAPLPP
VSYGPPDRDR EMGQTRHPEF HRNGYASSPH AQPVQAHGPA HVPPLAPLTH PHGAPEWRPG
PGPAPGPAPG PGPGPGPEYE QRPPAEYLHR KGISPAPNGH QHQHHQHPHH QHPHHPPPFT
NGGPPPPPPS LPPPHQYPYG PIAPHPSGAN TPYPGPGPGP STPGAGAGPA PGPSPMHFSP
PPPPSRTPLP GSHPPRMFPV DRPVQPKPNL SSPSAARRSL DPHQPQPPQS QSQAEPSPTA
GPTATPSRPR SESMGRQGSM GSMQPQSAPT SGSAASASPS LKNLLL
//
