ID W9XDC2_9EURO Unreviewed; 1131 AA.
AC W9XDC2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=NuA3 HAT complex component NTO1 {ECO:0000313|EMBL:EXJ78218.1};
GN ORFNames=A1O3_09379 {ECO:0000313|EMBL:EXJ78218.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ78218.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ78218.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ78218.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ78218.1}.
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DR EMBL; AMGY01000009; EXJ78218.1; -; Genomic_DNA.
DR RefSeq; XP_007737663.1; XM_007739473.1.
DR AlphaFoldDB; W9XDC2; -.
DR STRING; 1182542.W9XDC2; -.
DR GeneID; 19173463; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_002663_0_0_1; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
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 405..455
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 459..577
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 126552 MW; 4524F0D288AEAA01 CRC64;
MGPLRNVQGR TRPRRETKNT ASVFDDSERD DLADFQDVEP PSKRIRTSRK AQLPSKWIPG
GRGGGGRHVD KEGTPSATRT PRGKNDYALP RTRPRTSRDR RRTMTSTPRY SARSRNRGST
RPRYSTAAAA SAAVAHGDGY KPREERGWEE FHPDLDLEAD FAVIPSEEID GLVKKPTMNG
TPEEGGMSTD GVTATLGSAT PPKRRPGRPH RTHNSMVNAL LTPEAPKLVP VPGPNPRERL
TLPKPSYRIL DPFVSYEQKD FAQVDFVDKS MANVGYQESE IFLRPARNYI RQTEGSAEED
LDLSPDLITN GENSAIGSSG VGRVEYDMDE QDVKWLESFN RGRIKDGVQT IKPAIFEITM
TKIEKEWHAL EKRIPKPNPK APQTQRPRSS SAAAVNGEPA GEEPDSKCAI CDDGDCENAN
AIVFCDGCDL AVHQECYGVP YIPEGQWLCR KCQLVGNSRP SCIFCPNEGG AFKQTNNSKW
AHLFCATWIP EVTIGNPSLM EPITDVEKVP PGRWKLVCYI CKQEMGASIQ CSDGRCYEAF
HLTCARQAGL YLRMKTGGGQ NTLMDTSQLR AYCHRHTPAD WKYEHNTDRA YEEATKYFKE
HFRGQIWADS RASALAINDT HDIPNTDRGH LKVTLTNKKG QKQKTIWRLP SGAPVIPEVI
LKSIEDSLVR FTVQRKKEFV SEICKYWTLK REARRGAALL KRLQLQMDTF SSFEVTRRDY
KAQGAAGRAR LDRRIEFAER LADDMKRIVQ LCDLIKQREA LKLQEALMLK DVVDTVYFPI
PHVLEAIVDK ALKLDRGLFR DELLKLRTRV LRKEHTSVSS FAHDVVSVIN SQFGNDAGNL
SELVALVSGR AEDMSPEDRD RRTLARRIVK AIEPLIDDAG RKEAELNGRP YAQQIRELDE
ALVSRRDSLL AESFGMPVLD SVEPKHETGI ASPEDGDVEM MDSAHPTNES PVDHETVEVI
KDVAEKADLF KQDGLRVEVN GLSVDTPPAS TNGFRHDHLT NGDIVMGEVQ RIEPPTPPMS
LQGHSQILSS QGGIPWYATP FDPEGTTIFE ERWTGPEVLR EMSEELSEMD EDELQGLGAG
DDMAEATDGA HQALEAERTS TDSAAKKRIP KKAGKRGRSS GWSARTFRPR R
//
