ID A0A2T3ZNS1_9HYPO Unreviewed; 1229 AA.
AC A0A2T3ZNS1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M441DRAFT_63732 {ECO:0000313|EMBL:PTB46455.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB46455.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB46455.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB46455.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ679256; PTB46455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZNS1; -.
DR STRING; 1042311.A0A2T3ZNS1; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15670; ePHD_BRPF; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
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 434..484
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 488..607
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 768..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 70..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1055
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 135186 MW; AE46F331290A5A0C CRC64;
MAPTSPTPRR TPTGRRRGRP PGTTNAARAA RQASLAAAAA ASEPPPKRRR YVPGGPGGGG
RYLDADAIQT PDTARSNAGS RSRTSGAARL ALNGGSPLPP RRERSTRART AANEDSDEMR
WGSAAAMAAS VKQAEDYKPR EERSWEEFHP NLDIELPFVI FAADDVDGVV AQEAPNTPAL
DAPPPTTPHL DSMTPSKSVN PASTGNTPNP QATRSAEADA DDSAAGTPSR RPRRSTREVV
SFYNIRPLEF APTPRTPKIL PIQNQTPKER LDLKLPSYRK TNRIELFESK TFGQARYVDK
AMSNVGYQES DNFIRSERTL IKATDGNADD EFDQFSVAAG DDHVQQSRLG RVEYDMDEQD
DMWLEQYNAQ RKQNELEAIT REVFEITMTK IEKEWHALER RIPKPNPKPP QTHRPRSSSA
VAVNGEPHGG EEPDSKCAIC DDGDCENTNA IVFCDGCNLA VHQECYGVPF IPEGQWLCRK
CQLCGRGIPT CIFCPNTDGA FKQTNSSKWA HLLCAMWIPE VSLGNHTFME PVMDVEKVPK
TRWKLTCYIC RQRMGACIQC GNKNCYQAFH VTCARRARLF LKMKTVQGTL AVLDGSMVLK
AFCDKHCPPD HAQEYQVHQA TRAAKKFYKR NMRGRIWADN QAMANVIAAQ HRTAITDHPP
DESQMTGAKN LAILGDKKKG QAPKNLWKLP SGAPIIPQVV FDIVEASIQR FPFRKRKDYL
SEACRYWTLK REARRGAALL KRLQLQMESF SSMELTRRNF AAMGPSGKAR LARRIEFAQG
VIHELEQLKV LAEEIVQREQ LKLDAAELEQ DFVDECYFPT AKLLVPVVEK AIALDKGLFT
DGLADLQASI EKRVYVNVLG FAQDLGDVIS NGILTIPKNL ESAPHGSRGI EEEEAAPAPV
ADINSHNTST MAAQFADIRE RRKLGKRILK AVQPLLETSL QVESEISTKP SEGLQKELEA
LIDASIDIGR QVNGTAHGVP DDGAEDTIML DAPDPSSEPH ATVKSEPLAG ESGITSNDGD
VMDTAENDDD DEEEEEEDDD DDDDDDDDND GEGREEGDSI EVNTVGLGIM TNRPAVGLGI
TQEMAVKTAR VNSVITSETP PNSTGSFVVM AAPSQEGPPT PPQSNGSLGN EPSDPLSEGG
VLWYLRALEP HGTSILEEHW AAGRDAVRTL SEDLTDLDDE DFKDLGIDMG DTVTAAVMDA
EEPKDNSGSN SAKSKASRLR KRRASTRRR
//
