ID A0A2T3ZZI9_TRIHA Unreviewed; 1242 AA.
AC A0A2T3ZZI9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=M431DRAFT_512428 {ECO:0000313|EMBL:PTB50225.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB50225.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB50225.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB50225.1,
RC ECO:0000313|Proteomes:UP000241690};
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.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
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DR EMBL; KZ679689; PTB50225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZZI9; -.
DR STRING; 983964.A0A2T3ZZI9; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000241690; Unassembled WGS sequence.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd13292; PH_Osh1p_Osh2p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REPEAT 181..203
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 288..320
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 379..474
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1154..1184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 137814 MW; 802407F2D0BED1BB CRC64;
MSDVGESNHH KRSKSAAALS LLRRKDTRED ESGTEDDRLS TTGSHASPPK HATSAPRGHS
SRLSTPSAVL SRTPSNNQTA ASIKGSPIQD IKTGSLEQSV RKFRVVEALR SGDTASISKA
IRETADGVPR ASMSSLSGAS AGALEDTTIL HLAMQCAEFP VIEYVLSDGL GSLDVNSRDK
DGNTPLHIAA MHGRTQAVKL LLEQKEINDA IANSQGKLPI DLARTPEIFQ LLQLSRSMFT
DTKVQQIQDL IAKSDYDTLA QVLEEQRLKT MLDINSTEFV SDPAVAQAGG TLLHEAAKKK
NIQLIQVLLL HGADPFRRDR KGKLPQSITN DDNVKAILKK SPAAVAAQRG IQEKAVLGHA
ASQNATTGGP ADPLAGREAR EMKGYLKKWT NYRKGYQLRW FVLEDGVLSY YKHQDDAGSA
CRGAINMKIA QLHMSPDEKT KFEIIGKSSV KYTLKANHEV EAKRWFWALN NSIQWTKDQA
REEERQAARS AELLRIAKAD QSGSVSAQDS HSENTSMTDL RRVSTQLQAR PILSVKKSDM
TGTSIGSVDE EDFVDTYTEA DAMQGHEHPA GPGTLPGDGD DDDDYGEETS GREEPQATKD
ALNITAQSAK LQLETMGSVH SALMAELTRS PATTLSDTKV TQALSTYDAA IRSLTALVGD
LLRISKDRDA FWQYRLDRES NMRRMWEESM AQVAREQEIL EARVGESEMK RKLAKKALRE
VMEQGALPSA SVTPTMERVQ EEVEEVEVIV KAATRGLPRK PTALEQMAEL SDSESGVEDE
FFDAVDAGDV EVTEMPPSDT KQEKKDVVIS GIDISSSFSG YENGIRHKLK MESDDRPKIS
LWGILKSMIG KDMTRMTLPV SFNEPTSLLY RCGEDMEYVE LLDLAAERSD SIERLMYVAA
FAASEYASTI GRVAKPFNPL LGETFEYVRP DKNYRFFIEQ VSHHPPIGAA WAESPNWTYW
GESHVKSKFY GKSFDINPLG TWFLKLRPTA GGKEDLYTWK KVTSSVVGII TGNPTVDNYG
PMEIKNWTTG EVALVEFKAR GWKASSAYQI VGKVMDASGQ VRVSLGGRWN SRLYARLTPG
YEAAVDEPST KNKDIVHRGS IADPSRAYLI WQANERPAGI PFNLTPFVLT FNHIDDKLRP
WIAPTDSRLR PDQRAMEEGE YDFAATEKNR LEENQRARRR MRENAGEEFV PAWFTKATCE
ITGEEYWQFN GKYWTQREKA GPDGDYEAAW GGLEPIYDDI PA
//
