ID A0A2T4AP14_TRIHA Unreviewed; 1633 AA.
AC A0A2T4AP14;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB58760.1};
GN ORFNames=M431DRAFT_503713 {ECO:0000313|EMBL:PTB58760.1};
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:PTB58760.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB58760.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB58760.1,
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.
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DR EMBL; KZ679676; PTB58760.1; -; Genomic_DNA.
DR STRING; 983964.A0A2T4AP14; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000241690; 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; cd15497; PHD1_Snt2p_like; 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; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
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 SMART; SM00717; SANT; 1.
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; PS51293; SANT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 230..348
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 385..437
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 570..670
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 680..725
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 947..997
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1055..1187
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1026..1058
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 179316 MW; C703B626EFC9D822 CRC64;
MVQPTDSKSA EPEANPTSEP MAKTSPGSGA AEKDTVIDVA MPYGTRSRNR TASSRPNYAE
DKDIEMDMYD YYPDKKDSDS GKKSSRQMNG ASNGDAPRSN GTSRKNAAAA AAAAAAAAAA
DDTKAGPGQN GTQDSKSGGT IHASQAASGS GTSQPSRKRK AAANQNGTAA ASTATSAAAT
PPATSAAAKK NALAAQSQLQ GMTWPESNML TFETCKGMPD NGRMVADDGT VLEANDHVYL
VCEPPGEPYY LGRIMEFMHA SNDTARPVDA VRINWFYRPK DIGRKASDTR MVFASMHSDI
SPLTALRGKC EIRHRLEIEG LDDYRRRPDS FWFEKLYDRY IQKNYDLIPT RLIVNVPEKV
KKVLDERWKY VLVEQGRGKE LTSAVKLCKR CSSYCASNDS VDCAVCLHTY HMNCVKPPLL
KKPSRGFAWS CAACSRAQER KLEARHTPNT IDAGDAEDDE PLDEDEEDVH GVETERTSPG
DDEAPHQGTA EQIYQASLWP WRYLGMHCKP EDALDYDDRI YPRAGTRIGP RNQASVGPWP
GQPVQYVKPL EFKKGGKKDQ KLLKEQQEAE RARRGQRPKW VQDQPPGYVA RGEDLDEDDP
NCTAVLLWKP PAGDDPSTAK INSFVDDAMS KAKQLDLPER STNLRDAAVE TLYREDFDES
KALTVLSKKP RIEFKEPNLS PAEVKRFEEG VSKFGSELHL VMKHVKTKSP GEIVRHYYAW
KKSERGQQVW GSFPGRKGKK QAKREDAAAS KLADDVANDD DDSAFDADKA VQKKRSFICQ
FCNRTNDRQW RRAPNPLPGL VNDQGLKGSG KDKAGNQYVV ALCRRCAELW RRYAIRYEVI
EEVAKKVAQA GGRAWKRKQD EELLKELQLA QELGYMTPER APTPSKAASQ PLETQEPPRK
KLKAAADKEA DATPSDSGST TSAVPAKKKE KAVVEPPAAP EMPKPRILPC AICDQMEPMG
DQHLSCRECR LTVHRNCYGV IDHKVQGKWV CDMCANDKSP QVSIQYKCVL CPVEHTEHDF
VELPKLTHHK KKMSEKDRER EKMEVQQARK AAEFYRKKQE DMNRPVNPRE PLKRTADNNW
VHVTCAVWTP EVKFGNAKAM EPSEGIPSIP RSKYDEICQA CNQQGGACVP CHQCRAPYHV
ECARQKGHVL GFDIAPVKSS RRDQFNIVTI NGESGTMSAV LWCKDHIPTK TIVHRIHDVA
SESGLNALQL YVQNFKQADL TLTGTVRKAT LMAAAAKLSG APIQPGNRRA STTTTPNGNT
WAQPRNGEVV DPGSNAQHPG EKVCITCGID VTLRWWPIDN SQERKLTNGH HGVIGSEAQK
FVEQRKFQCH KCHKLRKTPR SPRLTLLPGP SPPPPELARP QPMETSLMTP VPPMTGSTPP
PLVDYRDGRH SSHPLSWPQP PPSHAMRAGS TPPSMPAPVH APAQVAGHRP APVYPPAPLP
PTRPPAYGEW APQRPGSQHG SPPRHLNGGP PPPILHSAPP PPPISNLSAL RPPAMAPTGM
PGSHPHGHAY GNGLPPSPRR LNGPTPPAPY VPPPYHGHTG HGGPVHPPAH LMGNGAPPPP
PPPRADAFSH GLHPQRSSYP PTPHASAPIL RNGPPPPPPQ SHEPPPPPMG PRPPENRPAT
GASTNPSLRN LLS
//
