ID A0A2T3B8G4_AMORE Unreviewed; 1637 AA.
AC A0A2T3B8G4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=PHD finger and BAH domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M430DRAFT_48750 {ECO:0000313|EMBL:PSS23160.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS23160.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS23160.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS23160.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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DR EMBL; KZ679008; PSS23160.1; -; Genomic_DNA.
DR STRING; 857342.A0A2T3B8G4; -.
DR InParanoid; A0A2T3B8G4; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000241818; 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 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; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 202..320
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 357..409
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 505..680
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 690..735
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 968..1019
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1070..1207
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1637 AA; 179537 MW; 3D81C89D010D15C7 CRC64;
MTASNSNSSN TPANDVAGSG TGAAVPYGTR SRNRTGTSRP NYAEDKELDV DFEVTVPAKE
NKESNGRKTT RGGSDIGSAS LETGRAVGTT RKTGPDAGHF VTVQSHYKDP IPGTSTFSAN
PTVTTVTTQP SKKRKAASQS STPAAHSQAQ LSNHGASADH AAARKASMAT QVMAGFRATN
MLSFDNCGAR LEGGKLRADD GTILEVNDHV YLVCEPPGEP YYLGRIMEFL HINNDNTQPI
DALRLNWYYR PKDIGRKVND TRQVFASMHS DISPLTALRG KCQIKHKSEV EKLDELRKTQ
DCFWYEKLYD RYIHRFYDVI PTSQVINVPV EVKKVLDERW RYIVVEPGRG KELTSAVKSC
KRCNKYCASN DSVDCAVCRN TYHMSCVNPP LLKKPSRGFA WACGPCSKAQ EKKLEARNTP
NMTDSVADPD DDDLMDEDDD LPSVPEDPPE TEQTSPTRSS EVEVSIHPGT AEQVHQASLW
LFRYLGIHCR VEDALDYDDR IYPRASSRLG PRHQANITQW PGRPVEYVKS ADVKRKYAKG
GAYKKDTKLS KETIAALEAE KVAREKRPKW VMDEPPGYVH RGEDYDSDDP NSTSKLLFQL
PEVGEKSVDR GQDADDGGSE HLDFSSREKL VHDYMARVKK LAKPLGLPEF STNLLDVGLQ
MLRTHGFDPE KALQALQAVD KKTFKEPELS PAELKRFEDG VAKYGSEVHS IKKHVKSVSA
GDIVRFYYTW KKTERGKQVW GNYSGRKGKK EAKKAEASTG KLQDDVADEH DDSAFDNEKA
FEKKRGFQCK FCNTRNSRQW RRAPNTPAGM MVTENTNGKS SGKEKGPQLM VALCWRCAEL
WRRYAIQWED IEEVAKKVAQ AGGRAWKRKI DEELLKELVA ANEVMNQAAN GPSIGSTPAG
GTPVPTPQNI PAGAEPPRKK IKGTLEIEFA EPQTDSGVVA TTGPQKKKAS VEKPSAPPPA
PELPKPKILP CAICGEMEPM GDQHLSCRDC RMTVHRNCYG VVGENRSPNK WVCDMCSNDK
NPQVSVQYKC MLCPVEYTEQ DFVEPPKHAH KKRNDKDRER DRVERENAQK AADYFRKKQE
EMNKPVNPRE PLKRTANNNW VHVTCAVFTP EVKFGNAKAL EPSEGIPLIP SARYDEICKV
CKQKGGACVG CHSCRAPVHV ECAHQAGYIL GFDIIPVKGS RRDQFNIVNI NGEVGTMTAA
IWCKEHLPAK TVVHRMHDVV DDTGLNALQL YVQNFKQADL TLTGTVRKAT LVNQSTKAVN
PVPSSALPAN RRTSTTAASS GPSLPGRGSV SHVKVEEGRG EVGLAVGGEA EKICVTCGVD
VSPKWWPCSP SPRDSTPAAP GSLCNGDYAH ENEPSVAGGS VLQPPGAENG SGHVALAAAA
LHQNGHQPAP TSTEFQCHKC HWKKIRKEPT PIPAALPPRD TSRPLIPPSS ASASSPDADV
VHPPYAWPHP PPYQSNGPYN NWSRQSPAPQ GVALVNQLNG NRSPRIGTGT VPQLNGQPPL
RQPVPPVQPV SHSPHQNGHI TQTPNGYPPS PHHSIGPTTL HMQNGPYSSF ASTRPTPQHL
TNGGPPPRAP EHPFSQGNAH MHHRASFGPP LQGSPPMLHE SHPQGRDLGS QQNGTRPNDG
RVNGGASASP SLRNLLS
//
