ID A0A395RPJ7_FUSSP Unreviewed; 1556 AA.
AC A0A395RPJ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Lid2 complex component snt2 {ECO:0000313|EMBL:RGP62066.1};
GN ORFNames=FSPOR_9524 {ECO:0000313|EMBL:RGP62066.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP62066.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP62066.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP62066.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP62066.1}.
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DR EMBL; PXOF01000153; RGP62066.1; -; Genomic_DNA.
DR STRING; 5514.A0A395RPJ7; -.
DR Proteomes; UP000266152; 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 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); 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR034732; EPHD.
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; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 207..325
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 524..623
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 899..949
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1007..1139
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..438
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 829..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 978..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 171721 MW; D8438E8028935A81 CRC64;
MAQQNDSKVS DPEAQSVSDP MTSQSGLDSA AKDASADAAS GYGTRSRNRN GSSRINYAED
RDIDADVYDY YHDKKDGDSK KTSRQSSAAV NSDAPRGGAS SRKAVIDESK PAQSANATKE
QQSGSSNNAP TTTLPPAASS QPTRKRKVAG SSAGSTNQAT SNTSNTTKKA TTSGTAAGIS
WPETNMLTFE NCKGQPVDGQ MIADDGTVLE PNDHVYLVCE PPGEPYYLGR IMEFLHVQND
NSRPVEAIRI NWYYRPKDIG RKSTDTRMVF ATMHSDISPL TALRGKCQIH HKAEISNMDA
YRKTSDSFWY DKLYDRYIQK NYDLIPTRSI VNVPANVKKV LDERWKYVLV EQGRGKELTS
AVKLCKRCTG YCARGFAWSC AACSRAQERK LEARNTPNVN DPTLDADDDE PMDEEDEEMQ
GVDTSRTSPE EGDHAPHEGT AEQIYQASLW PYRYLGMHCK PEDALDYDDR IHPRAATRVG
PRNQATVLPW PGQPVEYVKP LEFKKNGKKD TKSKEALAAI EAEKISRVNR PKWVQDMPPG
YTVRGEDHDE DDPNCTAKPM WIPPFEDVIK EKDINQYMEK AKGMAKDLGL PERSTNLQDV
AADTLFHTGF DTKRALKALP EKDKAEFKEP ELTPSEQKKF EEAVIKYGSE LYLVRKHVKS
MYYGMVTRYY YAWKKSERGM QVLENMAGRK GKKEAKRAEA AANKMADDVA DNDDDSAFDT
EKANQKKRGF VCQFCSTTSS RQWRRAPNPI SGVVNDSSSK NSNKDKGQER VVALCRRCAE
LWRRYAIRWE DMEEVAKKVA QSGGRAWKRK QDEELLKELQ AAKEMGMMTP ERAPTPSATP
AAVASAQEPP RKKLKGVPLD KDADNGHSDT ASAAGSTTSK KKDKSVESVT VPEMPKPRVL
PCAVCGELEP QGDQHLSCRE CRLTVHRNCY GVMDNRNPGK WTCDMCLNDK NPQVSIRYKC
VLCPHEYTEH DFVERPKLTH HKKKMSEKDR ERERLEVQQA RKAADFYRKK QEDMNRPVNP
REPLKRTADN NWVHVTCAVW TPEVKFGNAK AMEPSEGIPS IPRARYNETC KVCDKVEGAC
VSCHQCRTPL HVECARQQGH ILGFEISPVK GSRRDQVNVV TVNGESGTMS ATVWCKEHAP
TKTTVHHMHD IVDDSGLNAL QLYVQNFKQA DLTLTGTARK ANLMANAAKL TGTATQPGLR
RSSTTTLPTS HQRNGETGDA ASDPRHPGGK VCITCGIDVS PKWYPIDNSQ ERELTNGHYG
TLGSEAQKFV EQRRFQCHKC RKAQPTVKAH PPRRSPILPD APPPLAHEAA ISATAAPPLR
SPPQMIAHRE AHASAYAWPP HGHPQTGPPA MQAPALVADH ALGARPPAPH AYAAPPTHRP
AYSDWGRPAS QQSSPPRHIN GGPPPPPPPP PIHNAPPMSN LSSLRPPPVV GPAPPAPPPA
SHHGGHPPSP YTNGLPPSPR QLNGPAPPSR YAHPYQHHGR PGPPAHLPPP NMANGAPPPP
PPAPRGDGFP REIHPQRPPY TAPQTSPPGS RNGLPPPQNR PASGASASPS LRNLLS
//
