ID W9IUR4_FUSOX Unreviewed; 1566 AA.
AC W9IUR4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE RecName: Full=Lid2 complex component snt2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOYG_02911 {ECO:0000313|EMBL:EWY98402.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY98402.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY98402.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH717840; EWY98402.1; -; Genomic_DNA.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000030753; 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); 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; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 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:UP000030753};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 185..303
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 340..392
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 481..629
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 903..953
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1011..1143
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 982..1014
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 34..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1566 AA; 173422 MW; F9C16DBE7994F065 CRC64;
MTTQSSVDSA AKEAGADSAF PYGTRSRNRT GTSRINYAED RDIDGDVYDY YHDKKDSDSK
KTSRQSSAAV NGDAPRGGAS SRKAGTDEPK AAQVANTPKE QQSGSSNNVP TTTQQPAASQ
PARKRKVVGN PAGSTNPATS VNNSTKKTAA SGTPSRIPWP ETNMLTFDNC KSRPVNGKMV
ADDGTALEPN DHVYLVCEPP GEPYYLGRIM EFLHVQNDSS KPVEAVRINW YYRPKDIGRK
STDTRMVFAT MHSDISPLTA LRGKCQIHHK AEIKNMELYR KDPDSFWYDK LYDRYIQKNY
DLIPTRSIVN VPANVKKVLD ERWKYVLVEQ GRGKELTSAV KLCKRCAGYC ASNDSVDCAV
CQNTYHMNCV NPPLLKKPSR GFAWSCAACS RAQERKLEAR NTPNVNDPSF DAEDDDPMDE
EDEEMQGLET NRTSPEEGDH PHHEGTAEQI YQASLWPYRY LGMHCKPEDA LDYDDRIYPR
ASTRIGPRNQ ANVLPWPGKP VEYVKPLEIK KNGKKDTKSK EALAAIEADK ISRGKRPKWV
QDMPPGYTAR GEDFDDDDPR CTATRMWIPP PEKVIKEKDM NDYMEKAKGM TKDLGLPERS
TNLQDVAANK LFRAEFDTEH ALKDLSETKK EAFKEPELTP AEQKKFEEAV IKYGSELYLV
RKHVKTMHYG MVTRYYYAWK KSARGKQVLE NQAGRKGKKE AKRAEAAASK LADDVADNDD
DSAFDTEKAN QKKQGFVCQF CSTTSSRQWR RAPNPVPGVV NDGGSKNSNK EKGQERVVAL
CRRCAELWRR YAIRYEDMDE VNKKITQGGR AWKRKQDEEL LKELQAAKEM GMMTPERAPT
PSATPAVATV QEPPRKKLKG AASDKDLDNG HSDAASAAGS TTSKKKDKSV ENLTVPDIPK
PLVLPCAVCG QLEPQGDQHL SCRECRLTVH RNCYGIMDNR NPGKWTCDMC ANDKNPQVSI
HYKCVLCPVE YTEHDFVEQP KITHHKKKMS EKDRERERLE VQQARKAADF YRKKQEEMNR
PVNPREPLKR TADNNWVHVT CAIWTPEVKF GNAKALEPSE GIPSIPRSRY DETCQVCNKQ
DGACVSCHQC RIPFHAECAR QHGHVLGFEM TSVKSSRRDQ FSIVAINGES GIMSATVWCK
DHAPTKTTIH QMQDIADESG LNALQLYVQN YKQADLALTG TVRKANLMTN AAKLSGTTTQ
PGLRRSSTTN IPNGGWGQQR NGDTGDVASD SKQPGEKVCI TCGIDTSPKW WPIDNSQERE
LTNGHYGTLG SEAQKFVEQR RFQCHKCRKA QRTAKPHPRR SPLMADAPLP SAHGAGIPGT
TTHPLRSPPQ MMPAHRESNP SAAYAWPPPV HAPTVPPPPM QAPALVADHA LGARPPPPAP
YAPLPPQRPS YSDWGRPASQ QGSPPRHING GPPIHNPPPM STLSSLRPPP VVGPGPPVGS
SPPAPPPANH HGGPPSQPYT NGLPPSPRRL NGPAPPPRYT HPYQTHGHNA PPPPPPASHL
PPPTLTNGAP PPPPRHDGFS HELHPQRPTY PAPHGSPPGP RNGPQPPSSR PASGASASPS
LRNLLS
//
