ID D9J222_FUSOX Unreviewed; 1567 AA.
AC D9J222;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 22-FEB-2023, entry version 52.
DE SubName: Full=BAH/PHD-containing protein {ECO:0000313|EMBL:ADK22148.1};
GN Name=snt2 {ECO:0000313|EMBL:ADK22148.1};
OS Fusarium oxysporum f. sp. melonis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=61369 {ECO:0000313|EMBL:ADK22148.1};
RN [1] {ECO:0000313|EMBL:ADK22148.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21535351; DOI=10.1111/j.1364-3703.2010.00683.x;
RA Denisov Y., Freeman S., Yarden O.;
RT "Inactivation of Snt2, a BAH/PHD-containing transcription factor, impairs
RT pathogenicity and increases autophagosome abundance in Fusarium
RT oxysporum.";
RL Mol. Plant Pathol. 12:449-461(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HM246662; ADK22148.1; -; Genomic_DNA.
DR PHI-base; PHI:2453; -.
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; IPR029617; Snt2.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PS01359; ZF_PHD_1; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 205..323
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 360..412
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 501..649
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 923..973
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1012..1144
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 983..1015
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..31
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 115..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1567 AA; 173219 MW; 2EBD1C9C0A0D76A9 CRC64;
MAQHNDSNTS DPGAQSVSDP MTTQSSLDSA AKEAGADSAF PYGTRSRNRT GTSRINYAED
RDIDGDVYDY YHDKKDSDSK KTSRQSSAAV NGDAPRGGAS SRKAGTDEPK AAQVANTPKE
QQSGSSNNVP TTTQQPAASQ PARKRKVVGN PAGSTNPATS VNNSTKKTAA SGTPSRIPWP
ETNMLTFDDC KSRPVNGKMV ADDGAALEPN DHVYLVCEPP GEPYYLGRIM EFLHEQNDSS
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
NEYMEKAKGM TKDLGLPERS TNLQDMAANK LFRAEFDTEH ALKDLSETKK EAFKEPELTP
AEQKKFEEAV IKYGSELYLV RKHVKTMHYG MVTRYYYAWK KSARGKQVLE NQAGRKGKKE
AKRAEAAASK LADDVADNDD DSAFDTEKAN QKKQGFVCQF CSTTSSRQWR RAPNPVPGVV
NDGGSKNSNK EKGQERVVAL CRRCAELWRR YAIRYEDMDE VNKKITQGGR AWKRKQDEEL
LKELQAAKEM GMMTPERAPT PSATPVVATV QEPPRKKLKG AASDKDVDNG HSDAASAAGS
TTSKKKDKSV ENLTVPDIPK PLVLPCAVCG QLEPQGDQHL SCRECRLTVH RNCYGIMDNR
NPGKWTCDMC ANDKNPQVSI PKITHHKKKM SEKDRERERL EVQQARKAAD FYRKKQEEMN
RPVNPREPLK RTADNNWVHV TCAIWTPEVK FGNAKALEPS EGIPSIPRSR YDETCQVCNK
QDGACVSCHQ CRIPFHAECA RQHGHVLGFE MTSVKSSRRD QFSIVTINGE SGIMSATVWC
KDHAPTKTTI HQMQDIADES GLNALQLYVQ NYKQADLALT GTVRKANLMT NAAKLSGTTT
QPGLRRSSTT NIPNGGWGQQ RNGDTGDVAS DSKQPGEKVC ITCGIDTSPK WWPIDNSQER
ELTNGHYGTL GSEAQKFVEQ RRFQCHKCRK AQRTAKPHPR WSPLMADAPL PSAHGAGIPG
TTTHPLRSPP QMMPAHRESN PSAAYAWPPP VHAPAVPPPP MQAPALVADH ALGARPPPPA
PYAPLPPQRP SYSDWGRPAS QQGSPPRHIN GGTPIHNPPP MSTLSSLRPP PVVGPGPPVG
SSPPAPPPAN HHGGPPSQPY TNGLPPSPRR LNGPAPPPRY THPYQTHGHN APPPPPPASH
LPPPTLTNGA PPPPPRHDGF SHELHPQRPA YPAPHGSPPG PRNGPQPPSS RPASGASASP
SLRNLLS
//
