ID A0A367K0D2_RHIST Unreviewed; 981 AA.
AC A0A367K0D2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Putative PHD type zinc finger protein with BAH domain-containing protein {ECO:0000313|EMBL:RCH95628.1};
GN Name=SNT2_2 {ECO:0000313|EMBL:RCH95628.1};
GN ORFNames=CU098_002291 {ECO:0000313|EMBL:RCH95628.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCH95628.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCH95628.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCH95628.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(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:RCH95628.1}.
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DR EMBL; PJQM01002406; RCH95628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367K0D2; -.
DR STRING; 4846.A0A367K0D2; -.
DR EnsemblFungi; RCH95628; RCH95628; CU098_002291.
DR Proteomes; UP000253551; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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; 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; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
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 SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 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:UP000253551};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00094}.
FT DOMAIN 20..138
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 175..227
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 305..458
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 463..514
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 565..630
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT DOMAIN 651..696
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 704..814
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 236..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 111722 MW; 3F38451741CE7123 CRC64;
MSDVKSAPHI TSTTLANGAS VQINADHVYL APEHLGEPYY VGRVMEFCNS FKRKGLQARI
AWFNRPKDVI NRKSADPCLL VATMHSDINP VSSIRGKCVV THKYYIPKDQ LEVYKKKQDH
FYYNQLYDRY IQRVYDVVPS ETVQNVPMDT LEALKQRYQF IVVEQGKSAD LTVARRLCCV
CQGWCSSTAS VKCAACQKSY HMTCLNPPLP RKPTKGFAWQ CAFCARQELI ETSLPITSET
SDRVSDKDDT KKRQTRTTRS QISKTQPQRQ LPQPEPSNSQ PSAIKLKIKH PRKTRNIDDR
IYPRAKSRIG PKYQANVPDN DISKHLSLSP VSEPNSISSN KSKTKKIDKK GKSVQRPFIK
KPGEPSLPYN QCAYGPQYEV AERSPLAPIR GGDDTVTCIY TPGVIDDEQV DNYMERVKDL
ENIHLSSHTS DLMDSAIYEL HKSGYQPEIA YQKMSQLTTD DFEHIVDWSK REVDAFEQSI
REHGHDLNYV KKNVGTKSMA DIVRYFYQWK KTDRYEPVYS EWTKIFKPMK KFKSLAQKKK
LYQDIKNDVE SDEESDPTII PKATYDESYQ CMNCQTSDSA IWRRSPSDID RKRKVFTEVL
CDDCGIYWLK YAKTKPISEL VKRENMTNTQ QSSRASTVKP GIILKFQPTE CKVCFDCNSE
EKIFTCYDCG MSVHNDCYGI ENVDKEGWIC DPCSNKMNPV ASYVYECILC GKSSKETQQP
LKRTAGCRWA HVQCAAFIPE IKFTHPNTLS PIEYIGCVNS SRLDANCQLC ENTEGACVAC
AECKKTVHVQ CAIDHKFRLA FEVQTMPTFV GEKAKVPYVP AGLFHSSSPS GLMIPQLWCP
VHNVSSRKLI DLSTRTLNTR ESSVTVYAKS FKAVAKESTP ATRRFRQAMY HPYLSDNFSQ
YYHHRIPKVP TAREAALDAL TADEILSLNH HTTVLLPTNS SNHPKQKCAS EGCPVKHTAF
WWSVKANSKK KVCHSCHSVK T
//
