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Database: UniProt
Entry: G8BP68_TETPH
LinkDB: G8BP68_TETPH
Original site: G8BP68_TETPH 
ID   G8BP68_TETPH            Unreviewed;       784 AA.
AC   G8BP68;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN   Name=TPHA0B01260 {ECO:0000313|EMBL:CCE61799.1};
GN   OrderedLocusNames=TPHA_0B01260 {ECO:0000313|EMBL:CCE61799.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61799.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE61799.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE612857; CCE61799.1; -; Genomic_DNA.
DR   RefSeq; XP_003684233.1; XM_003684185.1.
DR   AlphaFoldDB; G8BP68; -.
DR   STRING; 1071381.G8BP68; -.
DR   GeneID; 11534722; -.
DR   KEGG; tpf:TPHA_0B01260; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_017047_0_0_1; -.
DR   OMA; WQHAICY; -.
DR   OrthoDB; 124870at2759; -.
DR   Proteomes; UP000005666; Chromosome 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15550; PHD_MLL5; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46462; UPSET, ISOFORM A; 1.
DR   PANTHER; PTHR46462:SF3; UPSET, ISOFORM A; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          353..488
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          198..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  90395 MW;  992EE44D68ED92AF CRC64;
     MNASSKYEVE GSGENISLME DASVLLMLSK NVPKNDKQSV DDIKKTNASS DDNMKRVISN
     NESLIKGEVE VKRQKLDNGD ELKENNEKKE KVWPVSDDYI VDPDAGVITC ICGFDDDDGF
     SIQCDHCFRW QHAVCYGIYD NENVPEIYLC DVCEPRNVDK EKAKKIQLQR FTNQEVPVNE
     TYEDEDTGKH DTINILTSEN GYIRKHTKPE AVNNDNKEVQ ESDVESINME SKSNKEESNN
     SDENDGKDRS RNIKEHIRTP TRNTRSRNDA IQNQGRIQSN DINDQNADIT DTTVQSKKKQ
     EVFYLSAKSS YEAMYLPMKK FSVQNNYVTL FLEKHLNDDV VTEVENATDF KNMPIEVKSY
     VESSYLRTFP GFTKLGVYLN KDCEEGKLIH DITGDVNFKS NYIRDPGSYY RVWGTSKPKI
     FFHPTWPLYI DTRLSGNSTR YIRRSCNPNV EIATIKTLNN KTKDYEIKFM LKAKRDIEED
     EELHLPWDWD KKHIIWKIIN NSSNPTHILE NLKDSDKYLL LNSIDTILRS CDCACGNNSK
     ECFLLIIKKF QQSLIKAIRS KMSNRYKINE ILNRYQGKRR RPPPILQRLQ DENIINQEKS
     LYLLNEFNTQ KLRFLEGQDA SSTNLSSKLY NAKKGKNFLD SNDRSMDSIS SMIEKDFNKP
     FKWKILHNKL DEQSRRKSTS KDIDSNLISN FTEYNETQIT NLEDLPIIID LKINQTKVNY
     IVESRKSVVN NNENISLIPG SSLAPDIELK AVSEAVNNYS AGNETDPLES LISATTQVKP
     SKKN
//
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