ID Q6M999_NEUCS Unreviewed; 948 AA.
AC Q6M999;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=29E8.260 {ECO:0000313|EMBL:CAF06059.1}, GE21DRAFT_6131
GN {ECO:0000313|EMBL:KHE88536.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAF06059.1};
RN [1] {ECO:0000313|EMBL:CAF06059.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAF06059.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KHE88536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73 {ECO:0000313|EMBL:KHE88536.1};
RG DOE Joint Genome Institute;
RA Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.;
RT "Draft genome sequence of Neurospora crassa strain FGSC 73.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; BX908809; CAF06059.1; -; Genomic_DNA.
DR EMBL; KN389634; KHE88536.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:NCU04389; -.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_009510_1_0_1; -.
DR OrthoDB; 124870at2759; -.
DR Proteomes; UP000053122; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR CDD; cd19183; SET_SpSET3-like; 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; IPR044435; Set3/4_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PTHR14571:SF9; HISTONE-LYSINE N-METHYLTRANSFERASE SET-26-RELATED; 1.
DR PANTHER; PTHR14571; UNCHARACTERIZED; 1.
DR Pfam; PF00628; PHD; 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.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 46..95
FT /note="Zinc finger PHD-type"
FT /evidence="ECO:0000259|SMART:SM00249"
FT DOMAIN 283..415
FT /note="SET"
FT /evidence="ECO:0000259|SMART:SM00317"
FT REGION 101..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 102503 MW; D53CFA84C8F6351C CRC64;
MTDKLPSLLT PIAPPSRTSF SVSAAVPVQD GIRAQENVEE EPYTIRCICK YPDDDGNTIY
CELCDTWQHI ECYYPNNSED ALRDPDFAHF CVECQPRPLD RERAKENQRR KLTTGVTEGM
ADKKSKRPIS KSHKKKPKPS DLPLTGQHSK AEKQASIQDS HPPTKKSKSS HKSSHSVSSQ
AAKRSPQFGS TKSNHAHPPS PAATPPDLPA DFEIHTYAPA LLSGSSDRGV EIVHTNSFAS
LQVSNAISAW LRDHNKLQKE TGWAYADIFQ PLPPNIDQLK RPVDIELSRK TLGQGTVASW
KCLKAPSAIA HNVPLVELNG QIGIQSSYCA DPDSRWQELT SPLPYVFFHP MLPIYIDTRK
EGSQARYIRR SCKPNAMLET YLSDGYELHF WLVTDRQVAA REEITLPWDF RFPNENKSRM
LRVLGLSDED TSAHAESSVD DGEYQALTSW LHNILSEYGG CACNLGSECA FARFHRNHLG
KSQAPANPPK TKKRKSKTQS SSTIGTGPAT DSRAASEGHL EDAPENDRRS VSGSARSKPP
SRDLTPTARQ GSFDTLGILT EPTDRDKRKV SMIEETFRRI ELQQQPTKKR KARGSDAATT
SKKGSKSSAT TQTTNATNGP DERHCHFANG ETAITSKATS PAASAKSGRV TKSKKTSSRK
GSVAVVSHPV PAQPVRLPSR PKYADAGTQT NPDTEANPAP SPARPKRRLV SVTMRIMQHH
RWLKEQQGKQ RLLNQAVATV PMDVDSPKDN KAVVSVAGSV QDTTLKPSAP SKVTTSDVEM
PDAPTVSASH LKAAQSTSVV TAPKSKVLDL RVPMPPVPPF PSSTSLALTS TTSLPAGTSA
AQSSFSVTGL PSPLGPSSIN GLTANPSPIK KKLSLSDYTK SRMNKAAAAR PSVSVPSLKP
NAALDEPKLT TSDDNGGAAS GSPTTEKVTD TTGSTTAALA LTTASSSV
//
