ID S8AVV2_DACHA Unreviewed; 562 AA.
AC S8AVV2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=MYND-type domain-containing protein {ECO:0000259|PROSITE:PS01360};
GN ORFNames=H072_886 {ECO:0000313|EMBL:EPS45101.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS45101.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS45101.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS45101.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS45101.1}.
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DR EMBL; AQGS01000023; EPS45101.1; -; Genomic_DNA.
DR RefSeq; XP_011106878.1; XM_011108576.1.
DR AlphaFoldDB; S8AVV2; -.
DR STRING; 1284197.S8AVV2; -.
DR eggNOG; ENOG502QXAC; Eukaryota.
DR HOGENOM; CLU_021696_0_0_1; -.
DR OMA; CERCVWE; -.
DR OrthoDB; 2785946at2759; -.
DR Proteomes; UP000015100; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR12197; HISTONE-LYSINE N-METHYLTRANSFERASE SMYD; 1.
DR PANTHER; PTHR12197:SF273; MYND-TYPE ZINC FINGER PROTEIN SAMB; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 304..345
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS01360"
FT REGION 96..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 62731 MW; 6B314331197BDC6F CRC64;
MLPEKRVARI VQDADGVLAS DPLQSRNLFT KALAISPYDP DLWQKRAVAH TKLGYPDLAI
GDAYRALLLV QELLEAHDES EFGFAGLVAW RGRRQQPRNT YATSDDTASS DDGHGEVEEE
TELDADSIPA ISESEDKDLR DTDIAARRLI CSSLLELGCL LDGLEQADAA LKVYPEDNEL
KRIKEEADAK VSAGREKGLS DYQLREGQVA RVIYPWNEFE PNRTSPVTVE RMNEFVNVSS
SGNLEVKVTE LPMLVPDPED EKKVITKKSI QLGVYAVKDL PANTQVFSER SILTVNNRLF
DPLCDCCNGP LDPLNTLSCP DCDEVMFCSD QCKDEALEKY HPTLCGIGID FLFKSAHSRH
EVANDASATA STSNPTKALY SLLLLRTLAM ALTQDVNPLE ILPVKYLYGS SPPPPPPEKP
PTLPFTFSDN ILSVFHILTR LEVDPFKVSL HTFDIWHTLT IHSKILGTAS ARHNPTSGQP
EVAALHLCYS IVNHDCEPCL MWECKSEMQF RTLREVKKGE EVRDCYTDPR IESWKKRREW
LIGSLGGGCR CGRCIRESQA DP
//
