ID K1XHI2_MARBU Unreviewed; 1402 AA.
AC K1XHI2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=SET domain protein {ECO:0000313|EMBL:EKD20213.1};
GN ORFNames=MBM_02165 {ECO:0000313|EMBL:EKD20213.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20213.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD20213.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20213.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921430; EKD20213.1; -; Genomic_DNA.
DR RefSeq; XP_007290054.1; XM_007289992.1.
DR STRING; 1072389.K1XHI2; -.
DR GeneID; 18758100; -.
DR KEGG; mbe:MBM_02165; -.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_254229_0_0_1; -.
DR InParanoid; K1XHI2; -.
DR OrthoDB; 1784562at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
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 InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR47250; SET DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47250:SF3; SET DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT DOMAIN 188..294
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 358..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 154007 MW; CD6068EE8FED0D86 CRC64;
MTALREACSI LRWSEKELRN KLSIWRGYRE IKDAGGWASL IFAGSGIYRF CKYRGGFGKN
LTTRLEKLRP SLEVAADTLH PDWRDLLSVI GQESQALYTG HPHDWVVCDG KEPVTLKSTY
TQWYPDFEFT HIEDSVLDPA AWGSEDPRRV SSIRTMFCNE CGYFQSGNVS SNECRCFPEL
YGSSKAQVPV QVFRTPLGKN NGLIARCDLP RGSAIGEFTG LITKGMDGID VMQSGSDERK
YQIFQGRMGN YTRFINHSCA PNSQFQKFSW LGTERIILVS RGVEAGSEVT VDYSHEYWEG
LDKKSTMAAN ISNGYKVVRI REERFDGGRG VDFLGSSTAP FYLVNAGQNL FYGEGTVNSG
GDGCDPSGVD GKKRPRASTN RKSIRGLEDP GLPPGEDSPP RQTPKQGPDT DLDSNLSSIS
SSQFTEDDLA SDLEGPGDNR EEETVTPSKR EQNSIRPAPP NIIDNSIIKP IQIPKPIKIH
IDFSRNSSFN PSTRSRQDVC VNVFVNGEFV YSKLFRAQSL RGSRENAYPK IAIGGRRVSK
TLEVPWIVLP IRAESPTAGV VGQEETGDTL QPSVNVAQGK PVELNVPALE SYNGDLIAEY
KRCSPAATTF AIPKPISEEA SPIPPSQSIS SAESRWDEIN QNLLTEAEKW GRDGEFDVFR
DPVGEYLVEL SKLKFPKNAK LADANSRNIG VMDVVISLGR SQAFTEHQSI LEPQRNLTEA
HWGNQLFRAP NESSFRGSSA PSAASTANSS TENHHRNTTG GSNSRAAGAE AAQTETQEGL
SMSSMPPPAS AVSAISLIAQ RGHMMSTDPQ IGHHPKTSRN VPQKTYRGLK SSQEEESEWP
SRSTRSRVSM GSPPAPQSSQ GTTDSILKTS RQTTRPQRSA ASGSRTASLS KDGSSDKVDE
WRRQPARFSG YLYTIIRNFV PSEPKKWTRE STDRNGYDGI GGDGKTPMRK RRSSDVPDDA
PEAKVARLDT EFMKVNAPNN SESPMALEIG TASSGMQRSE VDLISPTIDE PERQPSEETP
KRKRSQVSVS NRELSSLLSP HKASKIVDGS FGETFDKSFR RPTRNAAANL KQRRVTAKVE
GQMLIAKGLR QDEISTCSPN TPTEHSSTEK RVKEDSFGIE LKSHPNFVGS VPPHSQGSFS
KTLETLPSDP ESERTRPVGH EENYHSTQGF AASRQLKRPS MDLRQGQASK SKTNLAKGSK
PRQPELEARK SPEFHPFIAQ SLLEKPKNTA IASSYVSKAI LPAKSGKVSA GSRAKAFPGT
TGSRALTQSQ AGPNTNDSLR CTESQDTSQT EATASPRELL DPARSPIMNK QASETRTIEV
LDAKAERAAA SIGWRPTVLC QDSVLSYVGD EKTAKLLGID FKKKEGNFCR KTGADRMKVF
RACTILMGVR YVFGLESTAE KK
//
