ID A0A180GZI3_PUCT1 Unreviewed; 936 AA.
AC A0A180GZI3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=SET domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PTTG_12012 {ECO:0000313|EMBL:OAV97934.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV97934.1};
RN [1] {ECO:0000313|EMBL:OAV97934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV97934.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV97934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV97934.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
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:OAV97934.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADAS02000010; OAV97934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180GZI3; -.
DR STRING; 630390.A0A180GZI3; -.
DR VEuPathDB; FungiDB:PTTG_12012; -.
DR OrthoDB; 5481936at2759; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46223:SF3; HISTONE H3 (LYS9) METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 598..701
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 704..895
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 919..935
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 103077 MW; 1AF6FCB7575FACF9 CRC64;
MPGAVNGKPH TNQMASRPSM QPRPSSSINN PIKDTPSEVI SISDDEDDQV TVLSAPKSKT
HVKRSSSTYD VSSWNVRPKS KHHHGQNSVK DSSSRPILSS STIRSSVVAQ SHGRKNLNTN
TSNRQELFSS SQSVGQHHAA LSKGKQPILH VREPPKEQPQ HARTSNTSPS KGSTNASKTT
RPTDVSSTAK SGEFQNTKPA RTIKPSNEQS DVVNKLQNCF SHRPSSGSGS SSTRKDQISG
PVASTHSKPA ADTSNRRHES ESSWATSQIK QSMAALQAQR DINRAERERL QSRGNTSASG
SALSKGLTTT PNTNTHSAIE SSTPHTASGM LSATAKVKDN TLGMRVSNQQ DNSSSRDAIE
AIFSGISNRL DTSDAPHARK KIKHTNSLQS KKPEDRFLEL SDSNFTDPPI PSTSFLPPRQ
NISNTTSSEP ALQPKKGSST GLVTNNSTST HDSPCAIHPV AFLPLPRVLP RTRPVSPDWS
QIPSHRRPLQ GRERPGEFSD ELQKTWILNN NPDLSTPLGQ LIFTEEINAN QMWENPEIPR
IDVVVPDEVK AQMLENLKAE RQGDKTSGLD QSLAPPLEFI YTDRLVYRNN ERPIPPSWHC
NCHGDCLNNP NCECRAYQTQ MVKQAAAAVD LASDAGVQSF EGFAYVSTRK NRHTHSKKPD
NGDTEARCIA DIFIQNRFPV FECNSRCGCD SDCINRTVGR GRREKLSIQK TLSRGWGVFA
DHTIPVGRLV THYSGEVITD AMSAERGQLK YEKIGRTYIF DLDPWWIKTI STHNLSDDGL
FVISSESNKT SETQSVSTSA NSVGHQNANR SLATSSSTAK KKHSKSKRQD DEVECIYSVD
AFLYGNVARF MNHSCSANTV IVPVYIDDVD PTRPIFAMFA SKHLKADMEI TTSYSDPNEN
EVKELDKQIQ STKESQLTRY VECKCGAPNC KRVMFA
//