ID R0KMM9_EXST2 Unreviewed; 1387 AA.
AC R0KMM9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 28-JAN-2026, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA89187.1};
GN ORFNames=SETTUDRAFT_167742 {ECO:0000313|EMBL:EOA89187.1};
OS Exserohilum turcicum (strain 28A) (Northern leaf blight fungus)
OS (Setosphaeria turcica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Exserohilum.
OX NCBI_TaxID=671987 {ECO:0000313|EMBL:EOA89187.1, ECO:0000313|Proteomes:UP000016935};
RN [1] {ECO:0000313|EMBL:EOA89187.1, ECO:0000313|Proteomes:UP000016935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28A {ECO:0000313|Proteomes:UP000016935};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|EMBL:EOA89187.1, ECO:0000313|Proteomes:UP000016935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28A {ECO:0000313|Proteomes:UP000016935};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB908515; EOA89187.1; -; Genomic_DNA.
DR RefSeq; XP_008023028.1; XM_008024837.1.
DR STRING; 671987.R0KMM9; -.
DR GeneID; 19400289; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000016935; Unassembled WGS sequence.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:EnsemblFungi.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0140015; F:histone H3K14ac reader activity; IEA:EnsemblFungi.
DR GO; GO:0140008; F:histone H4 reader activity; IEA:EnsemblFungi.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031492; F:nucleosomal DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000182; F:rDNA binding; IEA:EnsemblFungi.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR GO; GO:0035973; P:aggrephagy; IEA:EnsemblFungi.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IEA:EnsemblFungi.
DR GO; GO:0042148; P:DNA strand invasion; IEA:EnsemblFungi.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IEA:EnsemblFungi.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0031496; P:positive regulation of mating type switching; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:EnsemblFungi.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 1.20.920.10:FF:000052; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 3.40.50.300:FF:000843; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 1.20.5.170:FF:000072; Putative chromatin structure-remodeling complex subunit snf21; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016935};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 151..186
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 390..462
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 568..733
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 879..1030
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1267..1337
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 65..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..82
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..223
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1208
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 157918 MW; 390D9B115519EB56 CRC64;
MASVQANPEM PGQGQLPANI TREQIQHVFQ RYTAMKQQGV PESNPEFIKA RNLLTMVQKQ
NQYQQQQKML RQQQMQQRQQ GQVDPHVAQQ NGTPTGMPNG TKPPVPADGK TTVPAPASSG
PSSTMQIATA GAQVPATDGQ TPTSASSASM ALSKDQLLML RAQIGAFKHL SKGLPLPSNM
QQQIFGHHQT KKPQNAADAV AAASQMLDNA TRAGSASSTA GGAVQETRTL PRLPDTFIDP
WSSEVFRDVN YISHTQRKNR PYLATIMPQG VDIDAVQQSM EEMRKEREIL LYNRLTARKA
ELEKMHANIG SWDTSKTDTP EDDGKVKLAL VIEQKKLNLL EKQRKLRREI AQQMIHADNL
AMTANRTVYR RLKKQSMREA RLTEKLEKQQ RDARETKEKK KHHEFIDAIR KHRTELQEAG
AAQRIRLQKL GRTMITTHQN IEKEEQKRIE RTAKQRLQAL KSNDEETYLK LLGQAKDTRI
SHLLKQTDGF LKQLANSVKA QQRSANNSYE PEPDSSSDES GDEDRPGKKK TDYYEIAHRI
KEEVTQQATN LVGGTLKEYQ LKGLQWMISL YNNNLNGILA DEMGLGKTIQ TISLITYLIE
KKRQPGPYLV IVPLSTLTNW TNEFEKWAPS VSKIVYKGPP NSRKQYQQQI RWGQFQVLLT
TYEFIIKDRP ILSKIKWVHM IVDEGHRMKN AGSKLSMTIT QYYTTRYRLI LTGTPLQNNL
TELWAMLNFV LPNIFKSATS FDEWFNTPFA NTGGQDKMEL TEEEQLLVIR RLHKVLRPFL
LRRLKRDVEK DLPDKTERVI KCNFSTLQAK LYKQLVTHNR LMVSDGKGGK TGMRGLSNML
MQLRKLCNHP FVFEEVEDVI NPTKGTNDLL WRSAGKFELL DRILPKFKAT GHRVLMFFQM
TQIMNIMEDY LRLRGMQYLR LDGATKADDR SDLLRLFNAP DSPYFCFLLS TRAGGLGLNL
QTADTVIIYD SDWNPHQDLQ AQDRAHRIGQ KNEVRILRLI TSNSVEEKIL ERANYKLDMD
GKVIQAGKFD NKSKDDERDA MLRIMLESAE AAESLEQEEM DDDDLNQIMM RHESELAIFQ
EMDRKRIAED PYGPGKPLGR LIGESELPDI YLNEEAPVVD EKDDTPAGRG ARERTRVKYD
DGLTEEQWLE AVDNDDDSIE AAIARKEAKV AKRGRNKASR EEESPVPSRA SSEEPAPKKR
GRKPKAEKRK ADDASLDADP APRKRGRPAP TKDLLPAGQR TSLQKIVNVV YEALNDLEEE
SSDPNIPNRG IIDPFIELPD KWDYPDYYQL IKNPICMKQI EKKINKKEYQ SVKQFRQDLG
LLCNNCRTYN EDTSLLFADA NLIEQTALDK LKEATAEHPE WQDYDDGSSV QGGASTAMTS
AVGTPRT
//
