ID F9XB39_ZYMTI Unreviewed; 1913 AA.
AC F9XB39;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGP87410.1};
GN ORFNames=MYCGRDRAFT_93545 {ECO:0000313|EMBL:EGP87410.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87410.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP87410.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; CM001200; EGP87410.1; -; Genomic_DNA.
DR RefSeq; XP_003852434.1; XM_003852386.1.
DR STRING; 336722.F9XB39; -.
DR EnsemblFungi; Mycgr3T93545; Mycgr3P93545; Mycgr3G93545.
DR GeneID; 13394211; -.
DR KEGG; ztr:MYCGRDRAFT_93545; -.
DR VEuPathDB; FungiDB:ZTRI_5.790; -.
DR eggNOG; ENOG502SCHT; Eukaryota.
DR HOGENOM; CLU_235561_0_0_1; -.
DR InParanoid; F9XB39; -.
DR OrthoDB; 2788167at2759; -.
DR Proteomes; UP000008062; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00167; SANT; 3.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR018465; Scm3/HJURP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR15992; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR15992:SF5; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF10384; Scm3; 1.
DR SMART; SM00339; FH; 1.
DR SMART; SM00717; SANT; 5.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 3.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS50090; MYB_LIKE; 3.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 341..394
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT DOMAIN 718..761
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 797..839
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 1087..1132
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 1477..1581
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 1477..1581
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 68..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1913 AA; 208647 MW; 45EF4CB042DA77B1 CRC64;
MARRKRSIPA PEAPSAAEAE VRQLELARNQ NDQKLKSRFE RIFRKYEHDF TDVGDEIDIE
SGDIVVDNGH LQNMRDEADP GQSRSASSRF VKTFQEKLGH EGEDDDEEEE EDDEEDYDDE
SGDGEDDEED QSDGTDETEE GDNVDTFERL PTVEPFRALK RPPPRLAQLL VGGTTPVDDL
DASIEDSASG TSTPTGLLAQ VPALQASMST LASKAKRPTV DTDTIQALGL TIANQLAQLM
AGTSKKRKRH PRPVSRSNTT DPAWDYPEIT HDRSTRRKQR RMKSPVPPAD NTSPQAPSPD
QRSLWAPTGR QKKNTWKEAN AATPVRRVLR SSLVASSVLK KEDLRRCGNC SLTNSITWQP
GPNGEDLCTS CGRYYDYHGR MKPFDSPTPS VEDLEEDGES SGDSSFDIRF ESAQSTPALV
DGANDAAMDS SSRAADGKAE GSVKPRIGQS ASEKSPQRIS QLSRGGKEPQ RTSSVVQQAP
SISDGPQHTQ ADAMPFQAAS TSHTTLPGSA SEASLRRHPA HTDLASVGHA SILGPSLAPT
SRHDPSLQRT KRGTGQSLPL VEHQIPAAAP FTRTQPVQSV IGNSALDVQP NGAIRSPSRL
RSSTQPSAPS LTQQPYPMGA PTDQSAWLAN NFAMTAPTQR ESGRHATTPF PTTQFGSNTG
EVPYRSAVVP EQSVPSAPAG TPKKEYDIFV NETPATLYTA NTSRVISDAE SPGGVLVPYT
AEEDATIIRL KEIDKLQWVL IADHLPERTA FSIQSHYRRV LQGKLGAGRR LLEARLAKRD
QSPPAPPLPA APHDPEWDND EDELLLELRE DRELEWDEIA EIMDNHTEAR LESRYEEIVE
SSRSGSSILP DELRTGALFS AEEDALIVRL REIDHVPWNN VAQHFRGRQL HSIQKRYSRV
LAPAKRKLPP VDPSEMTLEQ RMFEVDPELA ILLHSQSDPK AFNPREDQLI LQLRDQNLSW
QAIAPSFPGR TAETLQIRHA ELLASKEREQ QIATTPFVRR TDAAPQTFYH AASGQSTTPY
RSLAPMVNAR PVNNGASFAV PPQHGTNAQS VRGPAVAPHT YVPNSESAAP FRHPSDVQSS
NHGPGMRHPF TKTEDDTILQ LREKQGYGWH DIAVQLPGRS VNSISTRYMD ILRRGDPSAR
QGGNAPGVFR PDAAQRTAGR GTKASQNHHS ANARSNTRQS LPSATMVEAR VQPGLLRHAL
NNSRRLSDFV SEQTRGKASR GHNIDDPISL DDDDDNSTVA ISQQLNEELR HSVARPAPSN
ATKGTSTISE IRSADTRANA GVSSTISSKS SPRVTASSAA LQHFLSRAPQ QPKLPNFLES
KSAHAVAASA TVRHQQASAP TFPAASRPAS GTSQHDTTHD TSVTQTKAAP RFTMASPGPA
AAPGSQFQRQ SRPVLDDDVA GNSPTHAAEQ SEGRAAMRQK GGTHQPASST STTAIPASAD
AILDNAQAES TSAAVFSAPI HHSRGSGSEE SLVMPEKPRY SMLQLVHMAF QASQSETMFP
REVAAWVQTN FEYYRAVPDT WKSGILTELN YKDHFEPVET HRGREFRLRP GVGPEVASRP
QKTRGHARRV GEEKQATRDR SSTAVKQAQD VDHLVGKPKI TTNSRPTKRD ITSRTEAASP
SSSKSRVPPV APIHPDADDC APVLPLEDSD SITVVQPKRG RPRGSKMRKY SEDDDDDEYT
PQQETGMPIS NVATRARLRR STGSTQASTE VETVNEPSGA FREIPDSDEE NSQEVSSPVP
MARSSEKRVH FMETVEVRRP IASHERPTSS NGARPGISHQ EQTAGQHQTA APTGFPLSSE
SSRNLPAPTS STAFVKPSTP ASVLRKPKSR VSDGALAIHP RHRIAQLRKY ETPRRASTGM
PIFTPQRAGT PTAVFAYRAS PAASGAGDRF GYGRRVVETP VRELADPNED ELA
//
