ID A0A0L0VGF7_9BASI Unreviewed; 1457 AA.
AC A0A0L0VGF7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
GN ORFNames=PSTG_08404 {ECO:0000313|EMBL:KNE98328.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE98328.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) 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:KNE98328.1}.
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DR EMBL; AJIL01000058; KNE98328.1; -; Genomic_DNA.
DR STRING; 1165861.A0A0L0VGF7; -.
DR OrthoDB; 24699at2759; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR026817; Ect2.
DR PANTHER; PTHR16777; PROTEIN ECT2; 1.
DR PANTHER; PTHR16777:SF2; PROTEIN ECT2; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564}.
FT DOMAIN 148..449
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1213..1240
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1339..1366
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 161514 MW; BEB290887C957350 CRC64;
MDRRSASPGP AQAFRTNNPT LTKPRPISYC NPAIIRHQHS NSIMKPSPPS LLSLSQLSPL
PFLINPTTPT TKSTLVDVVV EGMGGGNDPG EGWQVPPELV FFLRSLGERL DPFSPTGKTS
NSAPAGHTKS LTAALNHATL RPTTDQAAIL ALFTELVVTE RAYLRRITAL NQSYAIPLKN
FSRLNQTKII DKYETTSMFG KIEAVVSANQ SLLACLEKSL QIIEQQLQQQ QGEQHWADAL
SDELLNIQRP YRDYLAGYDI VKETEQKLLK KSEAFRQFCE RTKETMYDDG MGRVGLRELL
MEPVQRITRY ILIFEQMLKK MSSNDPARNG LLACIATCNR LAVCELDDHT IKAATMWGLH
RSIEGFPAIL IKPGRYLIDS IDVLDIIPDN PSSTILHCTL FLFNDTMLIA KKPPNHHLTG
RGLAGLDDYD KLVAAMKKSK STTSSLNSVV SGGTDFFSKS LGGHNNNTPT KVKKGSMRFK
GLVDVHDVIV SNEPTQSGIG PTSEVSFDLY FERPPENVSE RWTDRRYRHY VVCPPPTLIL
SGHEKSLSLS SHPTPSSSNH QAGGLPPTTS HSLSHKSNIH HLNSNQSILA ALAERDRFLD
NLRKSQALVK AADDRSTVMR TKFINENEIL KPAIDSFWNL YDKQTYLAEL RKHRVVLQLV
GTDAVDPLQF STESIDPMPP LMIIRAHFND PDDPDCRVQV RRKPNHIFPS LNNNIPFEKV
DEDIVVQTEC LSGLIVRIIQ AYGIADIPPR GTQHIFTTTI STSQQQPQQT QAQYAGGTNP
PSPSRAFRTK SGSIALENNA NSALPHRLFT KEGLQRTKSM KSSHTKGSST SSIGYATTAS
QPGTPSVALR EIQPTATRSP GGPVWYRNSH NPSTTTTHTS SRFAPTKEKT IQDSNRISIY
EDLPRLREEE EVNQRSSSPA AGSTLKGKGR AGCVFDADED EDRDFNNGQT ESESQCSSVS
GLSSYDDDEE EDGVEEEDGS IEGGRSRTRA GGLVGPRELI VPVHQIERSN SLKTRSKSEP
PSKEKPPKTC NGNPKMNGIN GGYRVPQSIK QSLDSDRFLE TTTGITSRTG SRNPSGSSLG
KRSRSVDGDN LSTDIDNHTL QPDHDRVKRV QTLPLVVRKP PPSSSNQNKK NSPNSRHRRK
TRIPSNSLNT STTVGNHVKT NSVDHQDDNS NDNTLSGLDL NLTNPDPKHH KNDLDLDLGG
EFQVSEIGTT DLFNDVKGRM KLLKNQLKKL KQEINKIDHS SVTTTNEEST GSGSGLIGSR
NMNGSIPRSP RKLHLSEVAK DPSHLLRATS LTTSSTSTQK ESFKNLNGLL SEIEKSYDGI
HSKFKLIESS ETKSFKNQFE KYNKSIDIMK KEVQKYKNEV EVIKTQSTIS IQIQESLETE
NSHLYDAFNE ELDKMFNDIQ LSPPSQSLNL LIEDLKRFAE ERGKLSTLLG ATQRQLELET
AKSECLENLL REAGLLT
//
