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Database: UniProt
Entry: Q6BJ38_DEBHA
LinkDB: Q6BJ38_DEBHA
Original site: Q6BJ38_DEBHA 
ID   Q6BJ38_DEBHA            Unreviewed;      1380 AA.
AC   Q6BJ38;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=DEHA2G05456p {ECO:0000313|EMBL:CAG90242.2};
GN   OrderedLocusNames=DEHA2G05456g {ECO:0000313|EMBL:CAG90242.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG90242.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG90242.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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DR   EMBL; CR382139; CAG90242.2; -; Genomic_DNA.
DR   RefSeq; XP_461783.2; XM_461783.1.
DR   STRING; 284592.Q6BJ38; -.
DR   GeneID; 2904660; -.
DR   KEGG; dha:DEHA2G05456g; -.
DR   VEuPathDB; FungiDB:DEHA2G05456g; -.
DR   eggNOG; KOG4305; Eukaryota.
DR   HOGENOM; CLU_001251_6_1_1; -.
DR   InParanoid; Q6BJ38; -.
DR   OMA; FAHVNDI; -.
DR   OrthoDB; 5100844at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd04435; DEP_fRom2; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041675; PH_5.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF15405; PH_5; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN          676..866
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1060..1353
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1380 AA;  156478 MW;  38F9460101CFEB83 CRC64;
     MSSSEYPIYS YKRNNAAPNQ HPQYNIPTHL LPQALLDEQR QRQMQGSNSP QRGHIGLNQP
     MQGNNSPQRA QMGVNPPMQG NNSPQRAEMG LNQPMQRNDS PQRGQAGVNQ QMPIPIQNVP
     KQHVTQGQFM PQQDQGQPFH NQQQPIPQQP MYDSPERRQQ QYPQKVQQNV PNYEGMGNGR
     PFNGPRNASL SSLTYGNSGN GNYNKRVNSY SSQESIPQPQ PPYPVSGGYV PNPNNYGQEA
     PQIPQQRRTA RKAPPGSLPP IQTNQVLDSS GRRIVSSPSV PQYNSYSYAN HSPISQTHSG
     QMNNETRAKS LSSTSGKPYQ QQQQQSRMKP IPQGQASQPS PQQTNHQNHR PGSSGSGSSS
     SSHSFSLTSK SRSFTSLSKL SSLSTKKFNS STSLQGSKLD RNPSSATLSS QKTVTTPMPK
     KPIVYPAMLS RVARVFKETI ILTINTKDGL EYHDTFTGKM AVDIICKIIR TNDRNLALLI
     GRSLDAQKFF RDVTYNHRLR DSIHEVYAFN HIYGEVEFYQ DYNNTNNNSA NNSKHGSITE
     GHPQFQQVLL QQLPAHTTNS QPPTPSTPTM SNEGSTYNLN NNKEIPANST SATGVNGVFT
     ILTDCYSPTC TRNNLCYSIA CPRRLEQQAR LNLKPQGGLK RAVSRLSLHD KEENKTLWYE
     TVPQSILDKL DKREKMRQEL IYEFIYTERD YVKDLEFMTD FYIMPLRNPA NNIIPERERE
     VFIRTVFGGV SDLLRLAKNM SEALTRRQLQ QKPVIDTFAD IFVDFVGGFE PFIKYSGNKV
     FASFEHERQQ QVNMKYARFL DAIEKKPESR KQDLSSFLIK GIQRPARYQL LISGIIKNTE
     PESPDYKSLL KAKEEIEKVL VQINIQTGES TDRHKIMVLH RLLGKQNLET KNHFKLNYSH
     RIIYQVTLNR KRDNEKIDLY LFEHALLLIK HKIQNKREQH KIFEKPIYLP LLFVNSGYDI
     PTARSIMGNR LDGSLLSDPN LKNKAETSTS YINTSSSSSN KLPINFLGLG SNSVHATLFA
     DDMTNQNQVL QQIHQQQKKL IGQNDIFSLS KYETRRFHGN NKINCAVPCY GGKKLLYGTD
     SGVWVSTVRS ISATSNEKIC SDPTMVISKV YVTQIEVLVE YSKLLILSDK SLYEFDLSCT
     DSLDHNKNTR SGKLILNYVS FFKTGICDGR LLVCAAKHGS THSINIFEPT NPFDHKSSKN
     KNKKYDIREI SFSSDPVSIS FLKTKLCVGC TKGFEILSLE KGKKEPILDE ADPSLDFATQ
     RESVTPLAIH RLGKNFLLSY SEFSFKINRN GWRTQHDWSV FWEGNPQNIA LFYPYLLSFE
     PGFIEVRDLD STNLLRALVG ENIRFLHSNE HEALYACEEN GYDIIVSIDF LNLKPKVTQL
//
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