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Database: UniProt
Entry: G0VKX4_NAUCC
LinkDB: G0VKX4_NAUCC
Original site: G0VKX4_NAUCC 
ID   G0VKX4_NAUCC            Unreviewed;      1303 AA.
AC   G0VKX4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=CNH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=NCAS0J01830 {ECO:0000313|EMBL:CCC72162.1};
GN   OrderedLocusNames=NCAS_0J01830 {ECO:0000313|EMBL:CCC72162.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC72162.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC72162.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HE576761; CCC72162.1; -; Genomic_DNA.
DR   RefSeq; XP_003678500.1; XM_003678452.1.
DR   STRING; 1064592.G0VKX4; -.
DR   GeneID; 11525880; -.
DR   KEGG; ncs:NCAS_0J01830; -.
DR   eggNOG; KOG4305; Eukaryota.
DR   HOGENOM; CLU_002884_0_0_1; -.
DR   InParanoid; G0VKX4; -.
DR   OMA; HEIITWE; -.
DR   OrthoDB; 2044425at2759; -.
DR   Proteomes; UP000001640; Chromosome 10.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46572:SF1; RHO1 GUANINE NUCLEOTIDE EXCHANGE FACTOR TUS1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT   DOMAIN          499..689
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          745..885
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          942..1280
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..202
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1303 AA;  148224 MW;  DE15BE853AE5628A CRC64;
     MYRSSPSRGP KRTNKESLPL PKLPPLNTRD AFIDRSIHHV ATADDTLNTA ISDLSIGWTP
     ISENAVHNPQ TPSSSHVQSP PSTGPRTGSA SNSSKYRSRR RPPPPQTVLS AGAIPTTATM
     DSSFRSSNMD TPTKMKHRSL FSTPVQNTMD NDGSTATLQS SETGNFVDQD SVISSQSVLS
     PTSPSIRKHH PTHHHHHHHH HHGKNDDDIT ESYIDKILPP IPVLDSINDF FEAAMPPPLL
     LASTSRNVSG LSKNSDSVES YYSDSNYTFN NSTKRHATEF SSLLGGKPLQ LAPSITAPTQ
     PFNIDLLDEN KLYQCYSVFH LSDIYEWILK IYFEWFNEYI FGKIEFYQVV QRLLEFQLST
     SINQDIIDSN VDMIIESLIS QSAIRFEQND IVETEDSVED LVIIVAGLDV QGVFTQLLPC
     YSFVDTDYHS SNTACTQCYS YLCNHTSSST TSSTTTPING PVKKDLKISE IINKSVGVWT
     EYWHLTPSDL RDIEPREIQR QSFIFDLIIL EERSLNMANA AIEIYGKRFH PDLLPSEPNF
     SELAFDVFVP LIELHKEYLL SPIFWKIKTM GKFIDGIGKI YSKWCEQAHD IYLKYATAMA
     TVHEIITWEK AHHTEFAKWL NEIDNSPEIS RSKMYYDVIF FGGFFKSLQN MPLTLQSILK
     NTDPNVEDYL YLQKVIKDIE RLSSQVDKAH GDAIDHRNLI RFSEQLVVNI NSHLGYSNLS
     KKNKKIPHDS DQDNFDLRLY DPSRKLLISG LLLRKRDLWL DPSPIYLVLL DNYLLITERI
     IGNDKKTIRY KLIERPIPMD YLSLEKRTPN EDSSTTSLIK PLTSPLRKSA RIINQQSNES
     IETRINSLEC SFKIRNIATN ESFTFITESQ DERQRWVNTI INTLKSTSSL RVNDAIKLEV
     LSDNFAYNDK DIPSNLSVVP EGSEIDMALK AHRPTSNSTL IRTTVLCSLE FKFEGKCFLL
     VSTSDGVFLS KNKQCKMRFV KVLQCNEIRK MEMNLKMGLL FVLDDKKLCC YNLPSLLGAY
     YDPSEYLIDN CIVGIVIRDK VGSFKFADDF GNSKHLFYER KGKIIVVTPE FDQITKSLKY
     FKEYKQYRLP VFNNGLTVPE VKDIVIFKKS FMVCSSRGVF LFQADFNDIG NLLPTFIAND
     GAFECVDNET LGGSSDTSSS SGSTKQRMAE LVKNDISTNK TKPITCLQLG DPREYLMIYD
     EAIVRMNAYG QVVDWRKDIL VLDFYCANAT FHMGYLILIG ENLLQVYNLN SRKMRLCDAM
     PIQIIKGKRI KLMSMSENDD PVVILSHPNI ANKQLLLKCK IGK
//
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