ID G0WH66_NAUDC Unreviewed; 1392 AA.
AC G0WH66;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=CNH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=NDAI0J02520 {ECO:0000313|EMBL:CCD27144.1};
GN OrderedLocusNames=NDAI_0J02520 {ECO:0000313|EMBL:CCD27144.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD27144.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD27144.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
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).
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DR EMBL; HE580276; CCD27144.1; -; Genomic_DNA.
DR RefSeq; XP_003672387.1; XM_003672339.1.
DR STRING; 1071378.G0WH66; -.
DR GeneID; 11494481; -.
DR KEGG; ndi:NDAI_0J02520; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_002884_0_0_1; -.
DR OMA; LLPCYSF; -.
DR OrthoDB; 2044425at2759; -.
DR Proteomes; UP000000689; Chromosome 10.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 524..714
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 798..975
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1034..1367
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..426
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 159275 MW; 961B8F4EF11BF3D2 CRC64;
MYRNHPNEAE DRRYPKDNDL PEKVSLPKLP PLDTRESFLE RAAKKDSDDL TIGWTPITGN
DGPDSSLFSS KTPSPKQQSR TAINSARYSG PSPPLRPPPP TPPQSSSILN NRTRRRPPPP
TPSPVTSQNS SPLIYKFDQQ RLVDQSSPTL SRENMLPHNN NNIARIYHSP AKNSPSSSTP
RLPNLPSPSF SSPSQNKMLP TITSSNKHSS SGEKELPLTP IDFYKPQPLP IATLELRKFS
DSSRNSDSIE SYYSDSNYSF NNSTNKNKNP LTAATATTTS KILSTSTTSS RDITGSEFNS
LLGGKPLDFV PSIIQPTQPF SINLLDENKL YQCFTIYQLS DIYEWILKVY FEWFNEYIFT
KIIFYQVVQR LLEFQIPNNF NQNIIDDNVD KIIESLIQKN AIRFENKNEQ QEVRKQEQND
EDEDEDTIVI IVAGLDIQGI FTELLPCYSF LDTDYNDLSN TSLKCYSYTC NNNSVSSTTT
TPPTLEKKKQ LEISEIIHKS VGVWTDYWHL TSKELSKINP KEIQRQSFIF DLIILEERSL
NMANAAIEIY GKRFDPDLLP NEPNFASLAF DIFQPLIDLH KTYLLSPIFE KIETNGKFID
GIGKIYYDWC NEATDIYIKY ANSMAIVHEI ITWEKKHKTP FSKWLNEIDN SIEITKSKMY
HDVIFFGGFF KSLQNMPITL QSILKNTDPS MEDYEYLKMV IKLIENLSAK VDKVHGDSID
HRNLIRFSTQ LIISKTITNN NNNSKKGSAG YTNILETTTT TTTMSTNSQS ESNMKEEQDN
IIMNEDKLDL QLNDPGRKLL ISGQLLKKRD LWLDPTPVHL VLLDNYLLLT EPTFKNNMKY
YKLIERPIPI DYLNLEKKKS DNNNKETNND DASQSNNNTT NKLLNSPISS TPLSSVRPRL
FNTVTKTFHP SSSPLLNENK NLKNIATSIS NVNPNERGNF SFKVRNTATN ESFTFLAETH
DELDRWVNTI INKLKDINKK SSSFNAVEFE ILSTDFAYVE KDAPINLPVA PEGSEIDVAL
KRFNCNGTGI PPIATTILCT TFLHMENKKF LLIATENGVF LKQYDENKKP MTKILLCSNV
KKMEVNKKLG LLFVLDDKKL IYFNLPSILA CYYNPKQYLI NNCVVGLVIK DKVNWFKFAE
DFGNSRHLFF ERKGRIYVMT PEFDQINQSI KYFKEYKEYR LPIYGNNTGS LNLSHETRDI
IVLKKCFLVC TSKGVYVFND SFNDDGLVIP MFLCGQNTIY SDSTTTIDMP NAEKMLEFVK
NDIINNKTRP ITCFQLPDSM EYLIIYDEAV IKMNHHGQLE NWRQDILVLD FYCTNAAFYN
GNLILVGDNL IQVYNVKIPN MKLCKISPVQ IIKGKKIQLV SSEKCQDVTF TLSHPNLAER
QLLLKCNPCK KQ
//