ID A0A068SFM2_9FUNG Unreviewed; 1392 AA.
AC A0A068SFM2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cnh-domain-containing protein {ECO:0000313|EMBL:CDH60031.1};
GN ORFNames=LCOR_10830.1 {ECO:0000313|EMBL:CDH60031.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH60031.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH60031.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH60031.1}.
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DR EMBL; CBTN010000082; CDH60031.1; -; Genomic_DNA.
DR STRING; 1263082.A0A068SFM2; -.
DR VEuPathDB; FungiDB:LCOR_10830.1; -.
DR OrthoDB; 2734900at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
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; IPR041675; PH_5.
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; PF15405; PH_5; 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:UP000027586}.
FT DOMAIN 654..844
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 879..1008
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1039..1350
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 120..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 158310 MW; 4F53606F4BB182F7 CRC64;
MHYLIYKGNG IFKYVMSGIK QVTNADLVLR RGNDKVMISK TVTSSEHESV PFLFSSKHAK
GWVLLLDNTR FLEYIPPISV YLVIWLYSTD EDGNASRTSE GHTVSMNNAQ MPSQQTSYYH
EGGMVMPYPP NNNNGEGGGY PPPYPPRNAA PPPLPPRDPR DDQRWMSFPQ APGGGGGGGM
PMPAPQMYPP SSAGPMPYPP PSNTAMYPPQ QQQQQQPLYP PRTPSAPYRP ESPYPPRPSS
PYQHQEKHEL QPPNDNDYRS SPSSAHTSPH LSPHMSHPDA MPTPLYPPRP HHHHHQEPTQ
PQQHMYPPSV PSPSISSEML MPNPPNHPPP AASSSPSSSP AMPMPMPMPM PMPGGNRYYA
FQPQISYPPP GYARPPAQDF ISRFRSSTVQ PSSVLEAEHA ARKELREQLL RKDSTRQHAT
EDSSDEEQED EGRLESKPLP PAPSEQDAVS PGSDDDDGDD RVLFESTDPA LLSVVAKMFA
RSIKEVVRLR QLSFTDEYPD AFTGQEALDT MTQLLQSQYP GNEHMREYCL GLLTALHNSS
PKRLLVSVDP FNKIKRHIVQ GSAEETFQLK STRIVGVYTP MTRCYVKGCR PGEGCYAPRC
PNKASVQEQE TEDALARSVS QRTIAHSEGM QVAETWGQRM DPEFYQSVDK RERDRQEAIN
EIIYGEEQYL KDLELLREGI IDPLKESQVI DEAEWEFFAR DVFNNHAELE QLSINLFNDL
YERFKEHEDG CIPGIGDILL KHFDHFRDPY ALYVPNVNLA EYIVADLKRS NPAFNEFLAS
RLSDPRLNRQ PFRHFLLRPV LRLPRYPLLL QALMKKTDKE DPKYEILAQC NEKIAQVCKL
CDQLTATVKT RVEILLLNNA LTCRQGEFYD LKLTDPQRKI YYRGDLKLEN LGLDIGEKFI
HMIVFDHIVL LTKARKTSDT TEYKIWRRPI PLQMLHVQGI ENDFMLPSQL SMTSSSTYAS
LKPSLTMRSE NLSLVLTHPG RHGETYYLQC ANQQEKDQWL FALKQARSDL KQLVDAFNII
SMESTFFRDY GASSTSEGCG KVTSTVPFVT ENNVEMLAIG TSVGVYFKPL KGGRARPILS
LRNVTQLGVM QKYQILLVLA DKMLYAYPLD ELTSPKNSKA PDRLAHEISE PVHFFQTGVC
HGVELLVYAR QKTVYTIFTA LKPIRSIGSE SRSRGISLGH RGFFRSHSTK SPWFQDYKEF
SVGAQAVNIH FLKSKFAVVC DKAFEIIDPE DLSSSRSIPN EQDPQFDFLE QRSDGLRPLA
MYRMQSKFLL CYNKFAFYVN NRDQSLVPRD ETSALLCEWE SHPDNIVYHH PYVIAFDQRF
IEIRHVETGD LVQMIPGNDA RLTHYNGNGY LVGEPLVIHG CIVHSRNQQF QDVFYLEPNK
ELEEQQQQQQ QQ
//
