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Database: UniProt
Entry: A0A165SM43_9AGAM
LinkDB: A0A165SM43_9AGAM
Original site: A0A165SM43_9AGAM 
ID   A0A165SM43_9AGAM        Unreviewed;      1292 AA.
AC   A0A165SM43;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dbl-like domain-containing protein {ECO:0000313|EMBL:KZT25369.1};
GN   ORFNames=NEOLEDRAFT_1065480 {ECO:0000313|EMBL:KZT25369.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT25369.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT25369.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT25369.1,
RC   ECO:0000313|Proteomes:UP000076761};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425572; KZT25369.1; -; Genomic_DNA.
DR   STRING; 1314782.A0A165SM43; -.
DR   InParanoid; A0A165SM43; -.
DR   OrthoDB; 5100844at2759; -.
DR   Proteomes; UP000076761; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
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; IPR000591; DEP_dom.
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; 2.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 2.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076761}.
FT   DOMAIN          248..432
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          473..664
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          699..840
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          883..1192
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1292 AA;  147765 MW;  03C7CFA46C5BD8C2 CRC64;
     MPDLLGESSS HNRSYSTQSA NESGPSNGRT IHTDYPKDIK SRLGLNPEDF EEYDDDDDVY
     GYSDSEDAED RFVNFALLSH IAMRLRDKVP RGTHVKGGIP YPRAFTGKDI VSTIQGQIQR
     ELLISHGIST NDRRIALQIA RSLQSQLFFY EVEWGGRVLE DGVEDVYMFL DDEEGTSEAR
     IEREELPTGV ITMLTKCYSS DCSEDQPCYA YLCPRKVRIV CTTLRWRKEN GWEVPEEVIR
     TLPASEISRQ TIIHKVISKE KQYVEDLDLV ESLFIKPLRI ADPPVIHPDR LEDFIEEVFG
     NILDLRECNR RLLENLYVRQ REQAPIIQRI GDVFLDAATE FRLAYPIYVG HLPLAEKRMK
     DETDNNVEFR MFLELSARNP DSRRIDLKHF LTRPSEHLQK YPVLLEAIHH ETAEGNPDAD
     FLMEAIQAIK NLQTVAQLLT FQSAMGKGPT GKFEWHNLVS DEYRNSLPKK ESKRQMIIFE
     LIKGEMAYVK DLESFETIYI RPLRAADPPI IPPSRLESFI QDVFHNYRQL LYHHRKLLEN
     LHEIQREQHP VLRSITEAIL DAFLNFREAY LEYVPNYPIA AYRIDEEMAN NPLFKAFVDQ
     CVRHPDAHKL DIKNFINRPI PRLLRYELLL KNVLEETEPD HEDQEAIPQL LDVIKALGKE
     TEPGVASAKQ KVELWRYNAN LVFKPGEHVD MDLLDENRSL IHTGKLLRQP DTGLGLEGWT
     ELFVLLFDNY VVMTKPKERD SVTKYHVNRR PIPLDLLTLA SFTDPPTQRG TGLIGFNRGA
     KHADQPTPPA LNSADSATDA KLVYPLTIHY NGRMGGLYML YAESAQVRAD WKQKLEEAIG
     LRKVVQESNK VFEIDTLSTD TFLVPSILAG PTNPSWNNEN TFTGKVTCSV PFTTADGRAL
     VAIGCAEGVW IGFRHDSRSM RRVLHLKQVT QCAMLEDFGI FLVLADRSLF AYHIEALVPS
     SPQVVHASQT PQKLSKNSEN VHFFSVGNLN GRTLVVYMKK NRLDNVFRVL EPVVDNINER
     NRAPASLGSR FGFRSQRSEW FRVYRDFFLP SETFDLIFLK AKIAILCTKG FEIMDLTDFR
     SATVPQRDDP RMERLARRCE SCKPIGMFRS NEDEFLLCYD EFGLYVNRHG DPSRTAMTIE
     WEGTAEKAAW HPPYVLLFDT RFIEVRHVET GRLVQIIPGN DVRCIWDGRS SSSNMNLVTP
     GRDGWTENGL NQEARVHGVM NAPEAVRTGG MGPQRGNRAI AQHVFELVPT VPLYLPGSLH
     SPSNSAYFPA SNGPLSNSPP HSPRMTPVNN RW
//
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