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Database: UniProt
Entry: A0A1X2IF96_9FUNG
LinkDB: A0A1X2IF96_9FUNG
Original site: A0A1X2IF96_9FUNG 
ID   A0A1X2IF96_9FUNG        Unreviewed;       985 AA.
AC   A0A1X2IF96;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   RecName: Full=RhoGEF domain-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCR42DRAFT_51753 {ECO:0000313|EMBL:ORZ15329.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ15329.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ15329.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ15329.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ15329.1}.
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DR   EMBL; MCGE01000013; ORZ15329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IF96; -.
DR   STRING; 90262.A0A1X2IF96; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000193560; 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; cd00014; CH_SF; 1.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd13246; PH_Scd1; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 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; IPR010481; Cdc24/Scd1_N.
DR   InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   Pfam; PF06395; CDC24; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT   DOMAIN          239..413
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          437..555
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          900..985
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..812
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  111294 MW;  5514B2D20C95B5EA CRC64;
     MASTTLQRRT PSLGALSTIT PPHSQHSTPS LAPTTSSNTP PPGTSLYHTC RLVLDKLAFV
     PGMSCWLDME EDNLSPSLSP INTSSPPLMP LSTTSPALTA ASTSTADSAI TTTSCSTNNF
     NSDPLSKLCY LCRRGTPLFT LFNALNTNQP LKMDPNPKLN QVNNCKANVY HFLVACRKQL
     LFPEEELFAV SDLYVDDTNG FVKVVNTVLK ILQLLEDKGI ISSQCASRDS CPMVPPKDIR
     DQVVFELLST ERKYVQDLET LQTYMRELQQ QRILSQDTVH YLFGNLNALV DFQRRFLIEM
     EKTAENQPQD QHFGLLFSQM EGAFSVYEPY CSNFYSAQDL VVQEAPKLQK LNIMNPTHQL
     TSLLIKPIQR ICKYPLLLNE LIKSTNKEWS ITLSEMADGL DTMRRVADKV NETQRKHENL
     QMVVELKRRV DDWKGISIDK CGQLLLQDKM VVSAYDNERE MHIFFFENRL LLCKECKDNN
     KNRNTITIKK RRRGTLEPKG KIETSMITCI HNISKNGEWA LMIEWKEQDV EKFILKFRNE
     EQYKLWESTL NKQKGFQSTP SISSSSNNHV SGINSTMPTS LPLPQLLSSN DNWSFIDPDD
     EEDEVDFIED DGDYHGSGAR SRSNSFSAHI LNTFSTRPKS SRNNSTDMSA MKSLTVNATT
     GRPNTPGLNL QPLPRSNHGI PIHQHDVSQQ PSSGDYFFYP SSPPPSNPSS PTSSSRVSPN
     NSSSGRSFRD HTSSSSQQLH HHYLQQQQQH YSTKGLPMPR EPMTPAMDYF TIPTIDNFDA
     VVGRPGPSLS ERHQYQQHQH HNNHHHRKQM PPPTRSRAQS SPIIQSSESH IRRDGGGMTR
     FMDKSATWEQ YTHQPTTAPL PRLSDKKSSV SLHSQMDHIL ISSVSTTATA TATTTAPVSP
     GQLKVKMIYN DGAFSLVIPQ HISYIELMER VEQKLHAMID LRPGTSFRLK YRDEEGDFIT
     MSSTEDVQMA FDGYQHSGAR LYVFL
//
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