ID A0A1Y2DIG4_9FUNG Unreviewed; 1246 AA.
AC A0A1Y2DIG4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:ORY58595.1};
GN ORFNames=LY90DRAFT_381425 {ECO:0000313|EMBL:ORY58595.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY58595.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY58595.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY58595.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-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:ORY58595.1}.
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DR EMBL; MCOG01000066; ORY58595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DIG4; -.
DR STRING; 1754190.A0A1Y2DIG4; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF140; ATYPICAL_BCR PROTEIN KINASE; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000193920}.
FT DOMAIN 326..438
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 778..985
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 142938 MW; 10C52DC583A52082 CRC64;
MAEKESEHEV IERLITKLKE SEERNQELTN KVNELNSFIQ KQNIYIQKLR EEINAKELAF
SQHQQQQHQQ KNGSTSKEKS PKTPLSIKTT IPNQGVISYK YSKFASPTTD GFMSSTLSPI
FHVEHIRHSS TDDNIVSKDD IHKRKLSHSS QFGKETKYSQ SENNIMLSSS KSIDSVNNDS
NLNLNNSLND FEDKEISSDQ ITVYIQKLEF CKNERNKKDI AFVISIRNSD SGDELWRIRK
SYSDIQNLEN NIKTNYPKEK TQNIGKLPER NLNGLKLESK QIQLKITMEI YIQHLCNIFK
NSVEIADFLS KDIIETDNNI DSTKQTCIKS GYLFKKNNFM GWRTKYFVLD EKKLSFYESK
DGEPNGIINL KHAKVMTVTS SGLNKEKFHH AFRIIEYKDE KGGLSKASED KIFAKHLLCS
ENDNDRDEWV EKIKFVVTKL KEEDNNINAS STLNSSNNLI FKSKSNNTSF DVNDSFENSI
NEINKDHILG SKEIILSPID ASNSNGNDNE IKNENNDSNS SNNEDDENKN SSSNDNGISG
NNEVDTPQNN NNGWDSSEEE EDVNIILDYD EKNYLPEGFN FEDFEKQGMD INEYIKNNAL
KQNNYNNETN EEEEEEEEEE VEVEVEEENN NIINDNDYDN RKNEKDEEDN DSPNEKVDND
DSNNNSPNEK VDDDDSNNNS TNEKVDDDDN NEKIDNNNKN NKSNKKDIVI DDNERVMKQM
IPPPLVPKTK MAFAKTKLMK EEKQKKLHFS FYKFKKNNTN DVDIKESVPN KYKKVFGVNL
ETAVKNSKVK DDYELPAIVY RCIEYLDAKG AYEEEGIYRL SGSKATIQLL KNRFDKYGDV
NLLQDKEIYD VHVITGLLKL YLRELPTTIM TKEFQPRFIE IASIPDREEK IKALGNLISY
LPLANYTLLR CLAAHLVRIV QNSDLNKMTL SNIAIVFGPT LGIPIGLFVL ILSEFEAVFC
WTTLKESEEE ENIMSILFNG PEDYLNVHSI SKAQNEARNK MGLSSTKNSN FQRNSRLKNT
RSSPGLFNEI SQSEEKKNGE NNLLRDGNHS SDNSDSEILP INSDNLITGS IKLRGRSNTT
INTISKNSES LNNNNNNNNN KLVSIIKEES NTKELLKLDS EVEDIINRRC SNLSNESKDT
IQSMEKSSYT SKRKKRQERS SSLSISTQSQ GDYIKNLRRL SCDESPSSVK AVFNRNSQDY
MVGIPDNFRL SEMLAKEIKI KDNEGIMEGK EIRYSKVSYA HRSLAQ
//
