ID A0A137NSM5_CONC2 Unreviewed; 1493 AA.
AC A0A137NSM5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:KXN65767.1};
GN ORFNames=CONCODRAFT_53450 {ECO:0000313|EMBL:KXN65767.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN65767.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN65767.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN65767.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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DR EMBL; KQ964821; KXN65767.1; -; Genomic_DNA.
DR STRING; 796925.A0A137NSM5; -.
DR EnsemblFungi; KXN65767; KXN65767; CONCODRAFT_53450.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000070444; 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:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 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:UP000070444}.
FT DOMAIN 808..913
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1114..1315
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 168..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1493 AA; 166969 MW; CD31BC00CA0A58FA CRC64;
MNKNELEPIN DESLLTYNVH TITFEGERWV PLSEFEQCQE ERVTLVTQNK SLWKVIEKQR
VIIQQLQKLN SVKAGSGASS LRNKSVEDLP NQYGSTHSLK LAEHNIAQLD IKQGINLLKS
QSEGAVNFPP AIPSQSPSLN EFSIPEALTP YSPSITDRIS LSERTIDSSI KENSSQSIQP
PVDVQKPSLL SPVDELSEKE IHSRQDITEN EYQDSREINH SKKVREIEQR TGSPTSLMFP
STASLLSNEG ESSHLIVGRG SEFGGTNNGS RLSLDIAQQN DADIAQIIDE ASIEEITKHS
GIQDASDDEI HSKIQHVTYD SIKEANEAKV HNDIKHDMYS NIQADAQEDT KYNTSQDEVQ
ETVHYNNQYD TQDSVNSYQD SIQDTFDEKA KDLSLGAFGN RNGDKPSSSP PPLESKESKS
KTFRLTLEHP QPIIAPSVAS HTNLDSIQDS YDNDSISSFE NGSYERPSIL HSKNPSSVRS
APSIDNFHNN TFFTPPPPPS HPPPPDVTSR FQQKYVLPRK SSRRVRKATH GEADMPRSQF
ESDESIAANG HRPISKMYNS DPSLFRSNTE KIYSTSPDIS PISSSLQREG HTRDPSFDPN
RSASTIQSML NSENNDSHTN DDADTCANSI TASTAESNNS ISDNLVSIPV LPSDPTLLSI
DSRINILRGY VDHLKIRPIT FKAKINDQNI SVLVLVMGLY IILPSNDSEK PGKPFDLWIL
EKKYSDFMNL DGKIKMYQQA DHVQLPDQSM FTSNQPHLTK ARMLALKKYL NDLKDAGLGL
SREYCSFLST NLLGPEHKEA PTARPLKTYF KAGYLLKRGK KFGRLKQRYF VLNGPVMDYF
ETKDGFYLGS IKLAGSKIVK TIVGSVHSDI YENFTYSITI LEAKKTGSVK HIFFIDNSAE
WESWTSSLNY FSSGGLIAED SPPTNNTSTT VNDNVIHKRP SMLPPPRPTQ TENNHATGLV
HRPSLTDLNY NSALPPTPNS VPNNYNSALP PIPSDADEDS EILPETRFNT QTSLPSTLAE
DKKYFDKPLP PPKIDTHLAP SAQSEPSPSS PRDTTPTTEP SSAFKMLNAK SKVKIGLGDV
LRKEKEPEKP RKAFNWTKKN FFKRSGGSGK VFGVPLDVAV DNSRVKVGYE LPAVFHRCIE
YMEAKEARME EGIYRLSGSQ SVIMQLKEKF DSGNDYNLLK SSNKYDVHTI AGLLKLYLRE
LPNSILTAKL QPDFLSITDI LNYSDKVNEL GRLVCILPLC NYTLLRTLIA HLIRIIEKHE
LNKMTLRNIG IVFAPTLAVP AGIFSLMMAE FEYVFCVNDA GNASPRLMQP DAEPNLNSLT
TNITSIPIPR NKTIAQLQDG LEDRRSNCNS LVYKSSVPES LVNAERGIQF SNENPLKLSE
QDELDMLNLS YIPPPPPLHE EGSHTPGELS EDEYYEENDN FHYDELPIEQ LEKLHEFDPE
YVDQFATDIP VEAEFDITTK QEQGELTGVP TDKLLDNIRL SIDVKGIKNK SKN
//