ID A0A162WAU7_DIDRA Unreviewed; 979 AA.
AC A0A162WAU7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=GTP binding {ECO:0000313|EMBL:KZM18923.1};
GN ORFNames=ST47_g9947 {ECO:0000313|EMBL:KZM18923.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM18923.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM18923.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM18923.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM18923.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYNV01000317; KZM18923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162WAU7; -.
DR STRING; 5454.A0A162WAU7; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF348; GUANYL-NUCLEOTIDE EXCHANGE FACTOR RASGEF, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G04700)-RELATED; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 462..587
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 692..964
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 109088 MW; 34AFFD2D77F8B64F CRC64;
MQPPRRESVQ AGTGTDTGTC PRPGGLQSRD DEHDVDDDNK ESEDASEPQD GDEIANDSFF
QRFHLAHAES HDDQSHDDQS HDDQSHDDQS HDDQSHDDHQ NHDHQNHDNH QSDDNHDDDN
HDDHQSDDNH DDHNHDDHQS DDNHQSHDNL QSHDNHDDNH NVLDASTAGS ASASSTTDTT
PALQHLTFAV LGARGVGKTT FIRRALDLPD ATAPAACTRK WSIDGTPYLV RFLEMSVTDV
HLADRHHLAW PETVHDMATP RIDAAIVLYD VTAQHSLARV PDMLAMLANA HLPFALAACK
CDQHPAHREV DPAVVEQKAT SFLGPLSVFS TSESAPDTHR ACLSVVLRAA IAATAATAAT
APANRPRSHA SSRRRAKSSA VLSMTQKDLW AKKHERASSE LSSHYPRNPS LGAPAHRYKP
SDANKTFFND ESPTYDSDAS DASDASDASD ASDTARSILT VQPSDDNGYT FDQLVDRLLA
QPMSKSDSTF VAVFLALYRR FATPSQLLEA ILKRFDALAK NRDMPMIRVI AQLRYLAVLH
QWVAYYPGDF AFPTTRKLVR MFALAIAANR EFSVAAMEII RDLDVVADDD DTDWACSDRQ
RAQNDQLPAF YNTVLDEDSE DDEFARAIGH MALGSARLSV ARSTTTAASR STAGSLTIVT
QVERNERLAR QLEPNPIKPL SKVQWHQLMA QDDELIAREL TRIDWIMFSS VRPRDLIRDV
SLSTEARKHC KQLDNVTRMT AHFNHIAFLV TNYILLRDKP KHRALMLEKW MRVARQVRKL
NNYNSLTAII AGIKATAVHR LIATRDLVPQ PVTHDFLKLD ILMGSQKSHF AYRLAWENSS
GERIPYIPLY RRDLVSASQG SSTFVGVKAA APTFSPHPGT SVFAAAAGSR ESKEAPLGGV
VGKERINWRK FEIMGDVVVG IQRAQGTPYP AWSKVEDVRN LILDVKISKD DEELYDRSTH
LEATGANEKG RFAKWLEKR
//
