ID A0A0D2FIL5_9EURO Unreviewed; 1235 AA.
AC A0A0D2FIL5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW86502.1};
GN ORFNames=Z517_01900 {ECO:0000313|EMBL:KIW86502.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW86502.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW86502.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW86502.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846969; KIW86502.1; -; Genomic_DNA.
DR RefSeq; XP_013290310.1; XM_013434856.1.
DR AlphaFoldDB; A0A0D2FIL5; -.
DR STRING; 1442368.A0A0D2FIL5; -.
DR GeneID; 25301390; -.
DR VEuPathDB; FungiDB:Z517_01900; -.
DR HOGENOM; CLU_002632_0_0_1; -.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000053029; 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; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd11883; SH3_Sdc25; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF99; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS50002; SH3; 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:UP000053029};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 80..139
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 810..943
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 979..1218
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 136825 MW; C0B5465C95054A15 CRC64;
MSTSRRGTQD STSQGASAKS GSVLAAAFQY TEPSRPSHTT SRSRSSSVHH AGMSGLSPRR
RAQQAAMNSY VASTDLPPPP PPIFVRALYN YEADDHTSLS FRQGDIIQVL TQLESGWWDG
VINDVRGWFP SNYTAEITNL DELNEAGIGG HDESETGSGT EEDYDEEEED SDAQTQDEDS
DLPIEGASQA QEEAAFWVPQ ATPDGRLFYF NTLTGVSTME LPLETPTSSD ESGPRDRNNF
HVPEQTRPPP EMMAGGYAQN EEDYDGSASE ADGEQSFLSS RKKGSGSMTS ASISTSTSMD
SLNLSSSRQL GSQATNPFTN TFDSHLNMSL ALPPLGTSST SFAVGLPPKL SKSPTPRFFL
DDGGVAAVTW DSLVENMRTA IEAYRHAIRT RARADYVRRA EDISDHLRML LAAGSGTTDN
HSGNPSIISS NKALYPHFRE MMSKFSKLVL SSHIAAADWP GPDALTKCLQ EADGVMNGVY
GYVEVARQQR GEEIPRLFPG FILGSTVGGS WRDNNIDSQT NLDEVSFMDS NDEIGWRPSE
PLDANLLRHI DDSKRGLSAA IRRLEEVLVL TEKIVTPARL SAIGDAVCQG AGMILEQFRP
WVSYVESIDL SALGNVFQKP SLVDFGSQKQ KAYDSIGELV ATCQAVTTPL PDEWAEVRGE
SLDTRISNVR TVCQQLDTHV ANVGYALELL LPATTLNPAL ATNKRENRVT DGGETYQAHH
LRSDSKHAAN LRPALADLGQ SKSYTLGEDP MTDKLRRPPN KDKARQFFGQ IPPDLNPVKA
TIEPSYPVDE VPWYLQLDHA DEITYDTKND PPQVKSGTLT GLVEQLTRHD RPDTTFTTTF
LLTYRSFTSA SELFELLVRR FNLQPPAGLN RDEYSIWEEH KQKPARFRVL NILKSWLEQY
WMEADDGNSQ ALLERMLAFA NRTFTTTKIP LAKALTSIIE QRLKGGEALS KKLVLTLTNS
APAPILPKNM KKLKFLDIDP KEFARQLTII ESKLYGKIKP VECLAKTWER KSKSDSSSDT
APNVQALILH SNQLTNWVSA MILGQSEVKK RVVIIKHFVL IAEQCRVLNN FSAVTAIISA
LGTAHIVRLS RTWNAVNPKT NAILESMRNL IASSKNFALY RETLRQATPP CIPFLGVYLT
DLTFIEDGIP SLTKNTELIN FAKRTKTAEV IRDIQQYQNV PYSLHPVPEL QEWISDNMKN
AGDSHDDMFA QSLKVEPRER EEEKIARLLS ESGFL
//
