ID C1FZ72_PARBD Unreviewed; 1219 AA.
AC C1FZ72;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Cell division control protein 25 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_01098 {ECO:0000313|EMBL:EEH44809.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44809.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH44809.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH44809.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275957; EEH44809.2; -; Genomic_DNA.
DR RefSeq; XP_010756118.1; XM_010757816.1.
DR AlphaFoldDB; C1FZ72; -.
DR STRING; 502780.C1FZ72; -.
DR GeneID; 22580824; -.
DR KEGG; pbn:PADG_01098; -.
DR VEuPathDB; FungiDB:PADG_01098; -.
DR eggNOG; KOG1029; Eukaryota.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_002632_0_0_1; -.
DR InParanoid; C1FZ72; -.
DR OMA; DWPGPDS; -.
DR OrthoDB; 68574at2759; -.
DR Proteomes; UP000001628; 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 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 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:UP000001628};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 86..145
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 789..922
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 958..1194
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 152..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1219 AA; 135450 MW; 0C37DFD9650890FD CRC64;
MYLSRNAVPL TVNSKSVLNA KSGNFASAAF HYTEGQPSSN DDSRCHSNNQ TFSHTHMATL
HGGDAYNTTN NNGGAEEAYN SPIESPPALY VRALYNYTAD DQTSLSFRQG DIIQVLNQLD
TGWWDGVIGD VRGWFPSNYC AVVTEPDSIG FGSQFGHEGG DTSAESGADD YDDVDDDLDS
EGNPKDDQPI LLPIEGVRGS KGSEQEEAAF WIPQATSDGR LFYFNTLTGR STAELPLETP
ISATESGPRD RTNIYLPEQT RAPPEVMVGG IDREEDEYDG SGSEAEGESL IRSSHGSSSR
RRRSFISDGM SPATSLDSMN ASPIAKPYSE TKNAHHLPHP ASQLVPNSGM FTRATNGHSA
QSDRITAPSI SSTIPRNFLD DALSTPITWN TLVSNMRQAI DAYRRAIMEG NRAQYVRLAE
DISDHLRLLL AAGSDTTDNH SGNPSIISTN KPLYPHFRDM MSKFSKLVLS SHIAAADWRS
PDSDAKCLQE AEGVLHGVYG YVEVAKQQRG DEISRLVPGF VHGSSSFGGH WQNNNVGTRN
SPVFLDHANR DMGHEPAMVL DSSIIDRIEN LKSTLAASAR RLEDQLVLSE KTVTSRVHLA
ISDAVCAAGT KVVECFQPWM SLVESIDLAP LDRSSQNPQL VDFSFQKQRA YDGVADLVLS
CQAVSAPLGD EWSELRGDTL ETRLASVRCV CRQLQNYMTQ IGFSLTLLLE QAPSEPTITR
DVGTSSKVPS GSIGVPSSYT PAERQPVKTR ANIDKAQRFF GDTIPTEPAN PWFLNIDHES
EVFYDNKGDV PTLKCGTLAG LVEHLTRHDK LDTSFNATFL LTYRSFTTAS ELFEMLVHRF
TLQPPYGLDQ ADLQIWTEQK QIPIRIRVVN IMKNWFENYW MEPNDDANSR LLQRVYAFVK
DSVSKTKTPG CQQLLSLIDQ RMRGQDTSAK RMVPTISANA PPSIVPKNMK RLKFLDIDPL
EFARQLTLVE SRLYAKIKPT ECLNKTWQKK LAPDEPDPAA NVKALILHSN QLTNWVAEMI
LHQQDVKRRV VVIKHFVLIA DKCRAMNNYS TLTSIISALG TAPIHRLSRT WAQVSARISA
ILENLRRLMA STKNFGEYRE ALHLANPPCI PFFGVYLTDL TFIEDGIPSL TQSHLINFNK
RAKTAEVIRD IQQYQNAPYL FHSVPELQDY MLSNMQAAGD VHEMYDRSLE VEPREREDEK
IARYGRLNDA SVFALMGSG
//
