ID A0A0B7MXH0_9FUNG Unreviewed; 1623 AA.
AC A0A0B7MXH0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ras-GEF domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=PARPA_04501.1 scaffold 14269 {ECO:0000313|EMBL:CEP10736.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP10736.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP10736.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP10736.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN725192; CEP10736.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7MXH0; -.
DR OrthoDB; 5476208at2759; -.
DR Proteomes; UP000054107; 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; cd06224; REM; 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; 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:SF364; GUANINE NUCLEOTIDE EXCHANGE FACTOR LTE1; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 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:UP000054107}.
FT DOMAIN 411..537
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 1299..1619
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..728
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 181432 MW; 011CB06517DE2580 CRC64;
MPLRDEDPNA PPPRKRNNSL IPIELMKNNS GEGGRECAAL ATVFGVPEYI DSKVFWERQH
EGLQPKKQPF RPSTSTGGTV ENNSKYGHVS MNNVSVESRI LGSTISPNED DIILQGSQVR
SKFLISSYVD AVLDPVGSNE LTLGSTASPS DPVPTPTKSF SLPHIPTVSK FNDILIEDEH
GTELMFPANP SSILIHSSTP IMRASSLSSI QSAFTLSSQI NKQQQQQQQQ QQPVEEDQDS
LKTDSKLAVV IGTPEIFDLV VSDQDERFII WGPDPIALSS SMATATAPER PSSYANLYNN
QHSRPDLKGF SSNTTSTIAR SNSIQTSGKR TTSRRSSFVS ARLSAQSWSE SLRLSRPAPK
PSTSASTDQR STAATASQGS LLLKRAFGLN KSNKIKNGAA IDSETKSLAD IPKVIEAATI
HKLVEKLTNT LDYTFMTDFF LTYRDFLDSA DLCQLLVLRF YWALEDDEES RRIVRIRYDV
TFVVLRHWLN NYFVHDFIGN RPLRIILTEF LNALPHHPLV QTSPRDQRIV KILKRVVRRL
KKLYYNQSSG ASRVKVIPPP PPTAEQEQMG ELVRAKLSQN AIRRKTALGV DMSSHHNGNM
AVQDARYAPV VVVGSLNVKG PFIDSGLDSF KLPFITQQTV QQDSGDVVVV DDGQTIRSSV
HHRYDQSVHQ PAEAEEGHNN AAVGASSVAS VASDDSLESE LSAGETAPLE SEGFEDEDDE
EDNEDVNDDD YHVLQSSSQD YDDQGDEHER EWIREQQETL EYFQSMSKMS IDQSDLGSIS
INTSNLNQQE SITHVITESP TAIQNDGPPK ASSIEFVNIE KEAASSSPVG MDLTPKPVHR
VSSERWCKEE DAYRPLHSDN ALPDELLKEL SGDESQSKSP TGLSRKLSRR SIEKRKSVKS
FQETYSPRNS APSSAATSPY LTGAHSDKQA LEIPELPALT PDMLDQYGAV PKKKTAKKRR
KSQLRKRLST QEQTTEPIEV FASIPYEATQ IVNSEEVREQ DPKEEVPKHR LSRVLSKVFR
YSQYEEAVVP IALNSSVAES KAVSNEVVKN LEEKIQHDPS PRQQSQQQQQ QQQQQQTNQI
VSLIAQRLRH CSVDESDDSM EGRCACSKCS GNSQSTATCK RLSVMLIADD DRRRSLELRR
KRATSVDLDQ QALLNQLAAQ SSDEKSTKNL KSGPVYLGHL QARSLITSGI GDAGDEQNLS
DHNDDSSTIS SVPSGRSIQT EAQASSCRER LSLISDTATS HVVQSKIEID IPSASSTRLE
IDPATSTLDL STSSIPRPMA NDTNSPFRIN GRSFIMSYRT SMLASQLCFV ERDVLVKVGW
EELIHCKWTK MDSSGNINNA PIPQKPMSMF ENDFNVDDDE QINYTRQTEQ RRIEEQGIEQ
VIQRFNTVCQ WVSSEIVRTR NISERVKLIE KFIRLAKKCK MYSNYATLVQ ILLGLQSPAV
ARLEKTWSKV STKCQRQLSQ LTEFTSPMKN WKNIRDSMTE VAEEYGNSPA EVQVEMPGTT
ANRQKFKKTT RIKIPFGGCI PFLGIYLSDL VFNSEKPRFL QPNLEYQKIY SVNNTRNLPT
CLNQPLVNFR KHRVIATVIK RVLTFQGLAM RYSFDEDGIL LEKCRHLEVL DASEIRDLSA
SLE
//
