ID K1X914_MARBU Unreviewed; 699 AA.
AC K1X914;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=RhoGAP domain containing protein {ECO:0000313|EMBL:EKD21522.1};
GN ORFNames=MBM_00635 {ECO:0000313|EMBL:EKD21522.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21522.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD21522.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21522.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921428; EKD21522.1; -; Genomic_DNA.
DR RefSeq; XP_007288524.1; XM_007288462.1.
DR AlphaFoldDB; K1X914; -.
DR STRING; 1072389.K1X914; -.
DR GeneID; 18756570; -.
DR KEGG; mbe:MBM_00635; -.
DR eggNOG; KOG1450; Eukaryota.
DR HOGENOM; CLU_010730_3_0_1; -.
DR InParanoid; K1X914; -.
DR OMA; DSGWQAR; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07652; F-BAR_Rgd1; 1.
DR CDD; cd04398; RhoGAP_fRGD1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF138; RHO GTPASE ACTIVATOR; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 70..342
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 506..696
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 76163 MW; B1A7B949A1FE47A6 CRC64;
MADENPDRIL SEPPDSSNTQ RDGTGSTGTP PPPPNVTATT TASTGDDVSP VNGDSSTDSA
PPPAVDPNAK AVHEVVNSEI GISTLLNRLK QSIASAKEFA TFLKKRAALE DEHSNGMKKL
CRVTAESIRR PDHRHGSFLQ SYEEVMTIHE RMSDNGAQFA ISLHQMHDDL GEIATNMERG
RKQWKTTGLT AEQRAADAEA AMKKSKAKYD SLAEDYDRAK TGDRQQTKKF GLKGPKSSAQ
VEEDLYRKLK AADEDYASKV QTAQNLRSEL LAKTRPETVK ALEDLINECD SALTLQMQKF
ASFNEKLLLS NGLNISPLKG NESISKPRSL REVVHAIDNE KDLSKYISGF ASQVPPRTSE
IKYEKNPVLN NPAPAQRHSD TTASSRSQQQ GLPPQSMGVT QSSQQTHMSH PFNQHPPTPA
QGPNSSMQQY GTAPPGGPIR GTSYGSGPMG SSGPPQLSSL PFQNSPPPSQ HQSYHPSAVA
TQAPYSGPPP TLSIVNLPPL KPVFGLSLEQ LFDRDGSAVP MVVYQCIQAV DLFGLEVEGI
YRLSGTSSHV SKIKALFDND ASKVDFRDPA NFFHDVNSVA GLLKQFFRDL PDPLLTAEHY
AGFIEAAKNE DDIVRRDSLH AIINSLPDPN YATLRALTLH LNRVQQNSPV NRMNASNLAI
VFGPTLMGAS TGPNIQDAGW QVRVIDTILQ NTYQIFDDD
//