ID Q4WNH0_ASPFU Unreviewed; 1508 AA.
AC Q4WNH0;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Rho GTPase activator (Bem3), putative {ECO:0000313|EMBL:EAL88494.1};
GN ORFNames=AFUA_6G06400 {ECO:0000313|EMBL:EAL88494.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88494.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL88494.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL88494.1}.
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DR EMBL; AAHF01000006; EAL88494.1; -; Genomic_DNA.
DR RefSeq; XP_750532.1; XM_745439.1.
DR STRING; 330879.Q4WNH0; -.
DR EnsemblFungi; EAL88494; EAL88494; AFUA_6G06400.
DR GeneID; 3508137; -.
DR KEGG; afm:AFUA_6G06400; -.
DR VEuPathDB; FungiDB:Afu6g06400; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_002671_0_0_1; -.
DR InParanoid; Q4WNH0; -.
DR OMA; HQMFSDL; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13277; PH_Bem3; 1.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF137; GTPASE ACTIVATOR (BEM3), PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06400)-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 849..966
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1151..1367
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..603
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 165175 MW; 2523C9EC416ED2BD CRC64;
MSQLRHGSDN NPSLNQPSAV YPVSQQARDA GFPRSPLTGS LIPRDYLVTR ADAQPLRSGV
VAVTDPSKPM PSPLNTSDHC RENRQDNSSV LQSPVSPRSS VKTAPPPNHS STSRIVHAPS
PSKPSGSGQE STTSSAGDRV CGDPKQHDRG VIAIANDIGA RKLSDTGDSV QSPTSSPVSL
LDSLQSMSGD RTPGHRIMPR TSSIDSAISS LSSASQPHKS SFDASAVSQA DIDRLIATAG
STEAVIIHLL KEKHHAASQN AQLWRLVDKQ RTLILGLNKD LERALKEKER YKKRAKELQN
SIPPVPPTND HIVQSRSADT SAIPASRDLS KQEQAQGESS EAKSTNAGMQ DLCDSSVLSP
NAKVDRRSPA GADSPRLNTT FDNEFSRPGQ IEELDQQSNS QSLAYARKEM LSASPTSLAS
SSSALNETLP SEESQQRLPH PSRKPPPAPL KLGQTQRVAM ENSGNYDSES DYEDILEVDE
LPVERGRRKT RDDDDREREA ALDKEMGALK ATGEEPPQTC DPSHLLGKTP TGGLTAGVSK
DLWQPISSSS PIERQDSLNS AQNPQKIHAP SLNDQSAFAV PKSPGLPLSP RPEDRPIGSP
LPRMPREVPN SLAHLPMSSE NSLAGLALSP RPTNHPNPSA TGASKPNDTS PSHIDAHRHI
ATINHGSRKD TPRSHWSPAR EIYQGLMSED YPGLLLPPNA LPLIRVKVSS SRLRPSRNSY
LAPKPSEEEP VFTLGVFSRS ENLELWRVEK VVAALPQLDQ QIRQSSALWM KLPDRSIFSG
HSPAKIDARR AALNSYFEAL LDTPVDERAA LAICQFLTMD AIEPRDDESS LLKGNCKAAS
EVLPGQDRKP QKEGYLAKRG KNFGGWKTRY FILYGPELKY FESPGGPHLG TIKIFNAQIG
KQSQPANNTN NPLSGPEDDS ENQYRHAFLI LEPKRKDSSA LVRHVLCAES DEERDAWVEA
LLAYVDGQSD NEGTENASPQ SQVSTQARHL SQSTSKPKLF AGGSKKSGKG MNNADADLTD
TVQGFSYDDA VPAEPPLLGP PSEKQPPRSP MSPLEAAMEP SDTNPASDHV QLSSKVISGP
TNGTVIQDAG AWGNKTVTTT KEKKRSIWGF RTRSSYDLAS QLQASQEPSS AQAVVNPSTE
RKDLVRPVFG IPLAEAVQHC APHGIDVDLP AVVYRCIEYL KAKGAATEEG IFRLSGSNVV
VKALKERFNT EGDVDFLAGD EYYDVHAVAS LFKQYLRELP TTVLTRELHL DFLRVLGACR
CFPSFLHLFQ GTILIKSYLE LDERQKKILA FNSLVHRLPR PNLALLRALV QFLIIIINNS
DVNKMTIRNV GIVFAPTLNI PAPVFSMFLT DFESIFDKMP EGCSEPVELK VDRPALPEDI
RSPRHQMFSD LPTPAYSQTT FRRPTEVVDD SRHDTGFISI QPTYEQSSHN LVEHYNQQPD
SAAMNRMLMP SVDSSRSAKA KRRESSMLFM EYNHQDSGLP AMRNDQSKSP PITPELSHRL
QTDLRESR
//
