ID A0A074ZGT2_AURSE Unreviewed; 1181 AA.
AC A0A074ZGT2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUEXF2481DRAFT_2695 {ECO:0000313|EMBL:KEQ97766.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ97766.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ97766.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ97766.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584753; KEQ97766.1; -; Genomic_DNA.
DR RefSeq; XP_013346134.1; XM_013490680.1.
DR AlphaFoldDB; A0A074ZGT2; -.
DR STRING; 1043005.A0A074ZGT2; -.
DR GeneID; 25363374; -.
DR HOGENOM; CLU_003874_0_0_1; -.
DR InParanoid; A0A074ZGT2; -.
DR OMA; NCQEIFM; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000030641; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09394; LIM1_Rga; 1.
DR CDD; cd09395; LIM2_Rga; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000030641};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 20..82
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 992..1179
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 167..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 651..678
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 187..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1181 AA; 128932 MW; A581494349B683E8 CRC64;
MDADNNSNYP ESPMEEDEVF LCKGCGEILE QGRAFELAGH RWHLGCFRCH SCATLLDSDA
NLLLLGDGSL ICNNCTYSCD SCGNKIEDLA ILTGEQAFCA TCFKCRNCKR KIENLRYART
SQGIFCMNCH ESLMARRRKR AKASKQIAAG ASNPLVLDKS LPALPPSAVP QSALREASPS
GSYSSDHLKA SHDRKRDTSP MSMSDDSKKD TLTLPASTYK QERASTMSSN TMTTMSDVDD
GFLPMAYDPN PAPPPLPRRS HPESTPRMSD NLSPQGALSR SERNRPSSSR SVSTERDSIR
SPGVTHADRT RQQGLRNVSG NSTPVTTPAV ASPSSVTSQQ RPRLPTTNSA NFGLAPPEPF
KLQDVPRDRR VSRNSPRVGK NSPTSLDTQT QSRHTPTDSN LSLSPASVDT PSSSINPFDD
PKLREASSTA GPPAAKHPAR GDSLPPATDK THTSRVASPE TTPALKQADA AHERKQSATS
AQFVDAPSHP RTEAESTTAS GIEVPMAPPR AANRPSAPSK SVANDDFIAP RLPPAPPATE
RPRAESVGNP QLDHNPAASP RVWRTHLPKH SAGEAFSMEE EMSRILRGDE QKRKENEHAG
VLRRVSNAVK HGRSFSDKSI PLQKTPTISS ADISSPILIT SPISSPGQMD VASLKSQLRR
AQQKIAELEA DKLGLEEKMD TSADIKQVNT ELREKRSTMA FLDTQREMVV RELEIMTEHL
TRAKEDNKPL DISQLKSEIL QDFAHSLQKL KDNLGSQIED LVHKRNELTD DITNLIQVKD
KGLQEFESLS SKNLQLAELN NQLVSGIQDM YKSHNVKNGS MDRSPLTNGL GIYNGSSRGD
MTSLHSSSLQ ESSSLHDLMP HAADAEPATV LTAPQVVNIR KGQPKKFNWK KGSSGLAKNV
TKGIKGAFAG SNDRGVPIKA DGTYDITGMP YSQMQAGPGA IMGDQPLRTG DAKGFGFFSS
GQKNGMKPPG TLGKNGSSSN LLAEPPSVLF GSDLRERCDY EKRILPSIVT HCIEEVERRG
MDMEGIYRKS GGSGQVKLIQ QGFEKDGIYD IADPDLDIHA VTSALKQYFR KLPNPLITYE
TYDPLLEAAQ ITEKEKQIAG IKAALEAMPQ AHHDVLEYLV QHLCRVVKQE SENLMTPLNL
SVVFAPTILR PLSIEREMSD MQAQRMAVQA LLEHADAIFE N
//
