ID A0A178DR85_9PLEO Unreviewed; 1401 AA.
AC A0A178DR85;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAL45599.1};
GN ORFNames=IQ07DRAFT_213236 {ECO:0000313|EMBL:OAL45599.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL45599.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL45599.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL45599.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441657; OAL45599.1; -; Genomic_DNA.
DR STRING; 765867.A0A178DR85; -.
DR InParanoid; A0A178DR85; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR CDD; cd05137; RasGAP_CLA2_BUD2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 503..662
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 717..958
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 155916 MW; 4F18F496FF1E4298 CRC64;
MDQTRRARRE VSAADAGAAD RNFPATIRAV TPELDSSPSA TITPTDDAFA SQAFSPPISP
RAHNSQPSRT ANPRAFVARA SSETDYRNAR EQARPRTRTL EERSTRDRSP SNLFVAGRHR
IGSVTSTSST FQSLEESVVT SIGHISTISP QSQAQHQQPP PRTSSTSSRS RLVKPPPRTA
SPSNAPPESW VSPVPASDVK KLKALMRSTC GKMQGLLAFR RGEPHPWALS YCYINEESGS
LVYEPKNDTS YTRTLVPDLR GCRVNSAYDG EAYTAYINVV VHNSKLEVHL RPPTQDEFDS
WFAALLCWSP MRPKGIQNRM AKPQAPVVME RRLTDSRRHS EVSLLKDTPK KEAPIIKVGK
MIYWDTSVTY TNTGTPKSAG SSARPQAYRV QSHGSRRWRR VSCTLRENGE LKLYSDTDVT
LVSTVQLSQL SRCAVQRLDP SVLDNEFCIA IYPQYTASSS ALSILRPIFL SLDSRVLYEV
WIVLLRAFTV PQLYGPKSDA LNEEGTLSPS FGTQDMFRME KSLFVRVIEA RLLPPVSPKV
SDNSTPVRPS SSATTNPGGY LVEVLLDGET RARTMVKNEG TSPFWREEFE FLDLPALHTA
SLLLKKRPPS YSRGEKNTFE APSSSDPYAE GGYAGMTFDQ MIGKTDIYLD DLGPNQEMEK
WWPLVNMFGN SIGEVLVRVS SEECAILMAR DYYPLSELLH RFSNSLTLQI AQMIPNELKK
LSEYLLNIFQ VSGAAGEWLC ALVEEEIDGT LKESPASRLR FSKRLGSSDS NESALGTFGS
ASDRELFVRD MGNNAKLEAN LLFRGNTLLT KSLDLHMKRL GKEYLEETLS EKLREINEKD
PDCEVDPNKV SSQHELDRNW RRLINCTEEV WRAIYNSVSR CPQELRLIFR HIRACAEDRY
GDFLRTVKYS SVSGFLFLRF FVPAVLNPKL FGLLKDHPKT KARRTFTLIA KSLQGLANMS
SFGTKEAWME PMNTFLNSHR QEFRKYLDDT CSISTTSSPA PPIPPSYSTP IAILHRLPPT
FKEGFPSLPY LIDHSRNFAM LVNLWLNNTQ KSAPDIQAGD GDLLRFHNIC VSLNERTKDC
LNRAEPAERP SSSLSVKWEE LVEQLQGTSF IESGRGAATR NNRAPIMEEE FPTSPSNGED
YSSSSTSTPI TMKPPPKGRH QQNSSISASA SSLKSNSSAT ISYTNPFASK AWSGNRYGQT
GNDTVSVSHS ASASASASAS AAEDTPPGSS DGLHMASPPS YPPTLTQPSV SSSFNYSNPN
VHINQSNPAG LSANSYGRPP RSAGGQSMEG SEAGSVHEEE YTTALPAFSS KEGKDKERKD
RGFRGVLPFQ RKRKDKDKDK DKEKDKGKDR DRSADQDDRS GSALGVYGET TLRSRGTLRD
RDRDRDRDDR GPRDEKKDED F
//