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Database: UniProt
Entry: A0A178DR85_9PLEO
LinkDB: A0A178DR85_9PLEO
Original site: A0A178DR85_9PLEO 
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.
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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
//
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