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Database: UniProt
Entry: A0A1F5LQ69_9EURO
LinkDB: A0A1F5LQ69_9EURO
Original site: A0A1F5LQ69_9EURO 
ID   A0A1F5LQ69_9EURO        Unreviewed;      1260 AA.
AC   A0A1F5LQ69;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   RecName: Full=Ras-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENARI_c004G04511 {ECO:0000313|EMBL:OGE55354.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE55354.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE55354.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE55354.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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:OGE55354.1}.
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DR   EMBL; LXJU01000004; OGE55354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LQ69; -.
DR   STRING; 1835702.A0A1F5LQ69; -.
DR   OrthoDB; 22721at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd00030; C2; 1.
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; IPR023152; RasGAP_CS.
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; SM00239; C2; 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; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT   DOMAIN          503..671
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          726..960
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1191..1213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1260 AA;  141533 MW;  1E8C2D705AF3C2F4 CRC64;
     MEPDPNAFKR SSMQQALYSR PVERRASKKS SSRDRHGMVY PDSFRETTIR TVTPESHSPA
     NHSPLSEPDP LSGGTSSPQS TLPSRPTEPE RRREFSKHSS RGGEEDTPPE GRSQRARSRT
     TAAEEQRNET TPSSFKTRTR IGSINTASPS QPKVPEDPSS SIGFPSIQSR QYHSHSVPRQ
     RSSKPVTGIA DSQDSFASPL SSSEATKILQ LMKTTCGRMH GILSFRTAST TSWTSGYCAI
     NVATGSLIYQ AKGEPALAKT LIPDLRGCRV RTLFDPELQT TYLSVHTFTS GLGIQLRPHV
     NETFDSWLAA LLCWQPIRPK GVQNKMTKPQ EVVIGDRRIP ERRRNSESAA QKDATIIKVG
     KMLLWDKPSA SGAMPISGRR VSTYRQSRAL SSSWQKVSCT LQENGFFKLY TETDVSLLAC
     VQLSQLSRCA IQQLNPSVLD DEFCIAIYPQ YAAHPVPDSN VRPIYLALES RVLFEVWFVL
     LRAFTIPELY GPASKTEDPN KTPEADATVT PVLKDMFRIE RFLNLKIVEA KLFRAKEDTP
     RSRKASRSHG HGQQTPTSKV SDYYTEVLLD GEIRGKTAVK YRTTNPFWRE DFVFSDLPPV
     LSQASILVKT LNPTQKDWTL IAHGASNQDV NAVNAVNLLD EIEISANDAI FGRVDMRLEE
     LDAGVDTEKW WPILDDQDQA VGEMFMRARM EETVVLMSDE YAPMSELLHS FTNGLTINMA
     QVMSSELTHL AEMLLNIYQV SGSTVEWISA LVEDEIDGVH KESTTNRLRY TTRIHSNNSQ
     ESGQEREVLV RDMGRTATVE ANLLFRGNSL LTKALDLHMR RLGKQYLDDT IAERLRDIDE
     SDPECEVDPS RVPRHEDLER NWRNLTALTT SVWKSIAGSA SRCPPELRRI FRHVRACADD
     RYGDFLRSVT YSSVSGFLFL RFFCPAILNP KLFGLLKDHP RPRAQRTLTL IAKALQGLAN
     MTTFGNKEPW MEPMNKFLVG HRSDFKDFVD SICAIPADRP APIVTPSYTT PIQILGRLPP
     TSREGFPSLP FLIDHARCFA NLIRVWLDVA PARLNDLGEL DVNLAKFHQT ALDLRARTEE
     CLSRAEQAER PSGSLEIKWE ELVDSMERPV TFYDERSSQP STPAADPMMS GSAPAPSSHR
     NSIGYFASRP SIPRRSTDHA PDADEDTPPS SSSATWDQSR IPFAIPRWSD ARDSTGSSKN
     SSTYSLEYSD TSKVRRASVT KESSSKYRFF DFVPAPSRRK HKDRDQSQNN NSHEDLRNES
//
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