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Database: UniProt
Entry: A0A1V8TR44_9PEZI
LinkDB: A0A1V8TR44_9PEZI
Original site: A0A1V8TR44_9PEZI 
ID   A0A1V8TR44_9PEZI        Unreviewed;      1264 AA.
AC   A0A1V8TR44;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0A51_15167 {ECO:0000313|EMBL:OQO17202.1}, B0A51_17292
GN   {ECO:0000313|EMBL:OQO13830.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO13830.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|EMBL:OQO13830.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCFEE 5018 {ECO:0000313|EMBL:OQO13830.1};
RX   PubMed=28684563;
RA   Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA   Stajich J.E.;
RT   "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT   antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL   Genome Announc. 5:e00397-17(2017).
RN   [2] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQO13830.1}.
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DR   EMBL; NAEU01001480; OQO13830.1; -; Genomic_DNA.
DR   EMBL; NAEU01001067; OQO17202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8TR44; -.
DR   STRING; 1974281.A0A1V8TR44; -.
DR   Proteomes; UP000192386; 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:UP000192386};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          27..89
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1070..1260
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          823..885
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        189..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..604
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1264 AA;  136976 MW;  2B46D7F5B42E2393 CRC64;
     MTTIAPAMES PTNFPESPLE GEGEDVYPCK GCGEILEEGK AFELAGNRWH IDCFRCNTCG
     TLLDSDANLL LLGDGSLICN NCTYSCNACG NKIEDLAILT GDQAFCASCF RCRNCKRKIE
     NLRYARTSQG IFCMSCHESL MARRRKKSKG TPRPSAPSAT RSGSAIEKAL PSLPPGAAPE
     AAFSPDSETP PMETYTAGTN ANSPPPRALR PTKDGAADKF KRDVSPMSDE ARRDGQTLPA
     STYKESRSSH ISSGSDDGEN EGFLPMAFDP APAPRPPQIA RKKLPQSSDL SQQIALDSPP
     PRDYFAGRSA SKPHRDALRE DRSVSSRSAS TERDPSHAAT LGSTKPSPHI AYQDKSRAHK
     KVTSNSGQST PGALSTAQHS PSFAGATDRT ERPKAQTLNT GSYTLGPGEG FKLQEVPKEK
     RAASRSSSSK ENRSPVIVSP VDAAEKGNDR LEPTVTASPV STDSPQSGVN PFDDPRRREG
     PPSAAPPAPP KFQERPTRGD SLATGQLKPS ASVRSTPPTP TTSLAPNAQL SAHSRDTSSV
     SIPASFTDAQ STISAKTVES PTNRSSFDVP PRASSRPMGA PKPATNNDFV TPRLPPPPPP
     PAELHRTQES ISTRPSTDSR SDAQRSPALL SAGLQRQSTD GGFNMEEEMA RILRGEKANR
     DSHPEATQSV LRRVSKAVKH GRSFSDRGAT ATKSPSVTAG EVPGTPMTIS SPIMTSPAAK
     ESVDSLRASL RRAQQKITQL ETEKQVLEEK VNSSSDIRQV NSELKEKRST MAFLDTQREM
     VVRELEVMTN HLGKAKDSNQ PLDMPTLKDS VLQELSESLN KLKDHMGSQI EDLIRRRNEL
     TDEITNLIQM KDKGFQEYDI LSTKNEQLER MNNQLTQNFQ EFYKSNRGAN GGAPDVWKSG
     ATNGLGIYHP GAKPDSQLTS EMRSLNLVST DSSLPNLLHE TEAEPATILT APQMVNIRKG
     QPKKFNWRKG GAKAVTNVTK GLKGAFANND RVTTRDGLDI GVPYSSTQQT VAGSEQSSIN
     SKQGLQPNGL GWLAQKNGGL KAGSLGSTMR NGSSTNLTIA AGDGSVLFGT ELELRCDYEK
     RVIPIIVTRC IEEVEARGMD VEGVYRKSGG SGQVKNVQAG FEKEGTFDVS DEDLDIHAVT
     STLKQYFRKL PTPLITYDVY DTLLEAGQTS TVGDREQQML ALRAAVHELP EAHRNCLEIL
     ICHLARVMTR QEKNLMTPLN LAVVFAPTIM RPLSIEREMN DMLLQRTAVQ AMIELCDGVF
     GEEE
//
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