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Database: UniProt
Entry: A0A165FIJ2_9APHY
LinkDB: A0A165FIJ2_9APHY
Original site: A0A165FIJ2_9APHY 
ID   A0A165FIJ2_9APHY        Unreviewed;       381 AA.
AC   A0A165FIJ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 22.
DE   SubName: Full=ArfGap-domain-containing protein {ECO:0000313|EMBL:KZT09023.1};
GN   ORFNames=LAESUDRAFT_811104 {ECO:0000313|EMBL:KZT09023.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT09023.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT09023.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT09023.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV427613; KZT09023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165FIJ2; -.
DR   STRING; 1314785.A0A165FIJ2; -.
DR   InParanoid; A0A165FIJ2; -.
DR   OrthoDB; 1022106at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd08839; ArfGap_SMAP; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR044732; ArfGAP_SMAP1-like.
DR   PANTHER; PTHR45705; FI20236P1; 1.
DR   PANTHER; PTHR45705:SF1; FI20236P1; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          10..131
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          121..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  40687 MW;  DBC0B15C41FA23B0 CRC64;
     MSRQDKAITE RHAKQLREML KRPDNKVCAD CKRNDPRWAS WNIGVFLCIR CSGIHRSMGT
     HISRIKSVDL DIWTPEQMES IQKWGNRLAN LYWEAHLKPG HIPADHKMES FIRSKYESRR
     WAMEGPPPSD PSSLESQAPS TPVHTPAAAA AAAVQTPPAP RTSTPVESKI TATASRLSSI
     SVSRQPQPHQ LLSASVANRS HQAQTAPPAQ AQSQAPAATH ELFSLDFHAP AAPPSQPEAE
     AAPAKKDAKQ DILSLYSKAT SPAVPSAAFG QFTSVQAAWG AFDVQAAQQT AASPVTSMTG
     TTGVGMWGTS SGWTGAPAAA AQPSIWSSPA SQPAMSQQSL FTTSDVWGSS GGGTAAEGHM
     FSSSVKQKKD DAFGDIWGGF K
//
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