ID A0A1J8QH50_9AGAM Unreviewed; 619 AA.
AC A0A1J8QH50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Arf-GAP domain-containing protein {ECO:0000259|PROSITE:PS50115};
GN ORFNames=AZE42_07172 {ECO:0000313|EMBL:OJA11060.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA11060.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA11060.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA11060.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit apl3 and beta-type subunit
CC apl1), a medium chain (mu-type subunit apm4) and a small adaptin
CC (sigma-type subunit aps2). {ECO:0000256|ARBA:ARBA00034519}.
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:OJA11060.1}.
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DR EMBL; LVVM01005256; OJA11060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8QH50; -.
DR STRING; 180088.A0A1J8QH50; -.
DR OrthoDB; 389572at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR CDD; cd14833; AP2_sigma; 1.
DR CDD; cd08831; ArfGap_ArfGap2_3_like; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR027156; APS2.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR45686:SF4; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H; 1.
DR PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF01217; Clat_adaptor_s; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}; Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 10..130
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 147..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 67886 MW; BA0D3096F76B8C8A CRC64;
MTDPSKAESE QVFKVLRMQK GNRMCFDCQA RNPTWSSVTF GVYICLDCSS VHRNMGVHIS
FVRSTNLDSW QLNQLRTMKV GGNTSATEFF TRHGAAALLT DADTKKKYSS RAAELYKEEL
ARRVKEDAVN FPARVVVDGV DASPASAEVT QGEDDFFSSW EKPAIPKTTT SSAPTSPPVI
GRPASTGPVA SRTATSSSLR SNSSTSINGP PKFGATRLTS STSAIGSSAT SISQKKSKLG
GLGAKKASTP IDFAEAERKA AEEAERIKQL GYDRLREEEE ERAQKEAEKA ASQTKAKATD
AAVKVSTVQG KVDLQKGNSQ DLERLGMGFR KLGFGAVPTA SSTSSTARSS PANDDAPTTA
RDKFGNQKAI SSDMYFGRKD YDPSFVSESQ ARLQNFQGAT SISSSQYFGR DEEEELERAS
SDGGMLGDGS LANLELAAKD VMARVMANQD VQNVGESIRS GALKNRQGKT RLSKWYVPYD
DDEKVRLRGE VHRLVAPRDQ KHQSNFVEFK NYKIVYRRYA GLFFCVCVDA NDNELAYLEA
IHLFVEILGG QHTCISPPGY HLLASIYSDS FFDNVCELDL VFNFYKVYAI LDEIFLAGEI
EETSKDVVLS RLEALEKLE
//
