ID A0A0D2C2E0_9EURO Unreviewed; 1107 AA.
AC A0A0D2C2E0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=PV08_05009 {ECO:0000313|EMBL:KIW17814.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17814.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW17814.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17814.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369028}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847494; KIW17814.1; -; Genomic_DNA.
DR RefSeq; XP_016238030.1; XM_016379353.1.
DR AlphaFoldDB; A0A0D2C2E0; -.
DR STRING; 91928.A0A0D2C2E0; -.
DR GeneID; 27332092; -.
DR VEuPathDB; FungiDB:PV08_05009; -.
DR HOGENOM; CLU_002728_0_0_1; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd08204; ArfGap; 1.
DR CDD; cd07608; BAR_ArfGAP_fungi; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR23180:SF160; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN EFFECTOR PROTEIN 1; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|RuleBase:RU369028};
KW Cytoplasm {ECO:0000256|RuleBase:RU369028};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00094}.
FT DOMAIN 647..753
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 826..950
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 836..876
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 232..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 121866 MW; 22F946C79C0C0576 CRC64;
MGNIGSRIDD GSILYLKDQG RLSITSIVVS NGRRKVVLHA VPNAYPAARL VGKLDAADYR
PISFIQDPEA PGLLFLPRLD LEDELDVRFT FTTRQNSGPL PATPSTATAA VDTNISGLTF
AYAANAKELD TLVTREFHAD PNLHKNSNVQ FIGDFSTNGT PVITYEWTWR WKPPKPYEDR
GGGWRNCCSF LEYDSRAHRL NTLASFTFWV NNAAVPSATP LVSPNLELQV PPQRRMVSSQ
SYQSAVSDSE DRADFQNPPS PQVLATEFST TASSVAASNS APSVPVIDVQ CARPGEDVSA
VEDGPVFRAT MKSLEQKTGN MRIQVKKVLK KAEAAQQAQV ECNQAMAEFL RALQEASASN
STAFKPALDH YFTNIAQRIL KYEKENSSLL QKQIIDPISK LYNLDIKQAE AKKKDFEDES
RDYYAYVSRY LGQRQDSLKD KKRAESDSKY QSKKKNFELK RFDYSTFMQD LHGGRKEQEL
LSQLTKYADG QANSFLAAAK KVESLTPQLE ALVKEVSDAD KEYNLQRTER EEKRRNLEKN
GPNAVESDPP YQPLTSTNSQ PTVPNGQTGY TSDTDLSRAD STSSQFGRSS ANGLSPAPSG
TLQGIPTTAL STSPGASSVT PTTNKFKGIR DLDESSVTTS DRSSNGLYKK EGLLWALSKP
GSHIDPKGIN KQAWHKFWIV LDQGKLSEYS NWKDKLDLHR DPIDLRMASV RMARDAERRF
CFEVITPQYK RVYQATTEDE MNNWINAINN ALQNAFEAGG RASQQNSKDL AGREYGHVLT
GKSSSQSGPH GYTQRTDGSG VSRRITVGAR PTYMRTSSNS YDENPSKLLD QIRNHDFENQ
SCADCGSTSK VEWVSLNLGI ILCIECGGIH RSLGTHVSKI RSLTLDVHSF TNDIVELLML
IGNRISNMVW EALLNQALKP APTATREQRL KFITSKYVQR AYVDPVSQYG TADDLLLTSI
KKHDIKGVLQ GIAQRGNVNA HDRSRNTHAV FLALAAADPA RPVSSHSATP SPTMKAFPLA
ELLVQNGAEI PTNPPAIPLS SAAQLYIEQR TARLTPTNGG GHGDTLGPLP VMGSRVSPLA
SDGHARLQKR GSAGARFAGK VTGLGER
//
