ID G1X7K0_ARTOA Unreviewed; 1187 AA.
AC G1X7K0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=AOL_s00054g917 {ECO:0000313|EMBL:EGX50831.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX50831.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX50831.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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 -!- 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:EGX50831.1}.
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DR EMBL; ADOT01000093; EGX50831.1; -; Genomic_DNA.
DR RefSeq; XP_011120535.1; XM_011122233.1.
DR AlphaFoldDB; G1X7K0; -.
DR STRING; 756982.G1X7K0; -.
DR GeneID; 22891512; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_002728_0_0_1; -.
DR InParanoid; G1X7K0; -.
DR OMA; FSFWVHN; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000008784; 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 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 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; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|RuleBase:RU369028};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 648..754
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 847..973
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 787..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1131..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 130124 MW; D3749E78CC43BBFA CRC64;
MGNVGSHPED PAAVFMRDQA RLTVTSLVVT NSKKKPIVSI TPNAFPSTRA VAKKEIGDDA
LVEYVQDPYV ATQSPGILLK LTNEDELNFD FTFVARQRRD EAGTATDTNI TGLTFILASN
HRELDDLVTR EFHADPNLHK HANVDFLGDY STGGSPSVSF TWSWKWRPPK GVPEKSSGYR
NTCAFVEYDQ RAHKLSRLAE FSFWVHNKQQ STPLGLGLLD PRLLTPKLRA TSNISTDSNA
LSAASEPLSE PLTPGIESTT FDIASPPQPS KDTACYKDDD ILDDGPLFRA TMKEMESRTT
ILRQRMKKVI RRAEEAKRMQ AQWNDSLSLF AESLREVAAN NTSGTKPALE EYFERSAKEI
LRFERHNEAH LQKFIIEPIT KLYTYDIKAA EAKKKEFDEE SREFYGFVSR YLGMKNDSVT
QKKKTESDSK YVVKKRNFEI KRHDYGSFMQ DLHGGRKEQE MVSHLTKYAE AQAKSLLSTA
KRVQELQPQL EAIMEEIKNS EKQFKIQRSE REERRRAIEM GATVSEDSSM SDVNGQQVVG
TSAIPPPSLP VIMTDSGSLV ANMETPLPTG GNSTTPDVVT IRAVSSHSRS SPPLANESTT
TIAASTVSSS APVGLLSPTA TADSGKFKGF RDLEDKPVNG ANTVTGVDRR KEGLLWALSR
PGGHHDPKAL PKVNWHKYWV VLAAGQLCEY SNWKEKLDLH NEPINLRMAS VREARNQERR
FCFEVITPQY KRVYQGTSED DMNNWITAIN NAVKGMLEGS KSRTAFDPSK LVDDPTKKDI
SQVFGKGSSL SHLSSGQIAV RDPSHHHHHG SSGGGNSLAA NNLQRRITVG SRPTYPRRSS
TFNDDPDKLL QMIRDADVEN GRCADCGSTV KTEWVSINFG IVLCIECSGI HRSLGTHISK
VRSLTLDVNS FTPDLTELLV RIGNKTSNSI YEARLDPKEK LGSNQQVTRE MRLKFIKAKY
EDRAFVRPLA EGSGKMADEV LVEAAKRGDL VGAVYGVAIR GNVNFVDERG VHVVYWALNS
GDPVKEGAEP TNNTTEPLSP GHKGKEVKEP TFPLAELLLQ NGGAIGEVMA GKKLVVSSAA
KGYLALKSAK AGGFDGVKSG GVGGGVSGKS GSGREKAPGS SGGEGGSSLA AVDGSGSSRG
GIRSSQSLKG GSQSGDERGK KDKEEKLRKR VSTSGRIVGS RVLDSMR
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