ID A0A367LN29_9HYPO Unreviewed; 1105 AA.
AC A0A367LN29;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=L249_3583 {ECO:0000313|EMBL:RCI15652.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI15652.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI15652.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI15652.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI15652.1}.
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DR EMBL; LKCN02000002; RCI15652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LN29; -.
DR STRING; 1330021.A0A367LN29; -.
DR Proteomes; UP000253664; 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 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:UP000253664};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 637..743
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 823..947
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 38..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 121323 MW; 6A3DA074C41FA973 CRC64;
MGNVSSRPDD GAALFLRDQN RLAVSSLVIT NGRKRSSLNI LPNASPASRL SVSRPTGEAS
PIEYVQDPEP SNPANTPSFL LKLSGDDELI FTFTLVMRQS QSPSSSNVDA AASAQSDTSI
SGLTFVCAST SREVENLVTR EFHADPNLHK NANVDLVGDY GTNGSPSKSF EWTWKWKPPK
AVEDRGGGWR NSCSFVEYDS RAHRLLTLAS FSFWVSSTSV TLSHPGSPSP PFLLASPPKI
RVASAHSVDS RLTAGADVDE PVSPLLPPNE PAVPPATPLA KEPVKVDVSC PKPGDDVTVS
DDGPVFRATL KALEQKTGSM RTQIKKLLKR AEQAHSNQIE ANEAFHAFMD ALREASSTNA
NAVQPALEHY FDNIARQVLS YEQQSTTNLQ RIIIDPLNRL YQLDIKQAES KKRDFEEESK
DYYAYVSRYL GQRQDSVKAK KLAESDSKYQ NKRRNFELKR FDYSSFMQDL HGGRKEQEVL
SHLTKYAETQ TKGFLDTAKK VEDFLPQLEA LSTEVQVADK EYQYRRRERE EKRRGLEKSN
TPYMEPEQAS LSSTIPAILN GNAGSTSDSE LGRADSTGSQ VKNAIPIGAV QTVAAHGMEL
SRSPGSLTQN AMGSPAPSKF KGFRDLEERD SSQATASQRK EGLLWALNRP GGHVDPRTLN
KQGWHKFWIV LDQGKLSEYS NWKQRLDLHI EPIDLRMASV REARNAERRF CFEVITPSFK
RVYQATSEDD MNSWIVSINS ALQSAMEGRA GHERAGHAQG SGEMSGQRDI GSILTGKTHS
AGHGASPPHH AGTGSVLPSR RITVGARPTM VRTSSSGYDE NPDKLLQMVR DADQGNCWCA
DCGSGSKVEW VSINLGIVLC IECSGIHRSL GTHISKVRSL TLDIKSFTVD IVEMLLLIGN
RVSNMIWEAR LDPAGKAGPQ ATREQRLKFI TAKYVERAYV EPISSTLSRF GTADETLLAA
IKKNEIQQVL YALALRANPN VVDRMRGTHA IWLALAAADP ASPSPTPNVS AAEREDKTVP
FPVAELLTQN GAEMPAWLPA FPLGRFAMQY YEQKLGKGNG GAGDGLSSLP ANAGANEKLQ
REREARLQKR VSTGGRLAKS PIPEK
//
