ID A0A1Y2WFH0_9PEZI Unreviewed; 1097 AA.
AC A0A1Y2WFH0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=M426DRAFT_8566 {ECO:0000313|EMBL:OTB07568.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB07568.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB07568.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB07568.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369028}.
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DR EMBL; KZ111530; OTB07568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WFH0; -.
DR STRING; 1001833.A0A1Y2WFH0; -.
DR InParanoid; A0A1Y2WFH0; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000242955; 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:UP000242955};
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 627..733
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 813..937
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 230..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122046 MW; 761BE2AB1D463B42 CRC64;
MGIVSSRPDD GAAVYLRDQN RLSIASLVIT CPRKRISTTI VPNSFPATRA TAARSISDPS
PVEFIQDIEP SATPNFLLKL NNDDELIFNF TFVIRQEEGG AGVDTHINGL TYVYASTNRE
LENLVTREFH ADPNLHKNAN VELVGDYNTG GSSSVTFEWS WKWKPPKTTE DGGGGWRNVC
SFVEYDQRAH RLDTLARFSF WVANTSPFLS HPNSPSPAFQ LAVPPRIRVP SSQSVDSRIS
EQEEPSSPLH PLHPQSDALS VAPTIVPSLR ESVKLDISCP RPGEDMTVSD DGPVFRATIK
ALEQKTGNMR TQMKKVLKKA EHAHTAQLEA NDAFVGFMEA LREASATNAT AVQPAIDYYF
DKIAKEILAY ERTNALNLQK IIIEPISKLY TYDIKQAESK RRDFEEESKD YYSYVSRYLG
QRQDSVKTKK LVDSDNKYQT KRRNFELKRF DYSSFMQDLH GGRKEQEVLS HLTKYADTQA
RTFLTTAQKV EGMLPQLEAL TNEVQDADKE FQYQRREREE KRRVLEKSNL QYNEPETVTS
AANVATTHGT NGSQHVSDSD LGRADSTSSQ LKAVPTGNSG PMVSSGTDLS RSPGSLHSPA
QTSKFRGIRD LEERDFSQLT SLEKNSTHRK EGLLWALNRP GNHVDPLNLN KQGWHKFWVV
LDQGKLSEYS NWKQKLDLHM DPIDLRMASV REARNAERRF CFEVITPHYK RVYQATSGED
MSSWILSINN ALQSAVEGRG LKEKPTPAGE STTTSLKRDI GSILTGKSIS LNHGSHHGPH
TNTSSAPPSR RTTVGARPST TRTPSSHFDE NPDKLLQMLR DNDQGNCWCA DCGSGVKVEW
VSINLAIILC IECSGIHRSL GTHISKVRSL TLDITSFTPD IIELLLLVGN RVSNMVWEAK
LDPGLKPSPQ ATREQRLKFI TAKYVDRAYV EPISPTLSRY PTADETLLAA IKRNEIQQVI
YALALKANPN VLDKVRGTHP VFLALAAADP ASPSPTTPVS GRQEPEARVV PFPIAEMLVQ
NGAEIPAAMP AFPLSRSAQL YIEQKRGRNA AIEASGSSLP GSVSPSPSER LQRDKDARLQ
KRISAGGRLA KSPIPER
//
