ID A0A1L9VB11_ASPGL Unreviewed; 1136 AA.
AC A0A1L9VB11;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=ASPGLDRAFT_68833 {ECO:0000313|EMBL:OJJ81118.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ81118.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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; KV878907; OJJ81118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9VB11; -.
DR STRING; 1160497.A0A1L9VB11; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_68833; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:UP000184300};
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:PRU00288}.
FT DOMAIN 647..753
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 827..951
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 248..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125229 MW; 302CF58C63949FB1 CRC64;
MGNVGSRLDD TGSLFFKDQS RFTVSHVSVI NSKNRVLLNL APNAFPATRY TAKRDLGDDS
PIEYVQDPDL PPTAQVPNFI LRLNNEDELQ FNFTFIMRQT QTGNVANSTV NGVSTSLPEV
TDTVLTGLTF AHASNSKELD NLITREFHAN PNLQNNSNVQ LVGDYSTGGS PSVQFEWSWK
WKPPKTVEDR GGGWRNSCSF LDYDSRANRL NTLAHFSFWV QNNVRLLPSP QLLSPNLDLH
FPIRNRMPSS HSVRSHGSDA DTTASAHMPL PAPSENGDTN ANSNANNNSN TNNNSNNNYP
PHPQGPPPPP PVKLDLPTSR PGEDMSAVDD GPLFRATMKA LEQKTGNMRT KIKKVLKKAE
AAQQAQVACN EAVSGFLGAL NEASTSNANA IQPALDHYYE KSARQILRYE QVNTAQLQKL
VIEPLVKLYN NDIKQAEAKK KEFEEESRDY YAYVSRYLGQ RQDSLKEKKR VESDSKYQAK
RRNFELKRFD YSSFMQDLHG GRKEQEVLSH LTKYADTQAK NFLAAAHKVE VTVPQLDALV
HEVTQADKEF QFLRTEREEK RRALEKNSNT YLEPESFPNS GAPTTLSATS NGAQTQNTEN
ELGRADSTGS QVRNVISNTS TMSSQTNQTV LGTSGGASIS PTDASGQHRK EGLLWALSRP
GSHIDPKGIN KQAWHKFWIV LDQGKLSEYS NWKQKLDLHM DPIDLRMASV REARNAERRF
CFEVITPQYK RIYQATSEED MANWIRAINN ALQSAVEGRV VPPPSAVSSK NDGTGRDIGS
VFTGKSSSYS GHHSNSTGSN NVNRRTTVGA RPGYVRTDSN SYDEDPAKLL QAVRNADQGN
NWCADCGSTS KVEWVSINLG IVLCIECSGI HRSLGTHISK IRSLTLDVHS FSNDIVEILL
QVGNRVSNMV WEAMLDQSLK PNASSTREQR LRFISAKYSE RAYVQQLPSP RSRFTTPDES
LLASIKKHDI QGVLYGIALR ANVNVTDRSR NTHAVFLALA AADPASPGST PTSSASSRPS
TATSIKAIPF PVAEMLVQNG AEIPLQPPPI PLSPAAQLYL SQRTSRMPPP IGVGAGRTTA
DTLGTLPTIR NDYPGSSSHT PSSSLDNSSR DREKLHKRGS AGARFAGKVA SLGIDR
//
