ID A0A1F5LM59_9EURO Unreviewed; 1143 AA.
AC A0A1F5LM59;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=PENARI_c006G01581 {ECO:0000313|EMBL:OGE54298.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE54298.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE54298.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE54298.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE54298.1}.
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DR EMBL; LXJU01000006; OGE54298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LM59; -.
DR STRING; 1835702.A0A1F5LM59; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000177622; 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:UP000177622};
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 654..760
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 835..959
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 229..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 125686 MW; A779CE3B6869C22C CRC64;
MGNVASRLDD VGNLFFKDQN RFSIASVTIS NSRRRLLTLS PNAFPAARFV AKRDAGDDTP
IEYIQDPDTS SSVSVPTFML RLSNDEELIF NFTFIIRQTQ TGNAPNSVNG VSTTLPEVAD
TSLTGLTFAH ASNSKELDNL ITREFHANPN LQNNSNVQLI GDYSTGGTPS VSFDWCWRWK
PPKVTEDKGG GWRNSCSFLD YDQRTNRLNT LAHFSFWVHN SVRLLPSPQI SSPNLEPPVP
PRSRIPSTQS VLSQNSDTES SNPYLPSTTP PETENALPPP PPTAPPPPPP AKVDLPHSRA
GDDMSGVEDG PLFRATMKAL ELKTGNMRTK IKKVLKKAEA AQQAQTSCNE AMEAFLGSLN
DASTSNANAI QPALDHYFEK IARQILNYEQ LNTIQLQKLV IEPLIKLYHN DIKQAEAKKK
EWDEESRDYY AYVSRYLGQR QDSLKEKKRA ESDSKYQAKR RNFELRRFDY SSFMQDLHGG
RKEQEVLSHL TKYADFQAKN FLAAAQKVEG MTPQLDALIH EVNQADKEFQ FQRTEREEKR
RYLEKNSNPY LEPDATVTGT ANLPSVSAGT VNSGTSTEVE LGRADSTGSQ LRGVISNTSS
VSSQANAGSV VSSSGVCAPA SNPASAGNTG QNRFKGIRDL EEQNSFSSDR SGGQQRKEGL
LWALSRPGSH IDPKGINKQA WHKFWIVLDQ GRLSEYSNWK QKLDLHMEPI DLRMASVREA
RNAERRFCFE VITPQFKRIY QATSEDDMSN WIRSINNALQ SAVEGQGTPP PPPSSKDSST
SRDIGSVLTG KSSSVSGHHS YSSSSSNAGV NRRTTVGARP SYVRHDSNSF EENPAKLLQV
VRDADQGNNW CADCGSSSKV EWVSINLGIV LCIECSGIHR SLGTHISKIR SLTLDVHSFS
NDIVEILLQI GNRVSNMIWE ATLDQTLKPN ATSTREQRLK FITAKYVDRS YVEGLPSPRS
RFATPDEHLL ASIKKNDIQG VLYGLALRAN VNITDRSRNT HATFLALAAA EPASPGSTPV
TLSARSSAKA IPFPIAELLV QNGAEIPPQP PSIPLSPAAQ LYLSQRTARS SAFSTPIPPP
GRATAADTLG SLPTIRGKDS VSSTSHTPTL AESKEKDREK LSKRGSAGAR FAGKVASLGI
DRQ
//
