ID A0A436ZQP5_9PEZI Unreviewed; 1141 AA.
AC A0A436ZQP5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=DFL_009038 {ECO:0000313|EMBL:RVD81163.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD81163.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD81163.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD81163.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVD81163.1}.
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DR EMBL; SAEB01000012; RVD81163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZQP5; -.
DR STRING; 97331.A0A436ZQP5; -.
DR VEuPathDB; FungiDB:DFL_009038; -.
DR Proteomes; UP000283090; 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:UP000283090};
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 649..755
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 848..974
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 522..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 483..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 523..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 125049 MW; E87E5E84A33F0D07 CRC64;
MGNVGSHPED PAAVFMRDQA RLTITSLVVT NAKKRPIVSI TPNAFPSTRA VPKKEIGDDA
LVEYVQDPYV TTQSPGILLK LTNEDELNFD FTFVARQRRD EAGTATDTNI TGLTFILASN
HRELDDLVTR EFHADPNLHK HANVDFLGDY STGGSPSVSF TWCWKWRPPK GVVEKSSGYR
NTCAFVEYDQ RAHKLSRLAE FSFWVHNKQQ VTPLGLGLLD PRLLTPKLRA TSNISTDSNA
LSAAGDPLSE PLTPGVEATT FDMASPPQPS KDTTCYKDDD ILDDGPLFRA TMKEMESRTT
LLRQRMKKVL RRADAAKTHQ GNFNDSLGLF ADSLREVAAN NTSSMKPALE DYFERSSKEL
LRFERHREAH LQKFIIEPIT KLYNFDIKIA ENKKKEFDEE SREFYGFVSR YLGMKNDSVT
QKKKSESDSK YVAKKRNFEI KRHDYGSFMQ DLHGGRKEQE MVSCLTKYAE AQAKSLLNTA
KRMQELQPQL EALMEEIKNS EKQFKIQRSE REERRRAIEM GATVSEDTSS SDIGGQQVVG
TSAIPPPSLP VIMTDNGSLA ANIEVPVAAS GNGTTPDVVT IRTVSSHSGS SPPLASESTA
TIAASTVSSL APAGLLSPTG TADSGKFKGF RDLEDKLVNG GSSSVSGVDR KKEGLLWALS
RPGGHHDPKA LPKVNWHKYW VVLAAGQLCE YSNWKEKLDL HNEPINLRMA SVREARNQER
RFCFEVITPQ YKRVYQGTSE DDMNNWITAI NNAVKGMLEG SKSRTAFDPS KLVDDPTKKD
ISQVFGKGSS LSHLGSGQIA VRDPSLHHHH GSSGSGNSLA GNNLQRRITV GSRPTYPRRS
STFNDDPDKL LQMIRDADVE NGRCADCGST VKTEWVSINF GIMLCIECSG IHRSLGTHIS
KVRSLTLDVN SFTPDLTELL VRIGNKISNS IYEARLDPKE KLGSNQQVTR EMRLKFIKAK
YEDRAFVRPL AEGSGKTADE ILVEAVKRGD LVGAVYGVAI RGDVNFVDER GVHVVYWALS
SGDPVKEGTE AGGTTPATAA EPLSPGSKGK EVKEPTFPLA ELLLQNGGAV GEVMAGKKLV
ISSAAKGYLA LKSAKAGGFD GVKSGGSGGN SGKVGPGREK APGSSGGEGG VRRWRWGVVE
E
//
