ID A0A2T4ANT8_TRIHA Unreviewed; 1102 AA.
AC A0A2T4ANT8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=M431DRAFT_75964 {ECO:0000313|EMBL:PTB58745.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB58745.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB58745.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB58745.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; KZ679676; PTB58745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4ANT8; -.
DR STRING; 983964.A0A2T4ANT8; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000241690; 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:UP000241690};
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 634..740
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 818..942
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..423
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 521..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 122032 MW; C43195FF4587A3F4 CRC64;
MGNVSSRPDD GSTLYLRDQN RLSITSIVVT NPRKRTSIHI TPNAFPASRD PESSNGNGPP
NFLLKLSGDD ELIFTFAFVI RQTTQPALSN SPNLDGQTAS TDTNISGLTF VYASTSKEVE
NLVTREFHAN PNLHKNDNVA LVGDYSTSGS AAVSFEWTWK WKAPSRQEDK GGGWRNSCSV
LCRVRFTRSP IAHSRCFFIL GFKYARPVKV AKSSCSYTTP TQPSSPSAPF LLASPPKIRI
ASAQSVDSRL AAADIDEQPL SPLLTPGEMN LPPVPQTKES AKVDVQCVPR PAEDVTVADD
GPVFRATLKA LEQKTGNMRA QMKKVLKRAE QVHTSQTEAN EAFVAFVDAL REASSTNANA
VQPALEHYFD KIAREILAYE RQNTANLQKI IIEPITKLYQ FDIKQAENKK RDFEEESKDY
YAYVSRYLGQ RQDSVKAKKL AESDSKYQNK RRNFELKRFD YSSFVQDLHG GRKDQEVLSH
LTKFADAQAG SFLSTAQKIE NLRPQLVALA NEVQEADKEY QYQRREREEK RRQLEQSNKT
YTEPEQASLG SAATIVANSN NSTAHTSDTE LGRAESTGSQ LKPSTSSGAV QTTATIPAPA
DIGQASAIGS PSQSSKFKGI RDLEDQSSLQ SNLSQRKEGL LWALNRPGGH VDPRNLNKQG
WHKFWIVLDQ GKLSEYSNWK QKLDLHMDPI DLRMASVREA RNAERRFCFE VITPNFKRVY
QATSEEDMNS WILSINNALQ SAVEGRAYRD RQATSRGSDS SLKRDIGSVL TGKIQSVHGS
HHSHHSNANS GVPFRRTTVG ARPSPVRMPS STYDEHPDRL LQMLRDNDQG NCYCADCGSD
IKVEWVSINL GIILCIECGG IHRSLGTHVS KIRSLTLDIK SFTLDIVEML LLVGNRVSNM
VWEAKLDQTQ KLGAQANRER RLRYITAKYV ERAFVDPISP TLSRYASADE TLLAAIKKNE
IQQVLYALAL GANPNVVDKM RGTHAVWLAL AAADPASPSP IPGQSSTDSE NKPVPFPVAE
LLIQNGAEIP ASLPAFPLGR YAQQYYEQKK GKGFTIGGND TVPSLPTSGS SSADRLLKDK
EVRLQKRVSA GGRLARSPIP EK
//
