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Database: UniProt
Entry: A0A3Q1JL20_ANATE
LinkDB: A0A3Q1JL20_ANATE
Original site: A0A3Q1JL20_ANATE 
ID   A0A3Q1JL20_ANATE        Unreviewed;       839 AA.
AC   A0A3Q1JL20;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSATEP00000035857.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000035857.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000035857.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC       {ECO:0000256|ARBA:ARBA00005430}.
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DR   AlphaFoldDB; A0A3Q1JL20; -.
DR   STRING; 64144.ENSATEP00000035857; -.
DR   Ensembl; ENSATET00000036371.2; ENSATEP00000035857.1; ENSATEG00000024642.2.
DR   GeneTree; ENSGT00940000158956; -.
DR   OMA; PLGHQLW; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08854; ArfGap_AGAP1; 1.
DR   CDD; cd04103; Centaurin_gamma; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45819:SF3; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          334..561
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          582..702
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          749..781
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          240..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  90827 MW;  14B19131A35F6D8D CRC64;
     MNNNSKSVNS TAIKAEIKRH ESLQSAINRL FKQFERVQDQ QLRSGLKVFL TSIQVNIANS
     QEWTLNRSVP ELRLGILGSL KSGKSALVNK YITGSYSALE KPDGGRYKKE VLVDGQSYLL
     LIREEPGPPD AQFSSWVDAV ILVFSLENEA SFQELYQLYS QLSAFRTDIP VIVVGTQDKI
     SSTNPRVIED QRARQLCLDV RHSLFYETCA TYGFNVDRVF SEAAQKIVAQ KKQAALQACK
     SLPNSPSHSG GSTPGSASLP GQASNGPSSG YAYSLPSTPV VGHRELRVAQ GEGGGSINAR
     SLKSIPRRPS LFKNRDPDKK ASDAKGDLSS VRGVPIKQSI LWKRSGSSLN KEWKKKFVTL
     SNNGTLSYHS SSSDYTQNIH GKEIDLLRVT VKVPGKRPPR AVAPVGPSPV PPGSVPGVNG
     LNKDLTAADG TSTASVPQLC PATLSVVDDR AGALSPQGGE RGLQRCPSSL STKAQSVDAL
     EATASLFGGK DQGQSSPMSD RKKNRRKKSM NQKGDAAVGQ AEDEENADFI IVSFTGQTWH
     FEAQSLEERD SWVSAIESQI LASLQSCESG RNKARRSSQS EAVALQAIRN AKGNSLCVDC
     EAPNPTWASL NLGALICIEC SGIHRNLGTH LSRVRSLDLD DWPGELTQVL AAIGNHLANS
     IWESCTQGRT KPAPNATREE RESWIRAKYE QRAFVAPLQP ALGTQMPEDS MPEWLVSAVT
     EKDLPRLLLL LAHSTKEQIN SQPAGSSSLP QTALHAACQQ GDVVMTQLLV WYGIDVRGKD
     NQGQTAIMIA RKTGSKGCID ILLQHGCPNE TSPTTATPIL SRRSSTASLG RTSSRKRVT
//
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