ID   A0A3Q1I5J6_9TELE        Unreviewed;       725 AA.
AC   A0A3Q1I5J6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=RAP1 GTPase activating protein 2 {ECO:0000313|Ensembl:ENSAPOP00000034905.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000034905.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000034905.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1I5J6; -.
DR   Ensembl; ENSAPOT00000031119.1; ENSAPOP00000034905.1; ENSAPOG00000024516.1.
DR   GeneTree; ENSGT00940000165230; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 6.10.140.210; -; 1.
DR   Gene3D; 3.40.50.11210; Rap/Ran-GAP; 1.
DR   InterPro; IPR035974; Rap/Ran-GAP_sf.
DR   InterPro; IPR000331; Rap/Ran_GAP_dom.
DR   PANTHER; PTHR15711; RAP GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR15711:SF17; RAP1 GTPASE-ACTIVATING PROTEIN 2; 1.
DR   Pfam; PF21022; Rap-GAP_dimer; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SUPFAM; SSF111347; Rap/Ran-GAP; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          251..467
FT                   /note="Rap-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50085"
FT   REGION          30..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  79783 MW;  166103FD37B53F93 CRC64;
     MSQTGGRFHN KKAGIRAAVI LIGLLHKSRK AKEKEREKEE SEGKQELLNI SNVPLGECPP
     SPPRTAPPSM KVPKAEETKK WKDDYIPYPR IEDVLEKGGP YPQVILPQFG GYWIEDVEAP
     AGTPSSSESS FCEEEDGGEG MSPGGGHSYR LECNSTARAY RKHFLGKEHM NYYCTGSSIG
     NLIMSLKHEE AEGQEFLRIM LRSRTKTVHD RISLAGINQL PSVPQIAKLL CDDATGLKFN
     PVLYPRGSQL IVAYDEHEVN NTFKFGVIYQ KFGQTSEEEL FGNNEETPAF KEFLSILGDN
     IELQDFKGFR GGLDVSHGQT GFESVYTIFR QREIMFHVST KLPFTEGDVQ QLQRKRHIGN
     DIVAAVFQEE ATPFVPDMIA SNFLHAYVLV QAENPCTEHT TYKVSVTARE DVPSFGPPLP
     NPAVFKKGPE FRDFLLTKLI NAENACYKSD KFAKLEGRTR AALLDNLHDE LHRQSQATLG
     LGQVGEEDKL ENGAHGGLLE SFKRAMRVRS HSMETMVGSH RHRSPGVGGG VPASLSGGGL
     PQSTSECTKS TFTPPALSAK SPLKSPVKRR SGLFPRLHSS TESPSDKHTR SDQKHAEICP
     LSHEVKSETS SNPSSPEICP NKERPFIKLK ECSSGRPNIS RSSSSTSSFS STTGETEALE
     ELETASHPSM ASSSAFSPAL SVDSQGSGTP VIMCRSPTDG KNKTSPRSNL KFRFDKMSHS
     STTSE
//