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Database: UniProt
Entry: A0A2U9BIB9_SCOMX
LinkDB: A0A2U9BIB9_SCOMX
Original site: A0A2U9BIB9_SCOMX 
ID   A0A2U9BIB9_SCOMX        Unreviewed;       604 AA.
AC   A0A2U9BIB9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=RalA-binding protein 1 {ECO:0000313|EMBL:AWP03744.1};
GN   ORFNames=SMAX5B_006274 {ECO:0000313|EMBL:AWP03744.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP03744.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP03744.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP026249; AWP03744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BIB9; -.
DR   STRING; 52904.ENSSMAP00000021208; -.
DR   Proteomes; UP000246464; Chromosome 7.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd04381; RhoGap_RalBP1; 1.
DR   Gene3D; 1.20.58.90; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR039767; RALBP1.
DR   InterPro; IPR049041; RalBP1-like_Ral-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR12783; RALA BINDING PROTEIN 1 RALBP1; 1.
DR   PANTHER; PTHR12783:SF5; RALA-BINDING PROTEIN 1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF20924; RLIP76_Ral-bd; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT   DOMAIN          125..313
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  69285 MW;  ABC87A4AE8A30B40 CRC64;
     MVRERGRDGQ FQGTPREKRR AEGYAAFQED SSADEAESPS KMKRSKGIHV FKKPSFSKKK
     EKDFKVKEKE KGPKEDKAKD KKSKDLTAAD VVKQWKEKKK KKKPTTTEAE PVPVEVPTFR
     PIFGAPLTEA VKRTALYDGI QLPAIFRECV DYIENYGMKC EGIYRVSGMK SKVDELKAAY
     DREECPCLEE YDPHTVASLL KQYLRELPEN VLGRDLAQRF EDACGRQVEA EKMTEFQRLL
     SEVPPESRLL LSWLVTHMDH VIAREADTKM NIQNISIVLN PTVQIGNRVL YMFFTHVTEL
     FGNVVLKPAV RPLRWSNMAT MPALPETQEN VKEEIRRQEF LLNCLHRDLQ AGVKDLSKEE
     RLWEVQRILT ALKRKLREAK RQECETKIAQ EIASLSKEDV SKEEMTENEE EVINLLLAQE
     NEILTEQEEL ISLEQVLRRQ IATEKEEIER LRAEIADIQS RQQGRSETEE YSSDSESESE
     DEEELQMILE DLQKQNEELE NKNTHLNQAI HEEQEAILEL RVQLRLLHSQ KLQQEPAVQP
     PPAEQAPPAQ PSPEHRSEEQ TKRSVNAVVA AATAAADTAP LTEGKAAKDP LKPSPNKDKR
     DSSM
//
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