ID A0A2U9CFK2_SCOMX Unreviewed; 744 AA.
AC A0A2U9CFK2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Putative ras guanyl-releasing protein 3 {ECO:0000313|EMBL:AWP14469.1};
GN ORFNames=SMAX5B_008734 {ECO:0000313|EMBL:AWP14469.1};
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:AWP14469.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP14469.1, 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.
CC -!- SIMILARITY: Belongs to the RASGRP family.
CC {ECO:0000256|ARBA:ARBA00009566}.
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DR EMBL; CP026257; AWP14469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CFK2; -.
DR STRING; 52904.ENSSMAP00000028429; -.
DR Proteomes; UP000246464; Chromosome 15.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF178; RAS GUANYL-RELEASING PROTEIN 3; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF48366; Ras GEF; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW ECO:0000256|PROSITE-ProRule:PRU00168};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 10..124
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50212"
FT DOMAIN 218..453
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 490..525
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 528..554
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 564..614
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 688..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 84465 MW; 9F180B94311ACE29 CRC64;
MKRKLCTMGS STLGKAASLD ALLNECIQAF DDNGELQANL LPRCLLLMHR WYVTSSELAG
KLLMIYPESR LKICYLMRYW IVTFPAEFNL DLGLIRITEE FRDVAGQLGC EEHFKLIDIS
TIPSFDWMRK LTQRKKQAKK GKASLLFDHL EPMELAEHLT FLEITEEFRD VAGQLGCEEH
FKLIDISTIP SFDWMRKLTQ RKKQAKKGKA SLLFDHLEPM ELAEHLTFLE FKSIRRISFT
DYQSYVIHSC LVENPTLERS IALFNGVSQW VQLMVLSKLT PQTRAEVITK YIHVAQKLLQ
LQNFNTLMAV VGGLSHSSIS RLKETHSYLA PEVVKIWSEM TELVSSSNNY SCYRKGFSEC
QGFKIPILGV HLKDLIAVHV VFPDWVDDGN KVKILNLVKM NQLYMTFNEL VSLQSAAAQV
EPNMDLIYLL TLSLDLYYTE DEIYELSLLR EPRNSKSLLA SPTTPNKPLA PLDWASGVTT
KPDPSIVNKH IRKVVESVFR NYDHDHDGYI SQEDFESIAA NFPFLDSFCV LDKDQDGLIS
KDEMIAYFLR ANPLLQCKMG PGFIHSFQEM TYLKPTFCEH CAGFLWGIIK QGYKCKDCGV
NCHKQCRELV VLACRKLIRS GSVGSASPAR LTHSSLPSSP AMPTCKDEDE VFEFPAVTSA
GPSLASQSIT LMTGSAQRIS VRLQRATTSQ ATQTDPLWPE HSWGAADGGS HTFPKMKYRT
HRKTSKNKGF ACWENQNGRQ HQDS
//
