ID A0A3Q2ZFR5_KRYMA Unreviewed; 1160 AA.
AC A0A3Q2ZFR5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Guanine nucleotide exchange factor DBS-like {ECO:0000313|Ensembl:ENSKMAP00000002433.1};
GN Name=MCF2L {ECO:0000313|Ensembl:ENSKMAP00000002433.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000002433.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000002433.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q2ZFR5; -.
DR Ensembl; ENSKMAT00000002484.1; ENSKMAP00000002433.1; ENSKMAG00000001883.1.
DR GeneTree; ENSGT00940000157874; -.
DR OMA; LQRICTI; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01227; PH_Dbs; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11857; SH3_DBS; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035534; DBS_PH.
DR InterPro; IPR035532; DBS_SH3.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22826:SF115; GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 22..194
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 591..771
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 783..905
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1062..1123
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 546..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 131529 MW; 1BAB6BB1D4988516 CRC64;
MILWMKTEVM ALGELMERLR SVTKTIDEIM QLDTNPPRAA DIKADLRKQF AFLSGGRGDN
GSPIIVFPEF PAFGEITDRE FHNVLTYLTS VPSLSSADVG FILVIDRRQD RWAAVKGTLL
RIAGSFPGNL QLVLVLRPTT LLQRTISDIL FKFNKDEFKM KVPVIMLNSI TELHSYIDRT
QLTQELGGTQ LYCHEKWITH RTAIEGFALM VKKTAQTLQS FGTELAETEL PNEIQATNIL
LSTHTSKRDK MKEDILVALD QGSRLLESIN EPVMRDPDHN MNQDELENLA TVQRLLSQLD
ETERAFDEFW VRHQTKLHQC LKLRYFEHNY REVRALLDQV SEKLGTFSEV GISPAHADHI
FCELTAFEER VCEVLDRASA LCHEGEELIQ NSHYAEDSIR PKCSELTEIG ENVSCSLKAK
KEYLLKAMEL HHRLEKASKW VDDGIYLLAS QPVDKCQSHE GAELALQELE RYLDNAGQNQ
LSDLSTIWTE YEAVLNQQFR EQVERVYQKQ ASMQEMFDKR MVSLKKLAAK QMRPVQPVAP
RPEAFIKSPL SSPAHKAQQE KNGFSNSCEK NEDGNSRHAS LSEEEENLAV LRRHVMNELL
ETERAYVEEL LCVLQGYASE MDNPAMSHLI PANLQNKKEV LFGNMPEIYH FHKRTFLREL
EQYTDCPELV GRCFLERMTD LQIYEKYCHN KPRSESLWRQ CSDCAFFQEC QKKLEHKLGL
DSYLLKPVQR ITKYQLLLKE MLKYSKGCDG ADDLQEALTS ILGILKAVND SMHLIAITGY
EGNMSELGKL LMQGSFSVWT EHKKGHAKVK DLARFKPMQR HLFLHEKALL FCKRREENGE
GYEKAPSYSF KQSLSMEAVG FTENAKGDNK KFEIWCNSRE EVYIVQAPTA EVKTTWVNEI
RKVLTTQLEA CREASQQRAP DQGSPFPPVP SGTVSLSPFK TSQKSFKRGE EKKGEPLSSD
VNSSSSPKLP EKDEAVTSPT SDRAAVAKKR FTLQGFSNLK AQKGSPTSPD HKSKRQSDPT
PFGFKGWNKT SVSLDASEEH EDYSSAEDPL NSDPEDENIK KLCAGKYTVM ADHEMGGDQE
LSVKSGDTVQ LVKEGEDGQW FVHNLNTSHE GWIPAANLIT LIEKSKSCQS LTSSEGSGSG
NLSTSSSCSE TYTNFSDIKP
//
