ID A0A3Q2ZI80_KRYMA Unreviewed; 1163 AA.
AC A0A3Q2ZI80;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Guanine nucleotide exchange factor DBS-like {ECO:0000313|Ensembl:ENSKMAP00000002465.1};
GN Name=MCF2L {ECO:0000313|Ensembl:ENSKMAP00000002465.1};
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:ENSKMAP00000002465.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000002465.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q2ZI80; -.
DR Ensembl; ENSKMAT00000002516.1; ENSKMAP00000002465.1; ENSKMAG00000001883.1.
DR GeneTree; ENSGT00940000157874; -.
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 23..197
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 594..774
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 786..908
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1065..1126
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 549..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 131789 MW; 730062CAF077822E CRC64;
MYSKKIMVKK PKKCASELDK GIPMVTLKPY EIMQLDTNPP RAADIKADLR KQFAFLSGGR
GDNGSPIIVF PEFPAFGEIT DREFHNVLTY LTSVPSLSSA DVGFILVIDR RQDRWAAVKG
TLLRIAGSFP GNLQLVLVLR PTTLLQRTIS DILFKFNKDE FKMKVPVIML NSITELHSYI
DRTQLTQELG GTQLYCHEKW ITHRTAIEGF ALMVKKTAQT LQSFGTELAE TELPNEIQAT
NILLSTHTSK RDKMKEDILV ALDQGSRLLE SINEPVMRDP DHNMNQDELE NLATVQRLLS
QLDETERAFD EFWVRHQTKL HQCLKLRYFE HNYREVRALL DQVSEKLGTF SEVGISPAHA
DHIFCELTAF EERVCEVLDR ASALCHEGEE LIQNSHYAED SIRPKCSELT EIGENVSCSL
KAKKEYLLKA MELHHRLEKA SKWVDDGIYL LASQPVDKCQ SHEGAELALQ ELERYLDNAG
QNQLSDLSTI WTEYEAVLNQ QFREQVERVY QKQASMQEMF DKRMVSLKKL AAKQMRPVQP
VAPRPEAFIK SPLSSPAHKA QQEKNGFSNS CEKNEDGNSR HASLSEEEEN LAVLRRHVMN
ELLETERAYV EELLCVLQGY ASEMDNPAMS HLIPANLQNK KEVLFGNMPE IYHFHKRTFL
RELEQYTDCP ELVGRCFLER MTDLQIYEKY CHNKPRSESL WRQCSDCAFF QECQKKLEHK
LGLDSYLLKP VQRITKYQLL LKEMLKYSKG CDGADDLQEA LTSILGILKA VNDSMHLIAI
TGYEGNMSEL GKLLMQGSFS VWTEHKKGHA KVKDLARFKP MQRHLFLHEK ALLFCKRREE
NGEGYEKAPS YSFKQSLSME AVGFTENAKG DNKKFEIWCN SREEVYIVQA PTAEVKTTWV
NEIRKVLTTQ LEACREASQQ RAPDQGSPFP PVPSGTVSLS PFKTSQKSFK RGEEKKGEPL
SSDVNSSSSP KLPEKDEAVT SPTSDRAAVA KKRFTLQGFS NLKAQKGSPT SPDHKSKRQS
DPTPFGFKGW NKTSVSLDAS EEHEDYSSAE DPLNSDPEDE NIKKLCAGKY TVMADHEMGG
DQELSVKSGD TVQLVKEGED GQWFVHNLNT SHEGWIPAAN LITLIEKSKS CQSLTSSEGS
GSGNLSTSSS CSETYTNFSD IKP
//
