ID A0A091RMS0_9GRUI Unreviewed; 696 AA.
AC A0A091RMS0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 3 {ECO:0000313|EMBL:KFQ40587.1};
DE Flags: Fragment;
GN ORFNames=N332_04036 {ECO:0000313|EMBL:KFQ40587.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ40587.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ40587.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ40587.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KK822336; KFQ40587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RMS0; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15740; FYVE_FGD3; 1.
DR CDD; cd13387; PH1_FGD3; 1.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 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); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035941; FGD1-4_PH2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF14; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 123..307
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 336..435
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 496..554
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 584..683
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ40587.1"
FT NON_TER 696
FT /evidence="ECO:0000313|EMBL:KFQ40587.1"
SQ SEQUENCE 696 AA; 78002 MW; F7BBDC8BF3A02931 CRC64;
CTAVTVSKEP SAELGNKDST AELNSNGKIP NRDSGIDSPS CSLAGETFPS EDGAEQKKPS
VAGNPGEMEP DKKGTKASSA EQKRDSTQDE DSDIDEGSSE EQETAEVPKL EYLDVNKCTE
PQKLFNIANE LLHTEEAYVK RLHLLDQVFC TKLSEAGISS EVITGIFSNI SSIYCFHGQF
LLPELKTRIT QEWNVNPRLG DILQKLAPFL KMYGEYVKNF DRAMDMVNTC MQRSSPFKDV
VQNIQKQEVC GNLTLQHHML EPVQRIPRYE LLLKDYLKKL PEESPDRKDA EKSLELISTA
ANHSNAAIRK MEKMHKLLEV YERLGGEEDI VNPANELIKE GHIQKLSAKN GTAQDRYLFL
FNSMVLYCVP KLRLIGQKFS VREKMDIAGL QVQEIAKQNV AHTFSITGKK RSLELQARTE
EEKREWIQVI QATIEKHKQN SETFRAFNSS FSQEEEHLPD SSIASTSSVE SMPGTDGGGA
FGGSDSCRKS SKSKRDKEKQ TCKSCSESFN SITKRRHHCK QCGAVICAKC SEFKPLADNS
RHNRVCKECF LQFPASPCSP GVETVGEQKK RLAAEKQSIL AAENSLFSSY LQFLEKGKTW
YKMWVTIPKT EPLVLYLQGS SQDGRSPRPI PLPGYEVTLP GSGEKFEVKH VFKLCQSQQT
LYFSAEDEEL QLKWMEILTK AAKGETEDTA EGLGNP
//