ID A0A091P4N1_9PASS Unreviewed; 696 AA.
AC A0A091P4N1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 3 {ECO:0000313|EMBL:KFP86520.1};
DE Flags: Fragment;
GN ORFNames=N310_02300 {ECO:0000313|EMBL:KFP86520.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP86520.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP86520.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP86520.1};
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; KK844659; KFP86520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091P4N1; -.
DR Proteomes; UP000053537; 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:UP000053537};
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..106
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 31..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..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP86520.1"
FT NON_TER 696
FT /evidence="ECO:0000313|EMBL:KFP86520.1"
SQ SEQUENCE 696 AA; 77840 MW; 0AA3E0D5DE118886 CRC64;
CTAVTVSKEP SAELGNKDSI AELNGNGKIP NRDSGIDSPS CSVAGETFPS EEGAEQKKPS
VAGNPGEMEP DKKGTKPSSA EQKRDSTQDE DSDIDEGSSE EQETAELPKL EFLDVNKCTE
PQKLFNIANE LLHTEEAYVK RLHLLDQVFC TKLSEAGISS EVITGIFSNI SSIYCFHGQF
LLPELKTRIT QEWSVNPRLG DILQKLAPFL KMYGEYVKNF DRAMDMVNTC MQRSSPFKDV
VQNIQKQEVC GNLTLQHHML EPVQRIPRYE LLLKDYLKKL PEESPDRKDA EKSLELISTA
ANHSNAAIRK MEKMHKLLEV YERLGGEEDI VNPANELIKE GHIQKLSAKN GTAQDRYLFL
FNSMVLYCVP KLRLIGQKFS VREKMDIAGL QVQEIAKQNV AHTFSITGKK RSLELQARTE
EEKKEWIQVI QATIEKHKQN SETFRAFNSS FSQEEEHLPD SSIASTSSVE SMPGADGGGP
LGGSDSCRKS SKSKRDKEKQ ACKSCSENFN SITKRRHHCK QCGAVICAKC SEFKPLADNS
RHNRVCKECF LQLPASPCSP GAEAVGDQKK RLAAEKQSIL AAENSLFSSY LQFLEKGKTW
YKMWVTIPKT EPLVLYLQGS SQDARSPRPV PLPGYEVSLP GSGEKFEVKH VFKLCQSQQT
LYFSAEDEEL QMKWMEILTK AAKGETEDTA EGLSNP
//