ID A0A232EF78_9HYME Unreviewed; 595 AA.
AC A0A232EF78;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_006357 {ECO:0000313|EMBL:OXU17019.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU17019.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU17019.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU17019.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU17019.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Early
CC endosome {ECO:0000256|ARBA:ARBA00004412}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}.
CC -!- SIMILARITY: Belongs to the rabaptin family.
CC {ECO:0000256|ARBA:ARBA00006603}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXU17019.1}.
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DR EMBL; NNAY01005088; OXU17019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EF78; -.
DR STRING; 543379.A0A232EF78; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd15739; FYVE_RABE_unchar; 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003914; Rabaptin.
DR InterPro; IPR018514; Rabaptin_coiled-coil.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR31179:SF7; FYVE-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31179; RAB GTPASE-BINDING EFFECTOR PROTEIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF09311; Rab5-bind; 2.
DR Pfam; PF03528; Rabaptin; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 523..583
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 529..579
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 410..493
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 69179 MW; 84F74CE99E3A0D95 CRC64;
MDSTESGAQP DQDTKEEAEN APDATEDVHE KVKRLEAMNN QMREEFDVQR AKMKELFLQK
EEDAKKQMEE NSKLQEENSK LQHELNEVKS QLVIVDIKTQ NDIDLEKRKA EDEIASLQQI
ITSTVQDSST TRKEYESRIS KLKEENNNLR LQLMQSSSLD GPQISLSTMT KSLAKKVASQ
LGADSLSLGS ENEDSSSKSK RHADEDAEVL RSLVVPLEEE ITALKEKLRT TDDELQKYKE
KEEQIHNKQL RAKESGSWEN TCDMCSNYEA QLQRMQMEAK DLKKQLQETE QMLQSQKQDL
AKEVEFRKGM EEKWNEKKEE HKAEVTNLTS SVKLAKQTID ELKQQYNQTK ESITKELSRL
TKEREEVQKH LEQLQNQNEY LMGKHSKHSE HYQYEHINMP NNVEELHVSI LQIREELIVA
TIAKEEAERK CRSLECELEL LHDQIEQDNH EKEKKEAELQ SMIESASKTD LVVAELKQQI
TNLQQELNTG EQTQKDFVRL TQSLQVQLQK IRDSEKEVRW QYEDDVDECP TCHTTFTLAK
KKDKMHCRHC GQIFCQSCLN NVVKSGPKQR PSRVCNVCHT LLVQETAPYF SRDPP
//
