ID B3S384_TRIAD Unreviewed; 527 AA.
AC B3S384;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN ORFNames=TRIADDRAFT_58631 {ECO:0000313|EMBL:EDV22745.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV22745.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV22745.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV22745.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the lst-2 family.
CC {ECO:0000256|ARBA:ARBA00008755}.
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DR EMBL; DS985248; EDV22745.1; -; Genomic_DNA.
DR RefSeq; XP_002114611.1; XM_002114575.1.
DR AlphaFoldDB; B3S384; -.
DR EnsemblMetazoa; TriadT58631; TriadP58631; TriadG58631.
DR GeneID; 6756004; -.
DR KEGG; tad:TRIADDRAFT_58631; -.
DR CTD; 6756004; -.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_007360_1_1_1; -.
DR InParanoid; B3S384; -.
DR OMA; PELGYDR; -.
DR OrthoDB; 5394048at2759; -.
DR PhylomeDB; B3S384; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15731; FYVE_LST2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR043269; FYVE_LST2.
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; PTHR46465; LATERAL SIGNALING TARGET PROTEIN 2 HOMOLOG; 1.
DR PANTHER; PTHR46465:SF2; LATERAL SIGNALING TARGET PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 468..527
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 399..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 59739 MW; F36119A314E26368 CRC64;
MAGTGTEDYI IAQYLFGRRC KRCHCVKLKN NHVKSQAVDS AAKVDNITAV GIVPKTLVCI
SNKNDTRPLA QFYHANESLN KIIRELGSFD GKQDVQRCAT LVNKLREQHQ LVYQKMTAVM
EEAIPMNLRH PRHYRLKFPE DFLTDNLGGM IWFGIEGISA GSAVLNHEEE SQEMKPLAAE
LHKQLNTVRD RLKNQSLRNI NIYPKKVINE LIELDRLWSE FELRALKSDL ITSAELECFD
PTVFFAVPRL AILYCISGCH EEEFENDFNS DMTIPLMFNS FREELQEIKL LLREVGDEDL
SKLEIDLSNQ NNKVVKTAAK EASVNNDSIG MASQAPVSNS DGDDIKYTAL KVVQVQGNSD
ILHELFVKIS SIADRLHHIH AEDIRSALQK SIKVNLLSKP SHSDGDMNQS VAEEKNELST
PLEVLTTNEN SSSSNDGDKM HRTVNEVQHE RPQELQNDLI QPPSWVPDSR CDACTFCEAT
FTVLRRKHHC RNCGKIFCKN CVSASKKIPR LGFNRPVKVC QECFNNE
//
