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Database: UniProt
Entry: A0A3Q1IDP8_ANATE
LinkDB: A0A3Q1IDP8_ANATE
Original site: A0A3Q1IDP8_ANATE 
ID   A0A3Q1IDP8_ANATE        Unreviewed;      1537 AA.
AC   A0A3Q1IDP8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=FYVE and coiled-coil domain autophagy adaptor 1b {ECO:0000313|Ensembl:ENSATEP00000002581.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000002581.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000002581.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   Ensembl; ENSATET00000002607.2; ENSATEP00000002581.2; ENSATEG00000001858.2.
DR   GeneTree; ENSGT00940000154044; -.
DR   InParanoid; A0A3Q1IDP8; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15726; FYVE_FYCO1; 1.
DR   CDD; cd17698; RUN_FYCO1; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047337; FYVE_FYCO1.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR004012; Run_dom.
DR   InterPro; IPR037213; Run_dom_sf.
DR   InterPro; IPR047336; RUN_FYCO1.
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; PTHR46753; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46753:SF2; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF140741; RUN domain-like; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          97..230
FT                   /note="RUN"
FT                   /evidence="ECO:0000259|PROSITE:PS50826"
FT   DOMAIN          1231..1289
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1396..1525
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   REGION          342..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          298..339
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          374..598
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          627..661
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          694..728
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          836..898
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          924..1056
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1086..1215
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1537 AA;  175627 MW;  24301461A90652AE CRC64;
     MTNSFGIFLQ SHAVIYFVTV CPRHFISWGH FLLVNKSAFF VFFLLPHSEF LHDITIFTTM
     ASASSVGDNQ LQRIIRDLHD AVLELSREHR DCGEPITDDS ANLHKFFYKL EYLLQFDQKE
     KTTFLGQRKD YWDYFCDCLI KIKGANDGIR FVKSIPELKT SLGKGRAFIR YSLVHQRLAD
     TLQQCLINQR VTSDWYYARS PFLKSHLTAD IINNLYELNQ IQFDVAPRGY DLDADWPAFA
     RRTIGTASPA FAWKPPSRCS SINSLVSNYT QSQAQEFIPA RDSQTHSLFG EVEACSIVEN
     LRIELDQSEL RQQELLKQVQ ELGEEAAELK GVVKDLQGQL EAQKSSGQTN GQSSQEATNQ
     ERLNDLQISR EAINSELQDR LTAAENKNME LLSKLDEALK EKGQQTTSYC DSAWKIQELL
     DKLKIMEEER LEAKREAEDR ARQSDRLTQE LKLREEELRS SEKKLAEVKA GADKEREETL
     KRLEDLQGAV GRIQGALSLK EKETGNLRAQ LQDLQASLEC RERQAEELRK RLQEEREEVE
     QRWSTSSSQN EELECLIMDL RKTIRNREKE LAASSERIKH LEEQLEKLNV EKESLSSRLI
     DNEFTSCDQT KNFEDYKIQC SNLTEINTKL LQTVKNSEES ITELNESRTA LLEQLASLRA
     SEKTLKGRVE AANMVVEDRE KKLLDENLHL EEIIQKALVQ KEISDAQLKK LEHENKELLE
     GQSLLKKQLA TTQQELDCVT AKTAKLDKSL TMSQRSQTEL LEKLQETEAK LRDQTVQCGL
     LQARAEELES STRELHDEKG TAESNEKVQK LDDENHTVSM ETKEAPIRVV IAEAQLELNL
     REVTRLREEV VELRAQLLAG TEERMKVQAL QEVTEASRED LRLLTEQLKA QVEELNRGHV
     DEILRSRERE EALVHERDDE AQARASLAAE VTSSREELAK LKLQYDALSL ENSESSEALH
     RANTETAELG VHVCMLTAEN EEARLRYEGL SAKLQKLEED AAQEAERLNN CVEQLRQENR
     QLLDQLHNEK GLLVTEQELQ KELRKAQQKA DTVQETTQVE IQALRLQNSS EAMNHHSQLQ
     SVNQELHEVR LRLTTKQETV VNLENKLGQL EAENQRYCQQ IEEKNIQMAE SENLIRQKDD
     EIIHLKENLS RSEESLAAAQ QASQEMSENL RRVTQDKQSL DFKTAAELDD LYRTKKNLEE
     RLVELIREKD ALWQKTNALE FEQKLRDEEM EKDVNYCMDC HSQFSWLLRK HNCRLCGRPF
     CYYCCSNTVS TQQGGNREHC CRDCYNQHSA VVERHPQEVL SNSTPGSPFR RLLSKKAGRA
     AAPVSGSDEV DKLDDGVFDI ITDDEVSGVY DSDSFATACS PGHGQQGAAQ LNSSASVGDL
     ASEETEDVSA TVQDAEICLL KSGEVTHSVP FTVDDLSGFG DSSRELFIKS SCYSIIPITM
     RNPGPTVAWT FTSEPKSIAF SVVYRESAET PLEQAKVLIP LTRCNSHKET MQGELKVRNP
     GEYTLIFDNS FSRFISKKVL YRLSLDKSVI YDGTDLL
//
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