ID M7BGG6_CHEMY Unreviewed; 1755 AA.
AC M7BGG6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Zinc finger FYVE domain-containing protein 16 {ECO:0000313|EMBL:EMP36299.1};
GN ORFNames=UY3_06514 {ECO:0000313|EMBL:EMP36299.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36299.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SIMILARITY: Belongs to the FAM151 family.
CC {ECO:0000256|ARBA:ARBA00005758}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB525692; EMP36299.1; -; Genomic_DNA.
DR STRING; 8469.M7BGG6; -.
DR eggNOG; KOG3748; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15729; FYVE_endofin; 1.
DR Gene3D; 3.30.500.40; -; 1.
DR Gene3D; 3.30.1360.220; Domain of unknown function (DUF3480), N-terminal subdomain; 1.
DR Gene3D; 4.10.720.10; Smad anchor for receptor activation, Smad-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019356; Memorin.
DR InterPro; IPR022557; SARA-like_C.
DR InterPro; IPR024608; SARA-like_SBD.
DR InterPro; IPR037145; SARA_Smad-bd_sf.
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; PTHR46319; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46319:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 16; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF10223; Menorin; 2.
DR Pfam; PF11409; SARA; 1.
DR Pfam; PF11979; SARA_C; 2.
DR SMART; SM01421; DUF3480; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM01422; SARA; 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:UP000031443};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 746..804
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 292..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1755 AA; 192171 MW; 85BC4820B7A94ACC CRC64;
MDNYFKAAVC DLDKLLDEFE QNTDELDCYR TAANQCDSIQ HSVSSELDCL QPVFLIPKVQ
EYVSSCSMSE EFSLASQAIT NTAKFELNSS AQNEKNVTGL DLLSTVDGGA SNEIQPLSLG
RCSIPVCDLI SDTGNLIHST SNHEDIEKLQ PDDFQCNENS LVGFDLSLVP ATVCSLSVAF
SGVSGTEQQN GGDTTPQDAG HVATKELSQL DFKTHNRGKA KLSDSCDGQN RTETLKDIQI
FDQLEQITGL NATSAFVTSQ SPKALSSKDD TTIEKLPCES LKDESQCCMI SQEAPEESVN
DSVDSKDDGN GESLPSDLPK SSELHKNSLK LSGKCVIPDS SSQIEDRVVL DKMKSAEENM
CSPELNTNEI LHSVSNSHVT AEDIQTSLSC LPLAVSICGS LVVTEDKSDH IPQNEKADVI
SDTVTMHAGK SKHGFPSMES SGKMKPSEQE GYLNQINQCF VEEAITIDGK KRESDNKINK
GDSPQMHAAA AGPVGEAKIE LCSDGIQPVD SHDQSITCPV LADLTIEEYL IESDSLISDA
ELDAFLSGQS LQPNNSQPFE EGMDDLLEPD ANQANNLDFR KVNDSQTKAK LEEIGEISSI
NSTCRIADIE YKLESPPEKS TYPIQQEASN HITETRIEVP VPTLSHQNVH IGGARPKQLL
NLSQRTVIER EFSKPDMPRT EFQEVNSLPP KASLSETKTS TDISSKCNPS DTENSLEAGG
SCVPASVELG KEPLVLGLKQ PPWVPDSEAP NCMNCQVKFT FTKRRHHCRA CGKVFCGVCC
NRKCKLQYTE KEARVCIGCY KSINKAQAFE RMMSPTGTIP NSSVSSEYCS TVPPLQEAQT
VGTPNSPSSS LLLPISVLKQ PGADGLCARE QRRVWFADGI LPNGEVADTT KLSSGVKKSS
QELSPASPVA SPADDICVTD TKPKDEIAVS AGTEKFHCSL HVAPDDDQLP TAVQTEMLHS
LDSLIPAADE LPFITKVEKS PSLGTVNQTN DDSLVSPSDY RMLCGIENCV SKEFSLIPDD
DGLPPLLLAT GEKGKGKYIG NLENFTFTES FLGSKDHGGF LFVAPTFQKL DDLLLPNNPF
LCGILIQKLE IPWAKVFPIR LMLGLGAEYG AYPTPVTSIR HRKPLFGEIG HTIMNLLVVM
KVIHSSNEHV ISIGASFSTE ADSHLVCVQS DGVYQTQANS ATGHPRRITG ASFVVFNGAL
KTSSGFLAKS SIVEDGLMVQ ITPETMEGLR QALRDKKDFK ITCGKMDAEE LKEYVDICWV
ESEEKVNQGV VSPVDGKSME GIQSERILQG DFDTEEKLMK CTEVFYILKD HELSSATPHQ
FAKEIAVACS AALCPHLKTL KNNGMNKIGL RISTDTDMEQ PLFRGESRIL APRGPGRIES
RPQEAGLSRQ DPRPPPPAME RELVAMVRTY LKLFFMYAVL TLNIIDIGAW SENVLDYFLN
TNQIKTRDGA EIIWYHAANN RSQMKEAIQS AAHMVEADIL LCGEEEGNGE PIMAHPPETN
SDNTLQTWLN EIVNTKKGIK LDFKSQGQSY ISRSASMVSV SFGTPPTPST PEILTVTQLT
CIPDEAVAST STAPALEDSR VLQQLLSLAA VKPSMKLLEG IKLHLRRPVW INADILPGPN
GSNTVVDAKR FLDTVTSFCP DVTLSLSWTT GWQPQQCNKG YSWAMVKEMA QICDALTQPV
TFPVRAALVR QSKSELLWLL QKSNRYSLTV WTGMHDEYSI EDLLYLRENF DKSRVYYDIL
EPQNSEFRKA IGIEV
//
