ID A0A182RQD1_ANOFN Unreviewed; 1799 AA.
AC A0A182RQD1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 13-SEP-2023, entry version 31.
DE SubName: Full=FYVE-type domain-containing protein {ECO:0000313|EnsemblMetazoa:AFUN008473-PA};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN008473-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN008473-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN008473-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR STRING; 62324.A0A182RQD1; -.
DR EnsemblMetazoa; AFUN008473-RA; AFUN008473-PA; AFUN008473.
DR VEuPathDB; VectorBase:AFUN008473; -.
DR VEuPathDB; VectorBase:AFUN2_000894; -.
DR OrthoDB; 2945465at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028730; ZFYVE26.
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; PTHR46591; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 1.
DR PANTHER; PTHR46591:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1000..1060
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 59..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1799 AA; 202329 MW; FFFD9D74152301E2 CRC64;
MRSYASAYRY ATGTDNADTH FRNYCESSSS GSAKLFRSVE SIAAMDVANG QRHRYGYYGT
LPKHKSSRRQ TRHPLTATAV SSNSGGSNKD LQRQGSLSVD TKTESIAYGR TAADGELAGG
STRSILWHKT NFTKLFATPE TLAVVCLTNS RMSFAKQIIE THNLQDQPVG KLVERIEQMQ
TLKNDLAMLI KKNEQKQEMA LGFGGTQSSD SNSDVLLDDI RHKTAMGFEI SIVLSTLETI
LKSQPIGTED VLAPMDRFVS RYPFLGILTG KNLQLSQIVD IIVNLPFNYE LNLAIYNFLL
KNSHHMTHMA SSMMSSSIAG HGGETSQWIG NYVSFFGTIM DTLQISHKTA RARLSSADFK
LTINELLSRE VCPLDTVENG IVLKRRARFY RMIERCDELE DADNLNRTFA LLTESGSASL
TKVKLYMEHL TKLLESLLST TRQDTESDNL NLTEVNRLIQ TDVQKLMLER LAEKRISFAA
LDTLGSMLGI NLVQTIGKRI LEPKDEPAEM MFHTIDGLWE FIASKSELLC QLCKVEADCL
TPVNSSQSLI VNYSELIRAV GDLNYLPNGC SCIRTSSSVV SQTKLFPLDA YRPCCMLQQK
KGKYYTKVES VMLAANASME QKALALLANV DEFAVANEWI SASEHLLAAI PKNLEPQEQS
GIMPATRQQL QQKANELRTY LQIGTILQLS TNDNDTTQAD GDGWRKAQKF STENKSTVLH
QLIEQGEYRV CAEWIKLHPI DAEAELEMFI YAVHKVSTAS TLVMIPTDPQ DSDVPIVWLF
RIIETMPIEA VVKLYETIML NIRSVAVVRY MLEYLQRYTT TKPLYQKYQL SLKIFEHLAR
EEYDGLWNLA SRPLLIIEQC LMNSRLELLA AVMRSIRGLL VTDVCARCYE HREYIRDLHD
AVQGGPEEQP HTAGVRRYPV HDGLFISHEC VDCLLRVYAG KALEYKVFPD AISSSGAYTE
DPAHTLGPVS RVSSYDSLSE VDQPFVMPKE IPTRDRWVKD EEALHCMCCR RTFSMLNRRH
HCRRCGRVVC HSCSKKKLRL QSFYEDVAVR VCDDCWQNLA GTQAKDAQLE MGTAVPSGTQ
SRTSDQSGSQ FEWQLTGNER YDNVIRDEYS YEYAPSTNQC LAISNLHTAN EEMASFLLYH
CAKLEALLRP LHPGVPNPEI DYALVARMLL NLTLGVKVRG GGAEVEKMKE HAEIILSIVH
DNCESLLLHT PSMTNHGSLR KLRDALVKAE KWTLALELSL KCGFSLNGVM AAWGMACLRA
GCYDTAREKF SHCLPRVATE AECEAVLRMI EMPPVMIYAS ATKVPIVKRP TRCPPLLNEI
LYALTYTARL GAPSERVTAR VNAARQATVG SIGGSHEPAL NILSTLANLR HICQGEYDGD
IPGPNAERLA RNDSASLMCS RLFEEAMHYL LAYGSHQSVV QFLMRYQQTE VASLRYILAQ
RVDPDVFLHA ILLPYLQRGE LETVVQRLSD IDDTLLEWRE HIRYACRYLE TNDMLNSLYS
LQLLLKDPIR ASMTCVRFYT MGCRTFTDLH ASEHHLKTSV SHLQNELELC NWQEVRLNST
IDTHHSLLMK LDPKELNNHI NTILLQLDVT KFLATCEAKG RQTVTLLPKI FREASQLPTL
FGSSHDKLQL AILTLVCGQN VEEAFGLSYR IIQDYNLDMQ RVYALTAKYF INHSKIEDVG
KLLDVIVDNE GSTGATEPTV TVICDEIVRV SVDVAITRHG TGVHTKVALE ALINRASSVA
VRIHCYIVSG QLKAAYLLAN RHQRTGDIRK ILRQAELLGQ MHVKRLCEAR LNHPENSAS
//
