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Database: UniProt
Entry: A0A2C9WF90_MANES
LinkDB: A0A2C9WF90_MANES
Original site: A0A2C9WF90_MANES 
ID   A0A2C9WF90_MANES        Unreviewed;      1104 AA.
AC   A0A2C9WF90;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MANES_02G140700 {ECO:0000313|EMBL:OAY57988.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY57988.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY57988.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY57988.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM004388; OAY57988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9WF90; -.
DR   STRING; 3983.A0A2C9WF90; -.
DR   EnsemblPlants; OAY57988; OAY57988; MANES_02G140700.
DR   Gramene; OAY57988; OAY57988; MANES_02G140700.
DR   OMA; HPRGIPM; -.
DR   OrthoDB; 551430at2759; -.
DR   Proteomes; UP000091857; Chromosome lg2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   CDD; cd13365; PH_PLC_plant-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013591; Brevis_radix_dom.
DR   InterPro; IPR027988; BRX_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
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; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR   PANTHER; PTHR22870:SF437; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR-RELATED; 1.
DR   Pfam; PF08381; BRX; 1.
DR   Pfam; PF16627; BRX_assoc; 1.
DR   Pfam; PF13713; BRX_N; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF16457; PH_12; 1.
DR   Pfam; PF00415; RCC1; 6.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS51514; BRX; 1.
DR   PROSITE; PS00626; RCC1_2; 3.
DR   PROSITE; PS50012; RCC1_3; 7.
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:UP000091857};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   REPEAT          267..328
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          329..380
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          381..435
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          436..487
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          500..551
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          552..603
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          604..655
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   DOMAIN          660..722
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1031..1086
FT                   /note="BRX"
FT                   /evidence="ECO:0000259|PROSITE:PS51514"
FT   REGION          135..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          865..941
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        143..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1022
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1104 AA;  119512 MW;  38365D96EEFDB36F CRC64;
     MSRTDRMASD LSRTGPVERD IEQAITALKK GAYLLKYGRR GKPKVCPFRL SNDESVLIWF
     SGKEEKHLRL SHVSRIISGQ RTPIFQRYPR PEKEYQSFSL IYNDRSLDLI CKDKDEAEVW
     FSGLKSLISR SHHRKWRTES RSDGVPSEAN SPRTYTRRSS PLNSPFGSND SLQKDRDHLR
     LHSPYESPPK NGLDKALSEV TLYAVPPKGF FPSDSASGSV HSLSSGGSDS VHGHMKAMAM
     DAFRVSLSSA VSSSSQGSGH DDGDALGDVF IWGEGTGDGV LGGGNHRVGS GFAGKMDSLL
     PKALESTVVL DVQNIACGGR HAALVTRQGE IFSWGEESGG RLGHGVDSDV LHPKLIDALS
     NINIELVACG EYHTCAVTLS GDLYTWGDGT YNFGLLGHGN EVSHWVPKRV NGPLEGIHVS
     SISCGPWHTA VVTSAGQLFT FGDGTFGVLG HGDRKSVSLP KEVESLKGLR TLQAACGVWH
     TAAVVEVMVG NSSSSNSSSG KLFTWGDGDK GRLGHGDKEA KLVPTCVAAL VEPNFCQVAC
     GHSLTVALTT SGHVYTMGSP VYGQLGNPHA DGKLPNRVEG KLSKSFVQEI ACGAYHVAVL
     TSKTEVYTWG KGANGRLGHG DTDDRNIPSL VEALRDKQVK NIACGTNFTA AICLHKWVSG
     VDQSMCSGCH LPFNFKRKRH NCYNCGLVFC HSCSIKKSLK ASMAPNPNKP YRVCDNCFNK
     LKKTIETDAS SQSSVSRRGG VNHGSNGFID KDEKLDSTSG AQLARFSSME SLKQAESRSK
     RNKKLEFNSS RVSPVPNGGS NWGALNISKS FNPVFGSSKK FFSASVPGSR IVSRATSPIS
     RRPSPPRSTT PTPTLGGLTS PKLVVDDARR TNESLSQEVI KLRAQVENLT RKAQLQEVEL
     ERTTKQLKEA IAIAGEETAK CKAAKEVIKS LTAQLKDMAE RLPVGAARNM KSPSFTSLAS
     TPSNDIPNVS LDCLNGQIAS EGPETNRLNS QLSNGSGVIG IRNSGYSKQG HFDANGRNGS
     RTKEGASQHE AEWVEQDEPG VYITLTSLPG GVKDLKRVRF SRKRFSEKQA EQWWAENRAR
     VYEQYNVRMV DKSSVGVGSD DLAH
//
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