ID A0A024GF92_9STRA Unreviewed; 1229 AA.
AC A0A024GF92;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN9_064410 {ECO:0000313|EMBL:CCI45544.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI45544.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI45544.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI45544.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI45544.1}.
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DR EMBL; CAIX01000100; CCI45544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GF92; -.
DR STRING; 65357.A0A024GF92; -.
DR InParanoid; A0A024GF92; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 4.
DR SMART; SM00325; RhoGEF; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237};
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 DOMAIN 67..255
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 284..393
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 416..489
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 502..607
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 636..899
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 924..1023
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1050..1150
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 139571 MW; 83BD1E3EC404FD27 CRC64;
MWSISSPSAA SPRDTKWSSE NKTNSNISDN QHTHDLDQTQ HNEPASITSD SRRSNQDPET
NQLANRIRDQ AIQELYDTEA SYIRDLCMLH EYYILPLSEN RHPIMQNPQI AVLFNHTLQL
ITLHQKLHSD LHEVISSTCN SVPVEGIGAV FCRYVGLFTF HGAYAKDYEH ALHLFQSYRN
DPKLGFSDFL KSCRERMKSS QELESLLIKP IQRVPRYKLL LERIAKHTNA HHADHAYLQE
AVNRVTQAAM QMNATVAAQA NLEAIYATQQ RFKGHISLIQ PNRRLIKSGY LIKVSTRRKE
SVFLHLFNDL LLYSDPLLTG DFRIRRIVDL NSKAAGVIAT VPGSHQALLY SKTKSLTPNC
GFVVTSLSKS FLLFAPNIAQ RSEWVECIQY AIREAQRQAH GGAEGPNDAA ALWVPDRVAG
SCTVCHAPFR LYFRRHHCRR CGVVVCGNCS RRKSILFVTQ PTITPLQDPM NNPIPRKERV
CSRCFIVLDL VRRIAFQWYE KIVRFRGVLT RYKAQKWTSY SIEIAADTLK QYALTTLLIS
NERQFLDSMS LRGAIARHSR HAEVRRAYCF TVVPLKTEEL PQNAWILGSH SIDETREWMH
ALENAILKAS QRFELAPLSS KSLENGRLSQ ENSELQRLRV VRKIIRSEEC YVTSLNECIR
LFIQPLLLRR MEGQNVLQKR QKARNRLGTN VATTSHDAEH SNVSMDRYNR SRLRDVGAMF
TSRSRHFSSL DRMKNSSKSL LTHSFFENES IGLLDAEMAV FFSSIDPICT LHQQLLERLS
SHVNETQAMP PQLQSYCVGD ILVAYAPLFE LYITFACRHG AAMKTIDSAS FTAFLNELSA
EASLRRLGRY LSMPMHQLPQ LKTLLLQLLD ITPHDHADAS SLKLALHHVD TTAKKIETIL
CEYENKEKVS EFAVKLGISL GNRVYVKHGL LRKVCRRRVK QYTFLLLGDA IVFIRDGVSL
RRKPHLIELW ECKVADTPDG VTSIPPMHPT AFYFLSPQKS FMVLAESIAN KNEWIQAIRN
CIAKTFEAHP SENACREPMR PLECMSDVPF VVKNGWLNVT AMGCRKGRRL WITLTMQTFA
FSTAFKATQP DESFDIGCCI ALPLKHEKFF SVSVHLDATK QSDGKRTFIL ETQSLVDRNE
WLRALMHCIG NIGSSSTCTR HHAMELRRRS VHVAVLAPIF MSNKVSSVYS VGVSCVVIAH
DNDGVLRVRP GNGRTTVILD SSPCSGNGA
//
