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Database: UniProt
Entry: A0A024TQA2_9STRA
LinkDB: A0A024TQA2_9STRA
Original site: A0A024TQA2_9STRA 
ID   A0A024TQA2_9STRA        Unreviewed;      1272 AA.
AC   A0A024TQA2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=FYVE-type domain-containing protein {ECO:0000259|PROSITE:PS50178};
GN   ORFNames=H310_10976 {ECO:0000313|EMBL:ETV95512.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV95512.1};
RN   [1] {ECO:0000313|EMBL:ETV95512.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV95512.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI913980; ETV95512.1; -; Genomic_DNA.
DR   RefSeq; XP_008875706.1; XM_008877484.1.
DR   AlphaFoldDB; A0A024TQA2; -.
DR   EnsemblFungi; H310_10976-t26_4; H310_10976-t26_4-p1; H310_10976.
DR   EnsemblProtists; ETV95512; ETV95512; H310_10976.
DR   GeneID; 20088026; -.
DR   VEuPathDB; FungiDB:H310_10976; -.
DR   OrthoDB; 5481504at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_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; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR   PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          128..188
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          32..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1272 AA;  140413 MW;  EF3DC0521DF683A2 CRC64;
     MASLHGTSSS LDSKIMIELA TKNSSFPIDV VPSLSPTSSR PNASQAPENP LFAKHSPAEK
     RLTSFPQPGL VSDVEDLLDE RTQRSSGPRL SPVAVPPPSL PLIIPTVLSP AKRGAATSPH
     TRQTWMPDKV CKVCSDCGES FNIFRRRHHC RGCGHIFCHS CSPYAVESIE QGVKTHVRIC
     KRCHMNHSSS AINTTEVAMD FPPGLMSPIV SQTVFDYGNV AGFDLEFDPS DTVLPSVVDT
     SDTAQRSNSL YAHLFRRPSS ELASALKAIH DAEEHLEKSA SSMLDMVDEE SGGRGSMSQD
     QHWHRDHLDC QSPPLSSTKS RLSARHSFTE GMDGCQGLWA DHPDHIEAPV EPTPCTPFEA
     HQMAGRRQLR KLLVRGLDTA VDSLLPDAKD RVAVQDELER VIDETTDLLI RATYNRNAAD
     GMFNHQDMLH IKTIAEVPDD VPSTDTRSTY TGQVIHGIVC RKNVSHKKAP RMLENPRVLL
     LGGSIVTDRE SLKLTKFEDL LNDEAVYAQQ LVDKILAVKP SVVFVEQSVS RLAQDQLQLH
     NIALVLKVKE ATLRRLERLT RAKMVPSIDT MQPDDTSVVG TACGSFAVMP MRVADLTKEP
     GGWKRDSILI VDGCDASAGC TILLKGPNKA VLRALKALVL QLVPRAYDLM LRAEALADLA
     YPVRSNLADD EPDDKWTFQV IKYMLKHRDE VHKPKFSQCS RPQPHEVAFY SKHDKALGSY
     LQKEGIDSST KCQVPNCKVP LIEHLEAYSF FNGTVLISTE HLPDVARTEI ERTEGQHAAA
     AASDNQPLER SGTCMDDDST GPTIFFWRHC RECSKMVMPP RLLPVTTLKF SFARFLETIF
     NVPGPQSMPG HGPSELCTVY ESIPLESSDD SAATTLLANK GQASETSRHD QDPRDCICPH
     DGQTQHLLYF KCGKRAIRVE YMHDEPWSIK HDKCLHFDQN WYVAHQRQQA ADLKQAMANH
     FAVLYAKLRT LPPSSREVMC LELLMKTAQK TYMNELTDLM EHGEVVHASS VVRSAACVWF
     DDDSFQVDAN TVRRAFYHSC CDWSVMVHKI TKSLSANATP LDTSPPSNDI APVGDVDGMP
     ATPLAQSARV ELDALGLDTS STEGAPVEGD LPPLPPISVK ELSTGEMTPP VTMSSPSPMS
     WTTALSNSLG AILLGDKKPM DTLALDPHHA VPDVFAGGHP FLPVGANDRV VYVYDHLRFS
     FVTYALNSSE YLNETTAIRA ALEHDHVGEF LTSPVDTTVK LKVSSSDVEF TCQVHYALQV
     VPRVVDRHHV AT
//
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