ID F0ZKX2_DICPU Unreviewed; 2127 AA.
AC F0ZKX2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=F-box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DICPUDRAFT_152270 {ECO:0000313|EMBL:EGC35404.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35404.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; GL871061; EGC35404.1; -; Genomic_DNA.
DR RefSeq; XP_003288080.1; XM_003288032.1.
DR STRING; 5786.F0ZKX2; -.
DR EnsemblProtists; EGC35404; EGC35404; DICPUDRAFT_152270.
DR GeneID; 10501483; -.
DR KEGG; dpp:DICPUDRAFT_152270; -.
DR eggNOG; ENOG502SCYJ; Eukaryota.
DR InParanoid; F0ZKX2; -.
DR OMA; KLYQGNH; -.
DR OrthoDB; 5324at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IBA:GO_Central.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869:SF211; F-BOX DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2103..2121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..238
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 318..364
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 1894..1927
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 1984..2011
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2127 AA; 247274 MW; EDE090C149E7029E CRC64;
MESDAVISVP ENRIITGSDL LNFNEYADQK FDSSKLERIN LKLSKSNGFI VNNLLTKEEC
DYYIKESERK GYVTIEKEFP THYRNNLRYL GKNDNLSELL WERLEPLFLS DDLEGVRPYG
FDQGGIWIPV GLDNCFTFGK YLPGGRFKPH YDAVFADSPN RRSIYTLQVY LNEEFEGGTT
DFFTHANPLE LEKHILEDSV KPVTGRAILF NHDTLHCGQE VLSGEKYIVR VDMMFLRIDC
ESEELSKTQK EELEKARELF FLADSMEKDK KDLESAISTY VKAQMLLVNY PSFDDTASTL
SKLSLDDSKK KNTQKPKEME LETIPEFQLF LILEKLNCRD ICRLMCTSKY FSRVAKKDSL
WKRLYIREYS MEAFSFEQNI EGSIKVNSTK QQIKKMFNVK SSKQQKAKSW YLTYSNIHKY
ILKNEVAIID IGSEYIKYGD TKNRLGSCVQ KAGKHQEYAP HYVMTTFDRY NWLVGPNISY
YDNTDCVRRG EFKTDALSRE CLKEMINYVC TQVASRKRNL TAPILLIINP IVYASNGGKS
LIETRKSLRN DLILFRNGGL LSLQSHGLKS GIVLMMGRDV FVLAAYHNGH QVDSLQLKVC
GKDLESYLAS FNSPECKSTL FGNDPYYGER TANFKNGWFL LVRASNDYQK EIKERDPYVF
APEIFFNPSL IKYNTAKGVV EETVSFINQM KSKQCFIQNP DPLSTLVITG GFSCIPNFVE
RFTKDLNNAF DSSIKIHASG DRMFDQIIGA KIDLFLTESL HDEYQMMNMN EPSYIPTITR
STLKKNPTPT SSSSNYFYTV TYPEGIIDFS NQVLNGEQLD DLYIFLKKNL KVGNVVWSEE
QDRFDIKFCK IIKRLKKNNE SFNYHPSDYL CGVISGHVYL DKSYFEKEAI DFRDIEIFKQ
GEYTQTQLEH TEQYLKDLKI ISFENDNGFQ YALYENKKLH HVILAFRGTS TNTLKDFALS
FLEDSIGITL KKEDTHQQKK ALEATKKAID HCREKKYNLT ITGHSLGAWL SELAHYYCFY
RFDYTKVKTV VFDSPGALDQ YKVYDDFKEP AIPYTSMDIT VYLSEPNLVN CMNNHLFDGN
SSYRVYPEGI DKVDDSKMDF LLTTKYHSLI PIIQCFDYLT GKPKEYKLIK DWPFITPSQL
SSFMKYFKYN DNGYLENPTN EPIKGVKYKV EQVNLFGGSL VTDVLKIDQY FIQLSLKNYF
NSFNDFFISS QLKELKNLYQ IENAQDKYEI KVTNQSITLE NLKQRLSRVI DLSPKSIKKL
LKSKDDDSNF KEYKIRKNPN INDEDFYDPN NYLQSIAEIH KHQHMAIITG EEGSGKSSLS
LHYATKYYPQ IVQQQYSNQK VLFIKSDTKE MIMEEFGCIL LKNYSEETNG YDFNLSSNNL
TDFYKSIMDS TNTFYFFIFD NVSDPNVIEP FLYYLPKTNT KVIITSQLGK CRFNKNLLLS
KENIQDISVN VQLLTNEQAN DYLHKKGIKS NCNFSSPISI HLLNILLNHQ YLIQNNQPDN
SQPLDFNDLL KFLICDFIKA KPESSEVLYV LPFLDPENIS LDILSKIINN PDYNLEENIR
YWSSISIINE LPNKNINTYK NIQNIILTQI ISNADSLKNQ SKIIGLFESM NLSGEYPKGW
RIYFNHIRFF YNNFNEKVLE HFKIIENYGI CFRLLSLYQD SVKILNQAFE IKKKNNSSNL
ELAFTLFELG KTCVKSNNFN EALAYFSKCE LDVGEEKTTL SETYNYIGLC HFHLNNHDET
PLQFYDKALN LETRTKNLAS IHLNIGNFYL ANEKITEAKN EFFKSLHHSE QESEKNTPIY
AKSIFKMALV EYKEKNYIEA IKKFETSINL FKELFKSSNH KDIGTCYHMI GLCYFQLDDG
IDVNYLLNSL NNLQQALNIR LKIHRTNTCH KELDESYYSL GILYNKRKEH QLSFDYFKKS
YDIKKTNNDN LLDSLEKLST QSYLLGQYQT SIDFTIKQIS IIGNTNEPLL AKCYNILGNC
FRKLNQQQES IDNYENSIKI LNTLIKANER KSNENKSDII KQLNQSIQLY ELNGSNYYGL
YTLSPSNNNY KYQLSHYHNY LKKLSQSPYK NQLTNLSIIQ KSEWYTQYGS NNSILSIIKS
KKFLILTAVI TSSIIIGYLY NHNNSEN
//