ID V4A937_LOTGI Unreviewed; 400 AA.
AC V4A937;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LOTGIDRAFT_157676 {ECO:0000313|EMBL:ESP00469.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP00469.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP00469.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KB200701; ESP00469.1; -; Genomic_DNA.
DR RefSeq; XP_009048588.1; XM_009050340.1.
DR AlphaFoldDB; V4A937; -.
DR STRING; 225164.V4A937; -.
DR EnsemblMetazoa; LotgiT157676; LotgiP157676; LotgiG157676.
DR GeneID; 20237461; -.
DR KEGG; lgi:LOTGIDRAFT_157676; -.
DR CTD; 20237461; -.
DR HOGENOM; CLU_035319_0_0_1; -.
DR OMA; SWINVDP; -.
DR OrthoDB; 5471701at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF230; TRANSMEMBRANE PROLYL 4-HYDROXYLASE; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..400
FT /note="Fe2OG dioxygenase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004716684"
FT DOMAIN 106..141
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 226..375
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 400 AA; 45880 MW; 32B381B825F07CB9 CRC64;
MKIGTYRLCL CYLVCKLIAI LADDLTFCYL EDDGIVCGGS ETLRLTRING HEVGAERVVD
PDGKRLTMKT LSLNPLILEI PNFLSSEECD HFISVAKKQG LVNSSTGVNG AQQQMRLLDT
DGDGVLTIHE MRLTIENGFD VYPDDDDILQ MYIDTDLDTN RDGNITKDEM KNLSPRDMKR
YIKKFIEVNP EKHSRYSQQV WMYPDQSTDK TFIDIQNRVS EVVNLPLDVI RLSNFQVVRY
GPHGHYNAHF DSARLSTEVP CCRRFDSRPC RVCRYMTILF YLNDVTEGGE TAFVLAGNDS
LTAEEAKLSP KINLYRNCSE SALHIKPERG KVIVWYNHYI DQQTGWMGEM DDRTLHGGCP
VVTGEKWIGN FWVRVLDTKE EDLERIREIN KKLNKIKTEL
//
