ID F2UCJ8_SALR5 Unreviewed; 610 AA.
AC F2UCJ8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=PTSG_06314 {ECO:0000313|EMBL:EGD74305.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
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DR EMBL; GL832968; EGD74305.1; -; Genomic_DNA.
DR RefSeq; XP_004993205.1; XM_004993148.1.
DR AlphaFoldDB; F2UCJ8; -.
DR STRING; 946362.F2UCJ8; -.
DR EnsemblProtists; EGD74305; EGD74305; PTSG_06314.
DR GeneID; 16073780; -.
DR KEGG; sre:PTSG_06314; -.
DR eggNOG; KOG3844; Eukaryota.
DR InParanoid; F2UCJ8; -.
DR OMA; GWYHIPQ; -.
DR OrthoDB; 100633at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
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:UP000007799};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 133..258
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..610
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67649 MW; 3BA937B6BCE7075F CRC64;
MMMDEKRAKV DAGDGSDPKE QKELLSEGLL TKESREKYRN AYVTSKPYPH CIFDPICSPE
EFAQVRDEIV QNLETKYKET DLFKLYQTTD LANIDNTQPE LAAKLPTLLR LRDRLYSKEF
RSFISEVTGC GELTERVDMA ASAYTHGSHL LCHDDVIGTR AVSFILYFSK EGWTAEEGGA
LELYPLDPTS VVKREAQGDE GAEMLVQGVP TAHPTARHLP LFNTMGVFRV MPGRSYHSVQ
EVLSDGSPRL SIQGWFHGPR EPIGNDMASL NQLKTAQERE QPFEPIHADN STDNTSKDSS
KDSSKDSSSS VKPDGVEVDS LSDEDLAFLQ QYVNPVYLKA DAIAAIGKEF ENSSSVQLQR
FLKEDVAARV TAECLEADTK DGLLDERLPR DDTGIEGNWQ VVGPAHMQRF LQYTRASNAA
DKEADKQEDT ASPGATLARL ETAVFRSRPF LRYLSVVTGG RLTGLKTATR RFRSGLDYTV
AHHGQLQAEA ELDATLCFVD DSDELKGAQW TSGDAGGFEC YLAAENEDNV AAEVYCDDDA
AGNDLLSVQP SSNTLSLVYR DPGTMRFIKY VSAASSGSRW DISSTYQLHY DDDDVDEDED
EEDDEGDGEE
//
