ID A0A1Q9CYS6_SYMMI Unreviewed; 411 AA.
AC A0A1Q9CYS6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative prolyl 4-hydroxylase 4 {ECO:0000313|EMBL:OLP88088.1};
GN Name=P4H4 {ECO:0000313|EMBL:OLP88088.1};
GN ORFNames=AK812_SmicGene30625 {ECO:0000313|EMBL:OLP88088.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP88088.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP88088.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP88088.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:OLP88088.1}.
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DR EMBL; LSRX01000829; OLP88088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9CYS6; -.
DR OMA; LPVQGFH; -.
DR OrthoDB; 5488227at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
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 Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
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:SF159; PROLYL 4-HYDROXYLASE 13; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
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:UP000186817};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..411
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012773784"
FT DOMAIN 239..373
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 375..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46815 MW; DC347264F61E4A15 CRC64;
MIVLGLLWAP LLVGTTAIDG ACDLSPWLQE EPVDKGYHVI CVGDGEGTLY LNASAASRSV
LKFDDSLPEF LEELLQIKTH LGFKPHSKRS SAVQWKKQSW AFFTVAGERW TPEEASSKIH
EYDYRGVLLL FEGGTWRWPG IRVGYERPLQ PDSDVILRTV ALKPALFELV LQDATKGTIP
ELLSDVVQMS EKRLQRSLTE KEASEVRTSQ QHWLSYNSHP KLKQLKKFTS EVLRLPSSYF
ERDLQVLRYT KGQLYDAHRD YWDPREFPDE ERFVHPVSKT WNMRFATLLW YLRDAVHGGE
TWFPRAHGGP IPYGEWTACD DRGVKMSGRN GTVAILFYSL YSSGDIDTYS WHCGCPVGEG
TKWAANSWIW NQPQSPPYAK SRTTKVGRNK DNRVSLAPQK KGATDDVAIE S
//
