ID A0A1Q9EUV9_SYMMI Unreviewed; 1668 AA.
AC A0A1Q9EUV9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative prolyl 4-hydroxylase 11 {ECO:0000313|EMBL:OLQ11208.1};
GN Name=P4H11 {ECO:0000313|EMBL:OLQ11208.1};
GN ORFNames=AK812_SmicGene5001 {ECO:0000313|EMBL:OLQ11208.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ11208.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ11208.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ11208.1,
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:OLQ11208.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000063; OLQ11208.1; -; Genomic_DNA.
DR OrthoDB; 325231at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817}.
FT REPEAT 1438..1470
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1498..1595
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1668 AA; 184341 MW; 3855DE53DCB4AC6B CRC64;
MGKLGIRKRA ANRGPKRPSP VDQAKAAKDA GRCDEAIELL RAALAGRGAQ VEGLGRASLV
AKYELALLLS QLGRHEEADT WLRQLGLTWK LCPSVLDGSC LKGPTCRGEA NLVAAFDDVL
PSELLLLVQD AFRAGSPFWK EHKYPTPSFF SYNEPLMPDC AAATGAPLIR AVASRVKSLA
VASFPSIFGT EGCERRVSSV EWWAHTRPAG SGSGHQLHYD LDEVSLPTLK EGSLPHHPLV
SCVLYLSCGS ASTASTTIVT DQTLNPGSRA RRAWLCEPKV NRVLLFDGGL LHGVIPNIAL
QAHDPAEPPD PRATLMLGLW GEQGPCGSPA PSPTQPLGPN MQLPQGASWP ELLRTATAEA
PATATPADLA GPVQPVWCPT GASGATDIGV EFIGRWFLSH DPESLQRMVG GTGQIDVEEV
SMEELQQLRA LAENAKSECM HLTSGILDCL PPIDPQTRAP TGLRSLVVNE QQPRGMRSWR
LSGGTLVADE KDAVPMVARP RLIGLLAAHF ATKDASRVDR LRRLLRSVEE QTLSVPLLVS
WSTEDAEDRA SQDGVAERAS AVIDDFQRRG VIHAMPRLRG RRAQFQHYAR LRESLKRHIQ
PSDQPWVFFS DDDDLWHPRR AEEYVVAIQD RPDDVPVVHS RIHLSPGLGP RLPLDATSAE
VTRMEADGLL RLAISAEEEK PGLFGTATGE YFDAAAKFEV FDDFFDRHNN RVIANQFADI
RFRTHLLRGG AARVHRFLPS AGSGSAQSGH DHLPWMYFYD RPTMPYSTPP GEEDLEYVSE
ELPDPKRIAG LRQTLDCVLF QLVPTTGPLE ITEQDFAQSL VGTLNEVTPA NVAMALDRCR
KHGVKVVKCQ HLCDLAQGGW IRSLVGKYSD AKAETVESAA AQEMNALGNL AQGKQEFPMY
TLPLPTFLGL LKLLAHEEMV EAERLTIFDE TMGRAMFVSH QWLASHHPDP DNQQLQVLQA
ALRNLLSGVA QVSQPVQSEL FQGRLKCPTA ADLTSTPLYI WYDFLCCPQD TSERASRNRQ
RAIGGIPSYV SKCKYFVVLC PALAHAEQRE SLSYETWAGR GWLVEISALR GVQEFWEPLK
NLLDRAMLRV RVTVSSSSGW CRAEKMAQDL AARNDSCTII IESSTHAKLN DDLLRLPPAM
GTFTVESDRT RIGHMLVQMI WNKLWYYRER GDLHNYRLLL NEQKSRWFQG LSMDPIDGLV
EGFVTDADSF DQPNEFELAR FLHQNFLRSP LERDSAGWSP ICFAVVRGSS DLVQSLLARR
ADPNDAITKP KKELAMPRRF SLLSLAAVYH NQDVLLTLLS ARADVHARDA RNAIAILWAC
GANDACCIRC LCQARADPSD RCNPGLSALQ VASAFAAQDA MAELMSQAPA LSLKFCLHHA
LVVQGGFYEP ISFLIQAKAD VNEQFEAEGN MWWLVFKLGS FRHKFSPSRL TLISYHHAGA
TPLMFSILSG HFSVVPLLLA AGARTRTSSS CPLRPAQTSI VQRIEHRLAQ LAKLPIETLE
RLVVLRYEPG QEFTLHHDGK FRPITIFLYL NELPADAEGG DTHFPHLGFS FVPRRGCAVM
WPNAQADGAE DSRMVHAGRP PSTGVKYGVN CFFNLATKRL VRPGDLNMSS EECYVVNIAS
LEEGKKQSGE DRSCPRRRTF TLDTDPNVRV DAPCMLQAAL NQKNFRAL
//
