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Database: UniProt
Entry: A0A1Q9CP43_SYMMI
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Original site: A0A1Q9CP43_SYMMI 
ID   A0A1Q9CP43_SYMMI        Unreviewed;      1089 AA.
AC   A0A1Q9CP43;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Phosphoribulokinase {ECO:0000256|RuleBase:RU004082};
DE            EC=2.7.1.19 {ECO:0000256|RuleBase:RU004082};
GN   ORFNames=AK812_SmicGene34407 {ECO:0000313|EMBL:OLP84698.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP84698.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP84698.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP84698.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:19365, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57870, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:456216; EC=2.7.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00001430,
CC         ECO:0000256|RuleBase:RU004082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family.
CC       {ECO:0000256|ARBA:ARBA00009719, ECO:0000256|RuleBase:RU004082}.
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:OLP84698.1}.
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DR   EMBL; LSRX01001023; OLP84698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9CP43; -.
DR   OrthoDB; 276087at2759; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006082; PRK.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR10285:SF209; PHOSPHORIBULOKINASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   Pfam; PF00485; PRK; 1.
DR   Pfam; PF02037; SAP; 1.
DR   PRINTS; PR00478; PHRIBLKINASE.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS00567; PHOSPHORIBULOKINASE; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   3: Inferred from homology;
KW   Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OLP84698.1};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:OLP84698.1}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1089
FT                   /note="Phosphoribulokinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013136207"
FT   DOMAIN          453..487
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   REGION          313..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          376..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        330..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  118558 MW;  58F0B15AA27CEFFC CRC64;
     MSRRSNSGAL PLVAVLFGVY ALSFVGPAAQ QRKGTALRAG GESVPTGLVW PSPEAEEKLR
     EVDGIKLYPT HAWKDEMDPI VDASAKLEDT PVIVGVAADS GCGKSTFLRR ILGALGTEVK
     PGHTAIGDMM TVICLDDYHT NDRAGRKATG LTALDAREND FALMGAQIEA LKTGKAVYKP
     IYNHDTGNKD PPELIEPNKV MVFEGLHPIY DEKARSQLDL AIYIDIVNDV KFAWKVQRDV
     AERGWTEEQV REDIEKRLPD FSKYVDPQKA NADVVLRYEP SDKGLPFLKV KLIQKKGGKF
     PMVTLKKAVG QGDLSLSGSE PGATLKASEV SSDKKTKSGK MRERGKQAHD DNEHARPAKS
     LMYDDDWFGN DVTVVEMDGE IDMDNMEEQL KEVESNLEGL GAKSAEAMVS LKSSPGSQNG
     TGLLQTVIAM KVREIYEKIT GKAMRALVTS GEFERLTVPA LRDWLKGQGI ANTGKKQDLL
     DRIRALCFCL EMRLCGWAGQ SLILDGLDAS LMDRSCASID RFETLAMLAR VPRWQSRLTI
     FNFRVHFLRG EVPVHECQAK TIKDGQALAK AGLCGDLINK EPGPIPSHSG LVFQKQTAAD
     ANWAELPEVQ WNGKSKARWA DVCHSTTPVQ FRKGTRSSLR AICAALAAYK CLAQADRFCK
     RDKLSIFEIY DYAPGAWLDG EVVEGMDAAA SLDNLGSTRE LELASKAAFV SANPSNFRLQ
     SGISFEEVGP GTPQRRLWRQ SVAEDEGEAK DCQVWVPAVA FSRVDPGGVR VSKSEQFPLS
     TLLKEFAQAT QAVCTRQMLS IAAQVILGWV GPLLRKYEER CFGEDGMEVL HGLVAATGVL
     VPRCCMTFSV AVRQRPAPDS KCKAVQLSDQ VKLAPQSIQS CIGASESLIA VLRELSATDG
     SGQKRTEMDA NGKMQQNCCA FPLSARHADR MSAGTESQEV HVPHQQEVFI FQLWPVACRV
     RMGVGSEPLL GSIGSPVALF AVNSGACPRT TSASFRGDVS EDASCCALRA AVRPQTRKAA
     AQAMTTASPK LANARSRPAN MRQSLREQLL SVLSALPTYR FSGAFAVTGL ARWKLSALVP
     DGTALATGW
//
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