ID A0A0W8CY45_PHYNI Unreviewed; 537 AA.
AC A0A0W8CY45;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Calcyphosin protein {ECO:0000313|EMBL:KUF88920.1};
GN ORFNames=AM587_10011389 {ECO:0000313|EMBL:KUF88920.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF88920.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF88920.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005104}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424}.
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:KUF88920.1}.
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DR EMBL; LNFO01001760; KUF88920.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8CY45; -.
DR EnsemblProtists; KUF88920; KUF88920; AM587_10011389.
DR OMA; VRYYANV; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR PANTHER; PTHR34524; CALCYPHOSIN; 1.
DR PANTHER; PTHR34524:SF6; CALCYPHOSINE-LIKE-RELATED; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 271..306
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 307..342
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 343..378
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58585 MW; ECFAA521FE2E780C CRC64;
MSTLTSTDMG ELKRPTTRVH APPGGGSSWS FGDYSTPAST GRKRVNQXQT QPEQDTKMES
PRSSPPPAPV QIQNQNETQV TFQTESAVRV ALLKTSSDAE IVDTAVQNCQ AKLSEAVNSE
IFTVANIEQL PYAANKLTEF GGFDGVICFG FLNTQDPQFT AISAALTQSL IKISVKNVRP
VVHAVFIGEP RVASVKVRGG WGAEFAEGVV PLINLGGFIG PIAHPASGSP VKKHFEVSRG
NVLPAKLLRG SKTVLQSLEI LRDSLYEHGA KGIRGLGRKF RIIDDDGNRS LSLDEFSKAI
REHALELNEQ EVEELFHFID TNNSGGVDFD EFLLAVRGEL NERRTQLVLA AFKILDADGS
GVVDLDDIKA KYSAKQHPDV LQGRKTEDEV LLEFLDTFDG GEKDGKVHPS EFVRYYANVS
ASIDDDDYFE LVIRNAWHMS GGEGWSANTT CRRVLVKHED GRHTIEEVKD DIGIGAGNVE
AIRENLQAQG INDIQSVSTT GNVQAESDAN KRSNDSFQPQ VARKKQHGAG QSSIIFG
//
