ID F0YLX0_AURAN Unreviewed; 982 AA.
AC F0YLX0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Calmodulin {ECO:0008006|Google:ProtNLM};
GN ORFNames=AURANDRAFT_67645 {ECO:0000313|EMBL:EGB03894.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB03894.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|RuleBase:RU003857}.
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DR EMBL; GL833159; EGB03894.1; -; Genomic_DNA.
DR RefSeq; XP_009041446.1; XM_009043198.1.
DR AlphaFoldDB; F0YLX0; -.
DR EnsemblProtists; EGB03894; EGB03894; AURANDRAFT_67645.
DR GeneID; 20226350; -.
DR KEGG; aaf:AURANDRAFT_67645; -.
DR eggNOG; KOG0759; Eukaryota.
DR eggNOG; KOG1418; Eukaryota.
DR InParanoid; F0YLX0; -.
DR OrthoDB; 5489807at2759; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.287.70; -; 2.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR45618; MITOCHONDRIAL DICARBOXYLATE CARRIER-RELATED; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF00153; Mito_carr; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50920; SOLCAR; 2.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU003857};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..144
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 171..236
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 423..516
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REPEAT 788..869
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 878..962
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REGION 343..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 102002 MW; 828271E4CB753C92 CRC64;
MGSGPAMLAL LLLAPKRPRL PRMAAIINAN NTPKRRRGLP PLPTALVRGG RRGTSLKAPP
VVQPAPRLPI AKALAAFAAL AASATLALSR LECSLPDAAW LVATTATTTG FGDVAPITPA
GRAVCCGVAL AGFGLVGTLA ARVVDDWVAR QRNPGRRRRR SGLRLGLAAA CLLLFGAAGL
RRCDGLAWGD ALYLSVMVAT TTGYGDVVPS AAGRPFAAAF GLLSAVTFSN LVGALAVAPL
ERELAAARRA ALVSYPAERD TGDSTYPELT PATLAELARG AVVTDLGLSR NSSNISRDEF
TLLLLVKQGL VAPGDLDDAH ARFDALDADK TGVLSQADLD LAGDARRDAS RPAPGDGASE
PAARLGGGRL GGGRRARMSR AALFLAASAA AQAPVNVTVV ALALPAYGEA TTRVWRALGV
EGLHVGCGPA LRSGALNSDL ASPVAAAGVD APFVGVDGLA GGRRYFLRHD ATEPFPLPDG
AVDYVYAEHF IEHVPRSGAL AFLREARRLL SRGGVLRVPD LAAYAASYLG DGSFLAARHR
LNGDLFDLPP GAATLNNIFT AYGHGRGYLY DYAEFLGLLD EADLGCAPER AAFRESRRIP
DVAAAFDGLS RAHESFYVDV DLIDARQAQS AVNSESGAAN STQYVSAMVR ASVRHTRPAR
SANWKFFALG RTSTSLGKWS TQPSPSQCTG TLAWRRNANI GASCLTGSAV IALTNPLDCL
KSRFQVAPHS GGGVAAFARA LVAGDGLWRG LWRPGLATNV CACTISVGTR IGLYPTLRDS
FAPAEARRSP LFMYASGLAG GALGYSVAAP FFYATRVAHV RDLGPGLATL RRLAAPGVRA
LWRGAPLLVA RGAVMSGTQL ATYDSAKGFA VDRGLLDDGP ALHCAASLCA SVSLTTAMVP
LDVTLTHYQA SPPGAGGVAA CARGLLAARG PRVFVRGWLP LWARFLPSTV LTPRPAARVA
TRSNTVDKGT VPTKAPSPST TQ
//
