CALM_KLULA
ID CALM_KLULA Reviewed; 147 AA.
AC O60041;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CMD1; OrderedLocusNames=KLLA0B09427g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9818725;
RX DOI=10.1002/(sici)1097-0061(19980630)14:9<869::aid-yea278>3.0.co;2-u;
RA Rayner T.F., Stark M.J.R.;
RT "Identification and characterization of the KlCMD1 gene encoding
RT Kluyveromyces lactis calmodulin.";
RL Yeast 14:869-875(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels and other proteins by Ca(2+). Among the enzymes to be
CC stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC kinases and phosphatases.
CC -!- MISCELLANEOUS: This protein has three functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; AJ002021; CAA05146.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02341.1; -; Genomic_DNA.
DR RefSeq; XP_451949.1; XM_451949.1.
DR PDB; 4DS7; X-ray; 2.15 A; A/B/C/D=1-147.
DR PDBsum; 4DS7; -.
DR AlphaFoldDB; O60041; -.
DR SMR; O60041; -.
DR STRING; 28985.XP_451949.1; -.
DR EnsemblFungi; CAH02341; CAH02341; KLLA0_B09427g.
DR GeneID; 2897167; -.
DR KEGG; kla:KLLA0_B09427g; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; O60041; -.
DR OMA; SCDRHPP; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0005823; C:central plaque of spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:EnsemblFungi.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:EnsemblFungi.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:EnsemblFungi.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR GO; GO:0007114; P:cell budding; IEA:EnsemblFungi.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0016237; P:lysosomal microautophagy; IEA:EnsemblFungi.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006606; P:protein import into nucleus; IEA:EnsemblFungi.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:EnsemblFungi.
DR GO; GO:1903525; P:regulation of membrane tubulation; IEA:EnsemblFungi.
DR GO; GO:0051300; P:spindle pole body organization; IEA:EnsemblFungi.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR039030; Calmodulin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF401; PTHR23050:SF401; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..147
FT /note="Calmodulin"
FT /id="PRO_0000198319"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 120..147
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:4DS7"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4DS7"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:4DS7"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:4DS7"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4DS7"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4DS7"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4DS7"
SQ SEQUENCE 147 AA; 16063 MW; 98530C60AFB8D282 CRC64;
MSQNLTEEQI AEFKEAFALF DKDNSGSISA SELATVMRSL GLSPSEAEVA DLMNEIDVDG
NHAIEFSEFL ALMSRQLKCN DSEQELLEAF KVFDKNGDGL ISAAELKHVL TSIGEKLTDA
EVDEMLREVS DGSGEINIKQ FAALLSK
