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CALM_EMENI
ID   CALM_EMENI              Reviewed;         149 AA.
AC   P60204; C8VLM3; P19533; Q5BBN3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Calmodulin;
DE            Short=CaM;
GN   Name=camA; Synonyms=cam; ORFNames=AN2047;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R153;
RX   PubMed=2199442; DOI=10.1016/s0021-9258(18)77415-2;
RA   Rasmussen C.D., Means R.L., Lu K.P., May G.S., Means A.R.;
RT   "Characterization and expression of the unique calmodulin gene of
RT   Aspergillus nidulans.";
RL   J. Biol. Chem. 265:13767-13775(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 four functional calcium-binding sites.
CC   -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; J05545; AAA62800.1; -; Genomic_DNA.
DR   EMBL; AACD01000032; EAA64879.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF86075.1; -; Genomic_DNA.
DR   PIR; A37123; MCAS.
DR   RefSeq; XP_659651.1; XM_654559.1.
DR   PDB; 6XU4; X-ray; 3.18 A; A/B/E=1-149.
DR   PDBsum; 6XU4; -.
DR   AlphaFoldDB; P60204; -.
DR   SMR; P60204; -.
DR   STRING; 162425.CADANIAP00008716; -.
DR   EnsemblFungi; CBF86075; CBF86075; ANIA_02047.
DR   EnsemblFungi; EAA64879; EAA64879; AN2047.2.
DR   GeneID; 2875471; -.
DR   KEGG; ani:AN2047.2; -.
DR   VEuPathDB; FungiDB:AN2047; -.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_0_1; -.
DR   InParanoid; P60204; -.
DR   OMA; SCDRHPP; -.
DR   OrthoDB; 1386217at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005823; C:central plaque of spindle pole body; IBA:GO_Central.
DR   GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR   GO; GO:0005509; F:calcium ion binding; IDA:AspGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:AspGD.
DR   GO; GO:0051300; P:spindle pole body organization; IBA:GO_Central.
DR   GO; GO:0009847; P:spore germination; IMP:AspGD.
DR   CDD; cd00051; EFh; 1.
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; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Metal-binding; Reference proteome;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..149
FT                   /note="Calmodulin"
FT                   /id="PRO_0000198318"
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          117..149
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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         63
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   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   HELIX           7..20
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           66..73
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   TURN            78..83
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           84..93
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           103..113
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           119..129
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:6XU4"
FT   HELIX           139..144
FT                   /evidence="ECO:0007829|PDB:6XU4"
SQ   SEQUENCE   149 AA;  17013 MW;  37D3DC192C53222A CRC64;
     MADSLTEEQV SEYKEAFSLF DKDGDGQITT KELGTVMRSL GQNPSESELQ DMINEVDADN
     NGTIDFPEFL TMMARKMKDT DSEEEIREAF KVFDRDNNGF ISAAELRHVM TSIGEKLTDD
     EVDEMIREAD QDGDGRIDYN EFVQLMMQK
 
 
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