CATR_SCHDU
ID CATR_SCHDU Reviewed; 168 AA.
AC Q06827;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Caltractin;
DE AltName: Full=Centrin;
OS Scherffelia dubia (Green alga) (Chlamydomonas dubia).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes;
OC Chlorodendrophyceae; Chlorodendrales; Chlorodendraceae; Scherffelia.
OX NCBI_TaxID=3190;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8292788; DOI=10.1007/bf00042357;
RA Bhattacharya D., Steinkoetter J., Melkonian M.;
RT "Molecular cloning and evolutionary analysis of the calcium-modulated
RT contractile protein, centrin, in green algae and land plants.";
RL Plant Mol. Biol. 23:1243-1254(1993).
CC -!- FUNCTION: This calcium-binding protein is found in the basal body
CC complexes (the functional homolog of the centrosome in animal cell). In
CC mitotic cells it is specifically associated with the poles of the
CC mitotic spindles at the sites of the duplicated basal body complexes.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; X69220; CAA49153.1; -; mRNA.
DR PIR; S42551; S42551.
DR PDB; 3KF9; X-ray; 2.60 A; A/C=20-168.
DR PDBsum; 3KF9; -.
DR AlphaFoldDB; Q06827; -.
DR SMR; Q06827; -.
DR EvolutionaryTrace; Q06827; -.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division; Metal-binding; Mitosis;
KW Repeat.
FT CHAIN 1..168
FT /note="Caltractin"
FT /id="PRO_0000073573"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 97..132
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..168
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:3KF9"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:3KF9"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:3KF9"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:3KF9"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:3KF9"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3KF9"
SQ SEQUENCE 168 AA; 19334 MW; C64D63B9FB66198B CRC64;
MSYRKAASAR RDKAKTRSAG LTEEQKQEIR EAFDLFDTDG SGTIDAKELK VAMRALGFEP
KKEEIKKMIA DIDKDGSGTI DFEEFLQMMT AKMGERDSRE EIMKAFRLFD DDETGKISFK
NLKRVAKELG ENMTDEELQE MIDEADRDGD GEVNEEEFFR IMKKTSLF
