MYLK_MELGA
ID MYLK_MELGA Reviewed; 154 AA.
AC P56276;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Telokin;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Gizzard;
RX PubMed=1404391; DOI=10.1016/0022-2836(92)90226-a;
RA Holden H.M., Ito M., Hartshorne D.J., Rayment I.;
RT "X-ray structure determination of telokin, the C-terminal domain of myosin
RT light chain kinase, at 2.8-A resolution.";
RL J. Mol. Biol. 227:840-851(1992).
CC -!- FUNCTION: Corresponds to the C-terminus of smooth muscle myosin light
CC chain kinase.
CC -!- SUBUNIT: Binds calmodulin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR PDB; 1FHG; X-ray; 2.00 A; A=1-154.
DR PDB; 1TLK; X-ray; 2.80 A; A=1-154.
DR PDBsum; 1FHG; -.
DR PDBsum; 1TLK; -.
DR AlphaFoldDB; P56276; -.
DR SMR; P56276; -.
DR EvolutionaryTrace; P56276; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Immunoglobulin domain;
KW Reference proteome.
FT CHAIN 1..154
FT /note="Telokin"
FT /id="PRO_0000086407"
FT DOMAIN 42..133
FT /note="Ig-like C2-type"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1FHG"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1FHG"
FT STRAND 122..133
FT /evidence="ECO:0007829|PDB:1FHG"
SQ SEQUENCE 154 AA; 16944 MW; 66F5996028B8345B CRC64;
ISGMSGRKAS GSSPTSPINA NKVENEDAFL EEVAEEKPHV KPYFTKTILD MDVVEGSAAR
FDCKVEGYPD PEVMWFKDDN PVKESRHFQI DYDEEGNCSL TISEVCGDDD AKYTCKAVNS
LGEATCTAEL LVETMGKEGE GEGEGEEDEE EEEE