ID A0A091MXR3_9PASS Unreviewed; 1334 AA.
AC A0A091MXR3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Myosin light chain kinase, smooth muscle {ECO:0000256|ARBA:ARBA00021842};
DE EC=2.7.11.18 {ECO:0000256|ARBA:ARBA00012430};
DE AltName: Full=Telokin {ECO:0000256|ARBA:ARBA00030959};
DE Flags: Fragment;
GN ORFNames=N310_13783 {ECO:0000313|EMBL:KFP82258.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP82258.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP82258.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP82258.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; KK839499; KFP82258.1; -; Genomic_DNA.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004687; F:myosin light chain kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd20973; IgI_telokin-like; 1.
DR CDD; cd14191; STKc_MLCK1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015725; MLCK1_kinase_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 6.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|EMBL:KFP82258.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFP82258.1}.
FT DOMAIN 1..49
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 73..161
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 171..266
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 518..606
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 657..745
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 753..846
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 884..1139
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1225..1314
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 267..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 913
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP82258.1"
FT NON_TER 1334
FT /evidence="ECO:0000313|EMBL:KFP82258.1"
SQ SEQUENCE 1334 AA; 147785 MW; 111096D4BA12CBE7 CRC64;
DQPIQYAHST FEDGVAKLTV QDALPEDDGI YTCLAENNTG QASCSAQVTV KEKKSSKKTE
STQAAKLNKT FAPIFLKGLT DLKVMDGSQV IMTVEVSANP APEIIWLHNG KEIQESEDFH
FEKKGNEYSL YIQEVFPEDT GKYTCEAWNE VGESQTQATL TVQEPQDGIQ PWFISKPRSV
TAAPGQNVLI SCAIAGDPFP TVHWFKDGQE IVPGTACEIL QNEDIFTLIL RNVQSRHAGQ
YEIQLRNQVG ECSCQVSLML RESSASTAEM LRDGRESASS GERRDGGDHG KLTFGRTSGF
KKNSSETRVA EEEQEDVRGV LKRRVETREH TEESLRQQEA EQLDFRDILG KKVSTKSFSE
EELKEIPAEQ MDFRANLQRQ VKPKTLSEEE RKVHAPQQVD FRSVLAKKGT PKAPVPEKAP
PAKPAVTDFR SVLGSKKKPP AENGSANTPA PNARTNAEAQ NATPNSQAPV AKPAVKKEEK
NDRNCEHGCA VVDGGVSGKK AENKAPASKP PASKGTAPSF TEKLQDAQVE DGEKLVLQCR
ISSDPPAAVT WTLDSKPIKS SKSTVISQEG TLCSLTIEKA TPEDGGEYKC MAENAAGKAE
CACKVVVEDA SKTSKTTEKA KTKKPKTTLP PVLPTESEAT VKKKPAPKTP PKAAAPPQIT
QFPEDRKVRA GEAVELFAKV VGTAPITCTW MKFRKQIQES EYIKIENGEN SSKLTISSTK
QEHCGCYTLV VENKLGSKQA QVNLTVVDRP DPPAGTPCAS DVRSSSLTLS WYGSSYDGGS
AVQSYTVEIW NSVDNKWTDL TTCRSTSFNV QDLQADREYK FRVRAANVYG VSEPSQESDL
VKVGEKQEEP KEDEAELSDE EGKETEMEYR TVTINTEQKV SDVYNIEERL GSGKFGQVFR
LVEKKNGKVW AGKFFKAYSA KEKENIRDEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEM
VSGGELFERI IDEDFELTER ECIKYMKQIS EGVQYIHKQG IVHLDLKPEN IMCVNKTGTS
IKLIDFGLAR RLENAGSLKV LFGTPEFVAP EVINYEPIGY ETDMWSIGVI CYILVSGLSP
FMGDNDNETL ANVTSATWDF DDEAFDEISD DAKDFISNLL KKDMKSRLNC TQCLQHPWLQ
KDTKTMEAKK LSKDRMKKYM ARRKWQKTGN AVRAIGRLSS MAMISGMSGR KASGSSPTSP
INADKAENED AFLEEVAEEK PHVKPYFTKK ILDMEVVEGS AARFDCKIEG YPDPEVMWYK
DDQPVKESRH FQIDYDEEGN CSLTIAEVCG DDDAKYTCKA VNSLGEATCT ADLLVETMGK
EGEGEGEEED EEEE
//
