ID K7F8V2_PELSI Unreviewed; 1854 AA.
AC K7F8V2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Myosin light chain kinase {ECO:0000313|Ensembl:ENSPSIP00000004462.1};
GN Name=MYLK {ECO:0000313|Ensembl:ENSPSIP00000004462.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000004462.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000004462.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AGCU01193413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01193422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPSIT00000004487.1; ENSPSIP00000004462.1; ENSPSIG00000004151.1.
DR GeneTree; ENSGT00940000157879; -.
DR HOGENOM; CLU_000288_76_2_1; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05762; IgI_8_hMLCK_like; 1.
DR CDD; cd20973; IgI_telokin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; 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; PF16620; 23ISL; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 9.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 9.
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}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..73
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 112..196
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 385..473
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 484..569
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 592..681
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 691..786
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1028..1104
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1169..1257
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1265..1358
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1397..1654
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1744..1833
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 250..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1835..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1854
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1854 AA; 206579 MW; 27DA8FC78CB47234 CRC64;
SRFKAKVRGY PEPRITWYRN GLPITEGEYY IVDCSIRGIF SLVIKSVQEE DGGKYTCEAA
NDGGVRQVTV ELTVEGNSLK KYSLPSSAKT LRGRFSVPSV ENRPSIWGES PPKFATKPNR
VIVREGQTGK FSCKITGRPQ PQITWFKGDI QLQQKDHFNM FEKAGIQFLE IQNVRLADAG
TYTCTVTNSA GKASVSAELM VQGSDKTDLY VHSLCTPTKS TSTATKDHEN SEFKLATSNG
IAKELKSSST NLTVETKERT AVKKEASSIS SKEAKDNRQQ PLRETNTEHT QEPKREVRGS
QGLQKTSSTI TLQTIKLQSE PKAESMATST GQDEDRKGAP QALTTTRQTA SLIRQAGPRS
REAENRVGTR KSTIEEKREL QGFPPRFESR PQSQEALEGQ EVKFRSKVSG KPKPDVEWFK
EGAPAKGRAG IQIYEEDEIH CLCLMKARLE DSGSYSCTAF NPRGRTSTSW VLNVKRSKVE
EIAPWFSSVL KGCTVSEGQD FVLQCSVEGT PVPQITWLLN DEPIQYAHSI FEGGIAKLTV
QDALPEDDGV YTCLAENTAG RASCSAQVAV KEKKSSKKVE SAQSVPTDKT FPPVFLKGLT
DLKVMDGSQV IMTVEVSANP PPEIIWLHNG KEIQETEDFH FEKKGSEYSL YIQEVFPEDT
GKYTCEAWNN LGETQTQATL TVQEPQDGIQ PWFISKPRSV IAAPGQNVLI SCAIAGDPFP
RVHWFKDGQE IMPGAGCEIL QNEDIFTLVM RNVQPCQAGQ YEIQLRNQVG ECSCQVSLML
RESSVSRGEM HRDGREQASS GERRDGDGQG ILTFGRISSS RKSGGNTRSV EEQQEDVRGV
LKRRVETREH TEERLRQQEA EQLDFRDILG KKVNTKSFSE EELKEIPAEQ MDFRANLQRP
VKPKTLSEEE RKVHSPQQVD FRSVLAKKGT PKVSLPEKVP SPKPATPDFR SVLGSKKKPP
AENGSTDTQD QNTSTHSVAQ NASTNSDAQH AKPEVKEEAK NNTNCEHGCS MVDGGIIEKK
VDSNGTAPSF TEKLQDTQVV DGEKLVLQCR IASEPPAAVT WTLDGKAIKS SKFIVISQEG
SLCSLTIDKA LPEDVGQYKC IAENAVGRAE CACTVLVDDP SPTKIPKSAE KKTKKPKSSL
PPVFTTEKGE ATVKKKPAPK TPPKAVLPPQ ILQFPEDRKI RAGESVELFC KVVGTPPLSC
TWMKFRKQIQ ENENIKIENA ENSSKLTISS TKQEHCGCYT LVVENKVGTR QAQVNLTVVD
KPDPPARKPC ASDIQSSSLT LSWYGSSYDG GSAVQSYTVE IWNSVDNTWT DLTTCRSTSY
NVKSLLADRE YKFRVRAANV YGISEPSQES ELVKVGEKQE EIEPKDEAEL SDDEEKETEV
DYRTVTINRE QKVTEFYNIE ERLGSGKFGQ VFKLVEKKTG KVWAGKFFKA YSAKDKENIR
QEIGIMNCLH HPKLVQCVDA FEEKANIVMV LEIVSGGELF ERIIDEDFEL TERECIKYMR
QISEGVQYIH KQGIVHLDLK PENIMCVNKT GARIKLIDFG LARRLESTGS LKVLFGTPEF
VAPEVINYEP IGYATDMWSI GVICYILVSG LSPFMGDNDN ETLANVTSAT WDFDDEAFDE
ISEDAKDFIS NLLKKDMKNR SRLDCTKCLQ HPWLQKDTKN MEAKKLSKDR MKKYMARRKW
QKTGHAVRAI GRLSSMAMIS GLSGRKASSG SPTSPVNTEK VDLDDDAARA FLEAVAEEKP
PVKPYFTKTI LDIEVVEGSA ARFDCKIEGY PDPEVIWYKD DQSIKESRHF QIDYDEDGNC
SLIISEVCGD DDAKYTCKAV NSLGEATCTA ELIVETMGKE EEEEEEEEEE EEEE
//
