ID A0A3Q3LJ11_9LABR Unreviewed; 1641 AA.
AC A0A3Q3LJ11;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-protein kinase 3-like {ECO:0000313|Ensembl:ENSLBEP00000008765.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000008765.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000008765.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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DR STRING; 56723.ENSLBEP00000008765; -.
DR Ensembl; ENSLBET00000009233.1; ENSLBEP00000008765.1; ENSLBEG00000006761.1.
DR GeneTree; ENSGT00940000158534; -.
DR InParanoid; A0A3Q3LJ11; -.
DR OrthoDB; 5321836at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16973; Alpha_kinase_ALPK3; 1.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
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 PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 55..146
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1224..1312
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1340..1571
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 180922 MW; 8659BBA0A88A725E CRC64;
MGSRRITTRS SSGNGRSSNG DVTRPASCSY LSNVRPENRS TLCSVIAQLT EETQPSFETT
LKSKAVSENC NVKFSCVVTG HPTPQVIWYK DDMQLDRYCG LPKYELFRNG QNHSLHIYNC
TVDDAAIYQA SASNSKGIVS CSGVLEVGEM NEYKIHQRYF GKLKQKAENK RREAEGKENQ
EPFRTISPDR TQRKRRSTMD AFLSAPSSTE DEGSEVSPQA VTEEAETRLQ EEAAVEKVEE
KPVPITNGAV SAVTNRQAIS ENINKSGTYI YDSAQKSFTA HKPRTPFVKK KLRISNSAKV
AKSDAPGERT PEERRAVTSV ALTTTEPVRS EGNSEEVMEV ESILWSTVVD STSRNVREQK
AETVEVFPAE RPSEDKVSVK VTMPSHKELL SLSVPPATLT SSSYTVSGTT EKQATKHERD
TARRDKKEKL EMQNISPHSI SAQLQPIAAE AKQQSEVKED ISKKEHVSGM DVDKKSSSST
GGSPAHRDVQ SVNVQVESWT VLPQRPCEQA GDQLSETETS PHQKNVSVSG PTLLSEVTQA
HTKMNRNDAP VIPEVQSNQY TMDVQPPQRT PSKKETMTDD IQTLSLHSVP QSADNIMTQD
TQDHTRGSNE IHTVLYTDIQ KSSLQSPGHA ESSRGCNVSP CAIQSQVDTA IKTVEGTNLQ
VDEKVESNEA SRSLVQSDRW APKERVVEME TDTAALHMTE QIETEEMTKV TNPQTDAASD
EESKKNAHVL KRVEGNTLET HNWKSTRREP AMPLQTKPQE NTSLSQPPIK ELQEIPEPVT
AVISIAELLR SQIKALESTL ANSLTTIPLH ADSVQDPPST GKCTEFKDGN NKPDVRKSKL
DRVTETSNDV PPIRNIKETL MEIYHQLNQT DQELIQTQVE TSPPAPKMIP PISNEETGTT
IKTAGVHGSA REYKECAMDI CPETKTLAVV PQKHSTDVSL SGSESVNSLP LPSKEELIYS
SISKLSGSVT QEAGTPLTVA PLKASSQGEN ITVLEHAKVE PVLSKGIKVT QRLSPEIKLN
SKTEREIKET NSATDFDQYK KEDEKNTYLQ SLQRSPVKSA PGNTISQDLD SSRSTPPASP
TPEASPLLER RNSVSPIPSA TPQELASGAR RKIVIPKARP DEVTDTTSTT DNQSLIKEVS
TQSNRLSPSP VTLSTSPSLS RRSPLLQPPS EPTSPLVRHS PLFSRKKIVP ETQAPSQQPS
QGIQTTKSEE KPAENDKRDP FKAPQVIRKI RGETFTDTSG HLKLWCQFFN VLGDSTIKWY
KNEEQIAQIK RSAGDETQVN LAIVQASCKD SGVYRCTISN EYGTDSTDYL LSADLLAGLS
LREDLGVGEE IEMTPLIFSR GVADPGVWGN KFFGRVMMQE SRIGDGCSHK VWRAKVIYGL
EPVFESGNTC IIKVGNPINY GGKGESCLID RNLDFVKQEC KIQNLAREYC KIFAAEARAI
EHFGPSLEVI PVYLIYRPAN TVPYAKVEAD LTGLYQKYSV LDHTGRIDMK TGSEVERKCC
ALQHWIHQWT NGNLLLTRLE GVDTKITNVG ISVKSTGHQG LSVEGNAKVF EQFVSQHQCN
YFCGLLGLRS LKVMDSLLTP TKPKGSRSPL LQRKTTAGSA SPQNVRKAAG SPRMPRKTEQ
EGRNTTTKQN PAEAPKIVQI E
//
