ID L5K752_PTEAL Unreviewed; 1232 AA.
AC L5K752;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cyclin G-associated kinase {ECO:0000313|EMBL:ELK06611.1};
DE Flags: Fragment;
GN ORFNames=PAL_GLEAN10022978 {ECO:0000313|EMBL:ELK06611.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK06611.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB031030; ELK06611.1; -; Genomic_DNA.
DR AlphaFoldDB; L5K752; -.
DR STRING; 9402.L5K752; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; L5K752; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd14564; PTP_GAK; 1.
DR CDD; cd14036; STKc_GAK; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR PANTHER; PTHR23172; AUXILIN/CYCLIN G-ASSOCIATED KINASE-RELATED; 1.
DR PANTHER; PTHR23172:SF34; CYCLIN-G-ASSOCIATED KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELK06611.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transferase {ECO:0000313|EMBL:ELK06611.1}.
FT DOMAIN 1..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 351..518
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 524..662
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1168..1232
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 662..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK06611.1"
SQ SEQUENCE 1232 AA; 134346 MW; D6DBEC7730881325 CRC64;
GGFAFVYEAQ DLGSGREYAL KRLLSNEEEK NRAIIQEVCF MKKLSGHPNI VQFCSAASIG
KEESDTGQAE FLLLTELCRG QLVEFLKKSE SKGPLSCDTI LKIFYQVCRA VQHMHRQKPP
IIHRDLKVEN LLLSSQGTVK LCDFGSATTI SHCPDYSWSA QQRALVEEEI TRNTTPTYRT
PEAVDLYSHF PIGEKQDIWA LGCILYLLCF RQHPFEDGAK LRIVNGKYSI PPDDTQYSVF
HGLIRATLKV NPEERLSITE LVNQLQEIAA ARNVNPKSPI TELLEQNGGC GNAAPARGPL
PPGGPVSSGN SMSLALAEYD QPYGGLLDIL RGGTGRLLTN LKDTSSKVIQ SVASYAKGDL
DISYITSRIA VMSFPAEGVE SAIKNHIEDV RLFLDAKHPG HYAVYNLSPR TYRPSRFHNR
VSECGWAARR APDLHRLYSL CRSMHAWLRR DPRNVCVVHC ADGRAASAVA VCSFLCFCRL
FSTAEAAVYM FSMKRCPPGI WPSHKRYIEY MCDMVAEEPI TPHSKPILVR AIVMTPVPLF
NKQRSGCRPF CEVYVGDERV ATTSQEYDRM RDFKIEDGRA VIPLGTTVQG DVLIVIYHAR
STLGGRLQAK MASMKMFQVQ FHTGFVPRNA ATVKFAKYDL DACDIQEKYP DLFQVNLEVE
VEPRDRPGRE APPWESTSMR GLNPKILFSS RDEQQDILSK FGKPELPRQP GSTAQYDAET
GSPDTEPTEP ESPQTGSSTD TNHFLHTLDW HEDKDSETDL ESNFVKEMPS APAEDGGDSE
PSDEDAATLS AESRDTADED TPGPAARAPE PGPAPPASAS GGPPSNADLL SSLLGTPEAA
PEASPGDLLG GEEPLLFTSP APPPGTRSMP RDGPGPAPAS VSTADPFDSL LLTSDLDAPA
QPQPDLFCEF LNADPPAPPA SFPSAHSAPP PACSADFLHL GDVPAELSKV TASASHPDLL
GGWDAWAEAA APTPAAEGPF FSPGGQPAPA GPPASQTKSQ SLDPFADLGD LSTSLQGSSA
GFVPGGFGPK ATPLPKASGS WQTSRSPAQG ASRPSQAKPP PKACTQPRPN YAANFSVIGG
REERGIRAPS FAQKPRVSES DFEDLLPTQG FSKADRRGPR TIAEMRRRDQ ARDVDPLKLK
LLEWTEGKER NIRALLSTLH TVLWDGESRW TPVGMADLVT PGQVKKQYRR AVLVVHPDKA
AGQPYEQQAR MIFMELSDAW AEFETQGARP LF
//