ID A0A8M3AQY6_DANRE Unreviewed; 801 AA. AC A0A8M3AQY6; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 24-JAN-2024, entry version 9. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=dclk2a {ECO:0000313|RefSeq:XP_009290868.1, GN ECO:0000313|ZFIN:ZDB-GENE-050420-170}; GN Synonyms=cb572 {ECO:0000313|RefSeq:XP_009290868.1}, dclk GN {ECO:0000313|RefSeq:XP_009290868.1}, dclk2 GN {ECO:0000313|RefSeq:XP_009290868.1}, sb:cb572 GN {ECO:0000313|RefSeq:XP_009290868.1}, si:dkey-180n16.1 GN {ECO:0000313|RefSeq:XP_009290868.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_009290868.1}; RN [1] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|RefSeq:XP_009290868.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009290868.1}; RG RefSeq; RL Submitted (SEP-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00001433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_009290868.1; XM_009292593.3. DR GeneID; 572548; -. DR CTD; 572548; -. DR ZFIN; ZDB-GENE-050420-170; dclk2a. DR Proteomes; UP000000437; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd17141; DCX1_DCLK2; 1. DR CDD; cd17069; DCX2; 1. DR CDD; cd14184; STKc_DCKL2; 1. DR Gene3D; 3.10.20.230; Doublecortin domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003533; Doublecortin_dom. DR InterPro; IPR036572; Doublecortin_dom_sf. 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; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24347:SF376; SERINE/THREONINE-PROTEIN KINASE DCLK2; 1. DR Pfam; PF03607; DCX; 2. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00537; DCX; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF89837; Doublecortin (DC); 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50309; DC; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|RefSeq:XP_009290868.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M3AQY6}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000313|RefSeq:XP_009290868.1}. FT DOMAIN 64..150 FT /note="Doublecortin" FT /evidence="ECO:0000259|PROSITE:PS50309" FT DOMAIN 191..274 FT /note="Doublecortin" FT /evidence="ECO:0000259|PROSITE:PS50309" FT DOMAIN 411..668 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 712..801 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..398 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 715..750 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 751..765 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 440 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 801 AA; 88575 MW; 0521BC9ADA4B882B CRC64; MSSRNIEWEH FEEREKGHRS PRGSGGSHSG SRGNGIVPSP AHSAHCSFYR TRTLQSLTSE KKAKKVRFYR NGDKYFKGLV YAVSGDRFRS FDALLMELTR SLSDNVNLPQ GVRSIYTADG GKKITSLDDL VEGESYVCAS NEPFRKVDYT KNVNPNWSVN VKTGASRSMP SLTATKNELR ERESKDYIKP KLVTVIRSGV KPRKAVRILL NKKTAHSFEQ VLTDITDAIK LDSGAVKRLY TLEGKQIICL QDFFGDDDVF IACGPEKYRY AQDDFVLDHS ECQVIKSSYS ARSAPPVRYS GSKSPGTGRR SKSPGSARRT AGHFSTNSQS PVKSPINGAP NSQITTPKSA KSSSSSPTSP RSMRNFKIPT HHSSAGNVNG SSETPQHHNN SLSPEVNGNR NLAASTILDK YKIGKVIGDG NFAVVKECVE RSTGKEFALK IIDKNKCRGK EHLIENEVAV LRRVKHPNII MLIEEVDTPA ELYLVMELVK GGDLFDAITS STKYTEKDAS VMVFDLAAAL KYLHRMCIVH RDIKPENLLV CEYPNGTKSL KLGDFGLATV VEGPLYTVCG TPTYVAPEII AESGYGLKVD IWAAGVITYI LLCGFPPFRS ENNLQEDLFD QILLGHLEFP SPFWDNISDS AKELIGHMLQ VNVEARYTAE DVLSHPWVTE DAAMENNMKM EVAGKLKKHF NSVQKQSNTS AGVSVIMNTA LDKETIQLSH RRQDRNPPRP EKRPSSTNPE RRRSNRGRSS VQSEDSRSAA PIEPATSANP SAPAALPSDP SPQFHECNTE SEASKDLLKE E //