ID A0A401RPQ0_CHIPU Unreviewed; 1081 AA.
AC A0A401RPQ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=chiPu_0018778 {ECO:0000313|EMBL:GCC20165.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC20165.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC20165.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC20165.1}.
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DR EMBL; BEZZ01001690; GCC20165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RPQ0; -.
DR STRING; 137246.A0A401RPQ0; -.
DR OMA; QFTEPSS; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08477; Roc; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 667..861
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
SQ SEQUENCE 1081 AA; 121537 MW; EC5C1D9EEF62DADC CRC64;
MNGGGRFLVW LCLRFSPGQQ GINVGEDSHK EHQTLFNELR SHPEVKKADI AEMYWDVGHE
DGQEDNMAPG TETVPEIMGS KQSGLSSLPC DQCPTLKSIQ VAYSAGEMER AQQLARLYLE
ANCQVEKLLG IIATHGDTEM LQYLLQETGR ELSKELNDGN PAIIAARQGH EEVIKILLNS
TSDLCVDKDL LSWMLAVSCE QGHLDVVRLL VLVYKAETDS CGVKTQDHPI ITGQPLYAAM
KAGNEEIAEF LLDNGACFSS YVLLDHPELC YRLLRKQFTE PSSQYEISDR QIGLSLKWSC
LKLPWLELDW FIDVSNRITE LDLCRNSLTF LPSVIPWGLV HLKKLNLSAN QLKDLPNVTT
SEEILCLGIL EIDVSRNQLS CLPTGFLHLP RLEKLSAYSN LLEMLFDEEK ATNWIGLRKL
QEIDVSDNKL QLLPCTFLHC CKSLSSLKAS QNALKDFLEP WACPLEFCNV SGNVLISLPN
TLSIFWKNCL KEANFSDNLL KEVPANLFEL KNLNSLKLSG NQIQSLPPVD QWQCSSLKSL
DLSRNHLGKS EEGVRTRKVF FTTWLKKTSD TVSPVEFPQF LGECLEVLHL DNNFLDSVPQ
SVCWLRSLSE LYLSNNPGIR ELPAELGQLA NLWQLDIDQL SISNVPTEIR NEGPSSILTY
LRAQLRKAEP CKLLKMVIVG PPRQGKSTLL ETLQSGKSTQ TMSKESSIQT TSWELLRPAN
LKTKVDSIMF NVWDVGGAAI MSTVNQCFFT DKALYVVVWN LALGEEAVAN LQSWLLNIEA
KAPNATVIVV GTHLDLIDTK FRSERIATLR AYVLALCRSP SGPRATGYPD ISCRNLHEIS
CKTLDGLEGL RKLIFQVACS MKDTGNLTAS QRLVGRLIPK SHFNLLNAVL KEQQRRSSSN
EVQYLTDQQL EEIVQQTPDN DIKDFEDLQT AFSFLIETGA LLHFPDTSHG LRNLYFLDPV
WLSECLARII NVKASHVLAK NGIIQVTELR KLLIGTGFTE QTEEQYFQFL AKFEIALPIT
NNSYLLPHLL PSKPGFEISY LRGKSTNTIQ RLFKMNFVPV GFWQRFITRI LISLAEMDAQ
V
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