ID A0A099ZSE4_TINGU Unreviewed; 1499 AA.
AC A0A099ZSE4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=N309_06410 {ECO:0000313|EMBL:KGL84048.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL84048.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL84048.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL84048.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR EMBL; KL896989; KGL84048.1; -; Genomic_DNA.
DR STRING; 94827.A0A099ZSE4; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20865; C1_MRCKbeta; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGL84048.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 255..325
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 917..967
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 987..1106
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1131..1405
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1473..1486
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT COILED 352..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 592..719
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 809..850
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL84048.1"
FT NON_TER 1499
FT /evidence="ECO:0000313|EMBL:KGL84048.1"
SQ SEQUENCE 1499 AA; 171573 MW; 929385157B6AF41B CRC64;
QVAVVKMKCT ERIYAMKILN KWEMLKRAET ACFREERNVL VNGDCQWITT LHYAFQDENY
LYLVMDYYVG GDLLTLLSKF EDKLPEDMAR FYIGEMVLAI HSIHELHYVH RDIKPDNVLL
DMNGHIRLAD FGSCLKMSED GTVQSSVAVG TPDYISPEIL QAMEDGMGKY GPECDWWSLG
VCMYEMLYGE TPFYAESLVE TYGKIMNHEE RFQFPSHVTD VSEEAKDLIQ RLICSRERRL
GQNGIEDFKS HAFFEGLNWD NIRNLEAPYI PDVSSPSDTS NFDVDDDVLR NPEVVPPSSH
TGFSGLHLPF VGFTYTTDSS LSDRGSLKSA MQSDTVTKDM DAQRDLKNSS QIEGYEKKIR
KLEQEKQDLS RKLQESTQTM QNLQGPVSVT VNANRDKEIK KLNEEIERLK NKLTDISKLE
GQLADAVAFR QEHEDSIHKL KGLEKQCRVL RQEKEDLHKQ LVEASERLKT QSKELRDAHQ
QRKLAVQEFS ELSERVGDLR SQKQKLSRQL RDKEEEVEVS MQKIDAMRQD IRKSEKIRKE
LEAQLEEVAA EASKERKLRE HSEVFSKQLE NELEALKLKQ GGRAAGVTLE HQQELSKMKS
ELEKKILFYE EELVRREASH VLEVKNVKKE VHDSESHQLA LQKEIMILKD KLEKAKRERH
NEMEEAVGTM KEKYERERSM LLEDNKKLTT ENERLCSFVD KLTAQNRQLE DELQDLAAKK
ESVAHWEAQI AEIIQWVSDE KDARGYLQAL ASKMTEELES LRSSSLGSRT LDPLWKVRRS
QKLDMSARLE LQSALDAEIR AKQLVQEELR KVKDANISFE SKLKESEAKN RELLEEMEGL
KKKLEEKYRT DTGLKLPDFQ DSIFEYFNTS PLARDLTFRI HDIHSNILEG HWGRGAFITE
IQKLKTFYPE CVFQPKAHQL NIKSFTSPTQ CSHCTSLMVG LVRQGYACDV CSFACHVSCK
DSAPQVCPIP PEQAKRPLGV DVQRGIGTAY KGYVKVPKPT GVKKGWQRAY AVVCDCKLFL
YDVPEGKSTQ PGVVASQVLD LRDEEFCVSS VLASDVIHAT RKDIPCIFRV TASLLGLPSK
SCSLLILTEN ENEKRKWVGI LEGLQSILHK NRLRNQVVHI PQEAYDSTLP LIKASLAAAI
VDRDRIAIGS EEGLYVIEVT RDVIVRAADC KKVYQIELAP KEKIIILLCG RNHHVHLYPW
TSLDGSEGSF DLKLAETKGC QLIITGTLKK SSSTCLFVAI KRQVFCYEIH RTKPFHKKFS
EIQAPGTVQW MTLFKDKLCV GYQSGFSLLN IQGDGQSINL VNPNDPSLMF LSQQSFDALC
AVELSNEEYL LCFSHMGIYV DSQGRRSRMQ ELMWPATPVA CSCNSSYVTV YSEYGVDVFD
VNTMEWVQTI GLRRIRPLNM DGTLNLLNCE PPRLIYFKNR FAGFSLFTQL MHDNMQRLEI
TTVKNHSSPC PLPLPFFFPR EMLKDPELRS KMISNPTNFN HVAHMGPGDG MQVLMDLPL
//
