ID A0A3B4ULE8_SERDU Unreviewed; 444 AA.
AC A0A3B4ULE8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Serum/glucocorticoid regulated kinase family member 3 {ECO:0000313|Ensembl:ENSSDUP00000019501.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000019501.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000019501.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR AlphaFoldDB; A0A3B4ULE8; -.
DR Ensembl; ENSSDUT00000019848.1; ENSSDUP00000019501.1; ENSSDUG00000014185.1.
DR GeneTree; ENSGT00940000153776; -.
DR OMA; FINGGEX; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol 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; cd06870; PX_CISK; 1.
DR CDD; cd05575; STKc_SGK; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR037900; CISK_PX.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF197; SERUM_GLUCOCORTICOID REGULATED KINASE FAMILY MEMBER 3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..132
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 110..367
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 368..444
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 444 AA; 51741 MW; C3A824C5B36D5ED7 CRC64;
MEEQSSLPNV SIPCHNEQRD KRKRYTVYKV MVSVGQQEWF VFRRYAEFDK LYNILRKQFP
SMNLKIPAKR IFGDNFDPEF IKQRRAGLHE FIKRIVSHPQ LCNHAKPTDF DFLKVIGKGS
FGKVFLAKWK HDEKYYAVKV LQKKVILNRK EQKHIMAERN VLLKNVKHPF LVGLHYSFQT
ADKLYFVLDF INGGELFFHL QKERTFPEPR AKFYIAEMAS ALGYLHSLTI VYRDLKPENI
LLDQEGHIVL TDFGLCKEGI SQTDTTTTFC GTPEYLAPEV LRKQPYDNTV DWWCLGSVLY
EMLFGLPPFY SRDTHEMYDN ILHKPLAMRP GATSTAWSIL QGLLEKDRTH RLGSMDDFNE
IKAHNFFSSI NWDDLEQKKI SPPFIPRVSS YSDISNFDPE FTEEMVSSSI CWSQEHSIVN
ASVMEADDAF LGFSYAPPSD DSFQ
//