ID A0A2Y9JJR6_ENHLU Unreviewed; 988 AA.
AC A0A2Y9JJR6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC111148523 {ECO:0000313|RefSeq:XP_022360856.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360856.1};
RN [1] {ECO:0000313|RefSeq:XP_022360856.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022360856.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_022360856.1; XM_022505148.1.
DR AlphaFoldDB; A0A2Y9JJR6; -.
DR STRING; 391180.A0A2Y9JJR6; -.
DR KEGG; elk:111148523; -.
DR OrthoDB; 198307at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08221; STKc_Nek9; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042767; Nek9_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44535; PROTEIN CBG16200; 1.
DR PANTHER; PTHR44535:SF1; SERINE_THREONINE-PROTEIN KINASE NEK9; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 2.
DR Pfam; PF13540; RCC1_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_022360856.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000248482};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777,
KW ECO:0000313|RefSeq:XP_022360856.1}.
FT DOMAIN 52..308
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 388..444
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 445..498
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 499..562
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 563..627
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 628..680
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 681..738
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 14..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 107902 MW; D546947BC7345193 CRC64;
MSVLGEYERH CDSINSDFGS ESGGGGDSGP GPSSGPGPRA GGGAAEQEEL HYIPIRILGR
GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD
NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL
NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV
IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHACLD QDPEQRPTAD
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ
KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV
EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVAGPEVLE PMQLNFFLNN
PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RCSLVSVHLF SGRLGLDSEE DYYTPQKVDV
PKALIIVAVQ CGCDGTFLLT QSGKVLACGL NEFNKLGLNQ CMSGIINHEA YHEVPYTTSF
TLAKQLSFYK IRTIAPGKTH TAAIDERGRL LTFGCNKCGQ LGVGNYKKRL GINLLGGPLG
GKQVIRVSCG DEFTIAATDD NHIFAWGNGG NGRLAMTPTE RPHGSDICTS WPRPIFGSLH
HVPDLSCHGW HTILIVEKVL NSKTIRSNSS GLSIRTVVQS SSPGGGGGGG EEEDSQQESE
TPDPSGGFRG TMEADRGMEG LVSPTEAMGI SSGASSSCPG WLRKELENAE FIPMPDSPSP
LSAAFSESEK DTLPYEELQG LKVASEAPSG HKPPAGAWPP QLNPAATCAG KAAPLPPTCA
CSSLQGEVER LQGLVLKCLA EQQKLQQENL QIFTQLQKLN KTLEGGQQVG MHSKGTQTAK
EEMEMDPKPD LDSDSWCLLG TDSCRPSL
//
