ID A0A3Q2ZUS2_KRYMA Unreviewed; 921 AA.
AC A0A3Q2ZUS2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Kinase suppressor of ras 2 {ECO:0000313|Ensembl:ENSKMAP00000002039.1};
GN Name=KSR2 {ECO:0000313|Ensembl:ENSKMAP00000002039.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000002039.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000002039.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q2ZUS2; -.
DR Ensembl; ENSKMAT00000002087.1; ENSKMAP00000002039.1; ENSKMAG00000001503.1.
DR GeneTree; ENSGT00940000158519; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20873; C1_KSR2; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.10.140.1120; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025561; KSR_SAM-like_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF775; KINASE SUPPRESSOR OF RAS 2; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF13543; SAM_KSR1; 1.
DR Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 403..447
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 634..900
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 160..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 104199 MW; 7A56B8656647CD88 CRC64;
MNEEMTKSEE QHLSLQKALQ QCELVQNMID ISISSLEGLR TKCATSNDLT QKEIRTLEGK
LVKYFSRQLS CKCKVALEER SAELEDFPRL DHWFRIVNLR KEVTEEMSAG EVTLEGLLEM
SEVQVCELLQ KFGASEEESA RLNASLSCLR KAHQLGEGRS KQDWSIPWPT SESGKENTPV
CQPEPSQWIR FQLSQSPQVQ SKYNQHMCHS PQALAPPLYA DRLTVENPAT GLFPSLDSGH
RSLPPSPRQR HFGHTPPRTP LVVNTMTPPG TPPMRRRNKV KAPGTPPPPS RKLIYLLPGF
TALHRSKSHE FQLGNRLDDT QTPKAKKKTK PLNLKIHSSV GSCENLPTQR SPLHTERSLR
SFFFPSFIPS TPPVHAETPS ANTLSVPRWS PQIPRRDLGN SIKHRFSTKY WMSQTCIVCG
KGMLFGLKCK NCKLKCHNKC TKEAPPCHLL IIQRGGRESL KARLVRTESV PCDINNPLRY
TDLHISQTLP KTNKINKDHI PVPYQPDSSS NPSSTTSSTP SSPAPPLPSS ATPPSPLHPS
PQSARQQKQF NLTDVTPEAP PSRAPQVILH PVLSEPGFEQ ISLPLPQNED GNNEDSGDEF
EEMNLSLLSA RNFPRKASQT SIFLQEWDIP FEQLEIGEMI GKGRFGKVFH GRWHGEVAIR
LIDIERDNED QLKAFKREVM AYRNTRHENV VLFMGVCMSP PHLAIITSLC KGRTLYSVVR
DPKVVLDVNK TRQIAQEMVK GMGYLHAKGI LHKDMKSKNV FYDNGKIVIT DFGLFTISGV
LQAGSRREDK LRIPNGWLCH LAPEIIQQLS PDTEEDKLPF SKQSDVFAFG TIWYELHARE
WPYKNQPAEV IIWQIGSGMK PNLAQTGMGK EILDILLMCW AYKQEERPSF SKLVDLLEKL
PKRNRRLSHP GHFWKSAEYV K
//
