ID A0A093J985_STRCA Unreviewed; 827 AA.
AC A0A093J985;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Kinase suppressor of Ras 1 {ECO:0000313|EMBL:KFV75494.1};
DE Flags: Fragment;
GN ORFNames=N308_14352 {ECO:0000313|EMBL:KFV75494.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV75494.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV75494.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV75494.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL205841; KFV75494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093J985; -.
DR STRING; 441894.ENSSCUP00000007421; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20872; C1_KSR1; 1.
DR CDD; cd14152; STKc_KSR1; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF716; KINASE SUPPRESSOR OF RAS 1; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 Kinase {ECO:0000313|EMBL:KFV75494.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 275..319
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 542..812
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 112..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV75494.1"
FT NON_TER 827
FT /evidence="ECO:0000313|EMBL:KFV75494.1"
SQ SEQUENCE 827 AA; 93306 MW; 5431DB789A213FFD CRC64;
QVKLIDYIHR QRQCKLSVPL NDRTAELNSY PRFNDWLDIV NVRKEVVQRI PEELTLDALL
EMNESKVKET MKRCGARDEE CSRLNGALSC LRKVTESGGE LKDDVLMNLP EARRESSSVN
PTEPPCSSAP TWTPTALHLP KGSSQQARSA SVSTVPSSDS LASSHGPSVY ADNLLDPFAF
PAHSGRLAAR TPHSITITPP TTPQAKRRHK LKPPRTPPPP CRKVFQLLPN FPTLTRSKSH
ESQLGNRIDE IPPIKFELSQ GSPQMVRRDF GLAVTHRFST KSWLSQICQV CQKSMMFGVK
CKYCRLKCHN KCTKEAPACR ISFLPITKIR RTESVPSDIN NPVDRPTEPQ FGTLPKALTK
KEHPPAINHL DSSSNPSSTT SSTPSSPAPF PSSNPPSATP PPNPSPMGQR DGRFNFPAAY
YIQHRQQFIF PVLKLQIILQ GVKYKTYISD FFVFSEIPSP AQVAQHPETA EDTNADDQPD
TDGVHCEAEV EEPETNKSEP EDDEDEVEDL PNRRPHLQGM IYRKPSQTSV YLQEWDIPFE
QIELGDPIGQ GRWGKVYKGK WHGEVAIRLL EIDGNNQDHL KLFKKEVMNY RQTRHENVVL
FMGACMNPPH LAIITSFCKG RTLHSFVRDP KISLDINKTR QIAQEIIKGM GYLHAKGIVH
KDLKSKNVFY DNGKVVITDF GLFGISGVVQ EGRRENELKL PHDWLCYLAP EIVREMAPGK
DEDRLPFSKA ADIYAFGTVW YELQAREWPF KNQPAEALIW QIGSGEGVKQ VLATVSLGKE
VNEILSACWS FELSERPSFT VLMDMLEKLP KLNRRLSHPG HFWKSAE
//
