ID I3MRZ1_ICTTR Unreviewed; 632 AA.
AC I3MRZ1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Kinase suppressor of ras 1 {ECO:0000313|Ensembl:ENSSTOP00000014886.2};
GN Name=KSR1 {ECO:0000313|Ensembl:ENSSTOP00000014886.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000014886.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000014886.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01050864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MRZ1; -.
DR SMR; I3MRZ1; -.
DR Ensembl; ENSSTOT00000027456.2; ENSSTOP00000014886.2; ENSSTOG00000021257.2.
DR GeneTree; ENSGT00940000156066; -.
DR TreeFam; TF317006; -.
DR Proteomes; UP000005215; 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 CDD; cd20872; C1_KSR1; 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 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; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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 Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 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; 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:UP000005215};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 328..372
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 558..632
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 69420 MW; EE33A07A9681BF4A CRC64;
MDRAALRAAT MGEKKEGGGG GAGAAASRAL QQCGQLQKLI DISLGSLRGL RTKCAVSNDL
TQQEIRTLEA KLVRYICKQR QCKLSVPPSD RTPELNSYPR FSDWLDTFNV RPEVAQEIPR
GLTLDALLEM NEAKMKETLR RCGASAEECG RLQQALTCLR KVTGLGGEHK EDSGWSSLDA
RRESSSGPCA DALPPLGRVG SSGQGPRSIS VSALPALDSP APGLGEGLSD TCIPLHASGR
LTPRALHSFI TPPTTPQLRR HAKLKPPRTP PPPSRKVFQL LPSFPTLTRS KSHESQLGNR
IDEVSPMRFD LPHGSPQMVR RDIGLSVTHR FSTKSWLSQV CHVCQKSMMF GVKCKHCRLK
CHNKCTKEAP ACRISFLPLT RLRRTESVPS DINNPVDRAA EPHFGTLPKA LTKKEHPPAM
NPLDSSSNPS SATSSTPSSP APFPTPTNPS SATTPPNPSP GQRDSRFNFP DISAFPPPAP
IPDSADSARL DDPPKADVLE FPEVEAEEPE AGKSEAEDDE DEVDDLPSSR RPWRGPISRK
ASQTSVYLQE WDIPFEQVEL GEPIGQGRWG RVHRGRWHGE VAIRLLEMDG HNQDHLKLFK
KEVMNYRQTR HENVVLFMGA CMNPPHLAII TR
//
