ID L5LZM2_MYODS Unreviewed; 595 AA.
AC L5LZM2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE SubName: Full=Serine/threonine-protein kinase Chk2 {ECO:0000313|EMBL:ELK31492.1};
GN ORFNames=MDA_GLEAN10018492 {ECO:0000313|EMBL:ELK31492.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31492.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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DR EMBL; KB106121; ELK31492.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LZM2; -.
DR eggNOG; KOG0615; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd22666; FHA_CHK2; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF9; SERINE/THREONINE-PROTEIN KINASE CHK2; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELK31492.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000313|EMBL:ELK31492.1}.
FT DOMAIN 120..182
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 227..510
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 67286 MW; 1FE71CBC7053879C CRC64;
MSQETEGESQ QSQGTFSQTP GPSSQTPGPS SQTPGPSSQT PGPSSQSQST SSSSTSTVPT
SSQSSHSSSG TLSSLDTVST QELYSIPEDQ EPEEPVPAPW ARLWALQDGF SNLECVNDSY
WFGRDRSCEY CFDEPLLKRT DKYRTYSKKH FRIFREMGPK NSYIAYIEDH SGNGTFVNRE
LVGRGRRLPL NNNSEIALSV WNNKVFVFFD LTVDDQSVYP KELRDQYIMS KTLGSGACGE
VKLAFERKTC KKVAVKIISK RKFAIGSEKE LPCIIKIKDF FDAEDFYIVL ELMEGGELFD
RVAGNRRLKE ATCKLYFYQM LLAVQYLHEN GIIHRDLKPE NVLLSSQKED CLIKHKTQVS
LKDQITSGKY NFIPEVWAEV SEEALDLIKK LLVVDPKARL TTEEALKHPW LQDEDMKRKF
QNLLFEENKS TALPQLPAQI PLFGAKTIGQ RSPDGPVLSK AEFVEKVRQS NQACHDGDFH
TAIVLYNEAL AVDPQNCILY SNRSAAYMKI QQYDKALDDA IKARLLNPKW PKRERERDRE
LETSMREKHQ SAASCTSPTG DVPATQVHAL DRNRTWDPSV HKPMLYPLSQ TGFGR
//