ID A0A1V9XJL3_9ACAR Unreviewed; 488 AA.
AC A0A1V9XJL3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Kinase suppressor of Ras 2-like {ECO:0000313|EMBL:OQR73646.1};
GN ORFNames=BIW11_09606 {ECO:0000313|EMBL:OQR73646.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR73646.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR73646.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR73646.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR73646.1}.
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DR EMBL; MNPL01009567; OQR73646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XJL3; -.
DR STRING; 418985.A0A1V9XJL3; -.
DR InParanoid; A0A1V9XJL3; -.
DR OrthoDB; 5405065at2759; -.
DR Proteomes; UP000192247; 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 GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR Gene3D; 3.30.60.20; -; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR23257:SF780; AT08303P; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OQR73646.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transferase {ECO:0000313|EMBL:OQR73646.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 32..79
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 207..459
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 155..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 53912 MW; 8383C797205510FB CRC64;
MSSVSVNNRR MPHSEPSSPV MDYSKDYVVE PMLPRLQRRL SATKKCRTCH KIVYFTGIRC
KHCGYIAHEA CADATPHVCG GELLRRRRQQ TAFLFTPEAI LAASTCTGGP ASAPVSPKSP
KSPMSPTEFL KTAFSWMKGT KKSAPIVASV PACPSTSAEG AANESKDDRS ATWSSPERPP
SIVAEPTLAS EDSDSAVSEW CIPAKDLQFA KRLRHGREND IFEGRWHGAV SIYTFKRSQE
LWSQVNRLMQ VRHENCSLFM GACIERNNLA IVTSPRNGPL VAEANGQLTL DEKLSVALQV
AQGMGYLHAK GIVHGKLNAS NVVLEKRRAK ICLLDQSFPE VDKDRQGYGC LPKDTLAYWA
PELVKKIHVN GAKVSSRHPS TRASDVYAFG SFLFELFAGQ KPFAGTSAEA MLYKIGNGLT
TDLENFTTEI PRPIRELIAR CWSVVPQDRP TFQQVSAFFQ KNTLACSALH RRHSSSTPSR
LERVGLCR
//
