ID A0A094ZFX2_SCHHA Unreviewed; 1307 AA.
AC A0A094ZFX2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MS3_01526 {ECO:0000313|EMBL:KGB33370.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB33370.1};
RN [1] {ECO:0000313|EMBL:KGB33370.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR EMBL; KL250544; KGB33370.1; -; Genomic_DNA.
DR RefSeq; XP_012793129.1; XM_012937675.1.
DR STRING; 6185.A0A094ZFX2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20811; C1_Raf; 1.
DR CDD; cd01816; RBD_RAF; 1.
DR CDD; cd14062; STKc_Raf; 1.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23257:SF954; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGB33370.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGB33370.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 190..262
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 270..316
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 938..1193
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1217..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 964
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1307 AA; 146835 MW; 332864B12BD12969 CRC64;
MTVDSAVTII PVLQQKCDTL KSKIADFTLV NQALQLKTYQ LLNFINRHED FSGLITKEYD
EVSNDINIVQ SAIDRYTCEL EDWKSKLDQY MMMVTTVVLN NSTNSTTNGS NVSNLNNNNN
GDDSINLTFG STKLPIVASS QSPSLPSVFL SSTNSPVQLD NSSLGTLQSV NNKFSEFKSS
HPTTTTTTKL RLRAHFPNSQ FTLVEIKSGQ QIKHALEKKL SHRGLHLEQL IVYRSRTGLP
VSWEDDAEQI ALIGEELIVD FARRNFKRLE HHFQRKTFFE KAYCNLCHKS IFHGAICKAC
GCAYHNRCLP RVDKNCLSNL DDDVFYVGDQ LSSRNSLGTS NSSIHGSNWL VSSNATPGYT
HFYHFNPEDL TTVRVLTNST GGGFDSNNLL LNSQYLPTSF GSGGGHFPRQ CLSLTCRERS
SSTPNVSNNL IPPNQQKSLF TPSSLGKMKY LLHYILLFSD CCFHMLFRYY GIYMYGRLYP
KHVHNVFSPV CKPNHSKSIK SLLSNLLVSC SFCTGTNTSS HESNYQYYHH CDRPSKSCFK
NTMTDKQLET SNSLCPIIYV NGDNFESNNN NTNSDNIRCN GKYSDRKLST LSAPTYPLKH
CTLDNIRLVN TNSSLLFYHK TSTVTMTTVK PIDAKYMSTY NCNDKVCGEL SMKSRSSTIF
PRSISSCINE RGHNSVAYKS HLHVPYNSYG KLLTIGCDTT IKLHVSSCSS NSSKSSSGIY
ENCQPIGLHS LPLPTKNTYK ETFSTTSQLS TSCSLYEAFS ENPLNIVLTD NTSLRSLSRK
THNLSSNKQE PTSQDYKILL LPKRFYSPNQ NLCPDHISKL SLSPTTYFGI RRVRSFCASM
DSSVGFTEPR YWFYLTQLCK ANKIIQGSPL HIVYPVTNYN YTTGNGVPES PSIPNDGCFL
SNLSIPYNQR SGNDPKQSIK VKNRRGSNDE WEINGQEITK GPRIGSGSFG TVFKGYWHGN
VAIKELNVVD PTPQQLKAFK NEVSVLRKTR HENILLFMGC VSKPCIAIIT QWCEGSSLYK
HLHVLEHRFD VPELVDIAKQ TSQGMDYLHA KNIIHRDLKS SNIFLHDRTV KIGDFGLATV
KSRWWNTGCQ QPTGSIFWMA PEVIRMEGET PYTNLSDVYA YGVVIYELIT GQLPYSHYNN
RDQILFLVGR GLLKPDLTVC RADIPHQLQR LSLDCCSFQR ENRPPFSQIY PCLDSLYRSL
PKLHKCSSEP NINGIVSRGN VTIGSSNNER LDKQSTNTTI SNDHLSSPPP PLHLSDNNNN
NNTEEHVDRT PPSSSIIHDT SSNTSSPPSP SSIVNERTIL IVDNKIV
//
