FHKB_DICDI
ID FHKB_DICDI Reviewed; 1142 AA.
AC Q1ZXH2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable serine/threonine-protein kinase fhkB;
DE EC=2.7.11.1;
DE AltName: Full=Forkhead-associated kinase protein B;
GN Name=fhkB; Synonyms=fhakB; ORFNames=DDB_G0280599;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHK2 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000037; EAS66876.1; -; Genomic_DNA.
DR RefSeq; XP_001134559.1; XM_001134559.1.
DR AlphaFoldDB; Q1ZXH2; -.
DR SMR; Q1ZXH2; -.
DR STRING; 44689.DDB0233266; -.
DR PaxDb; Q1ZXH2; -.
DR PRIDE; Q1ZXH2; -.
DR EnsemblProtists; EAS66876; EAS66876; DDB_G0280599.
DR GeneID; 8622630; -.
DR KEGG; ddi:DDB_G0280599; -.
DR dictyBase; DDB_G0280599; fhkB.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_277634_0_0_1; -.
DR InParanoid; Q1ZXH2; -.
DR PRO; PR:Q1ZXH2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1142
FT /note="Probable serine/threonine-protein kinase fhkB"
FT /id="PRO_0000367467"
FT DOMAIN 480..551
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 625..885
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..302
FT /evidence="ECO:0000255"
FT COILED 393..434
FT /evidence="ECO:0000255"
FT COILED 1090..1132
FT /evidence="ECO:0000255"
FT COMPBIAS 1..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1065
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 747
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 631..639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1142 AA; 133379 MW; 77B9483D73110079 CRC64;
MSQDIQTQNS YSDELYSSQI YSTQQPQQPQ QQPQQQQSTF SSQQSQSSSY DFIYSTPQIH
SQNSQNSQFS QNPLYDDFIH STQNSYSQRV SSQRSYSQKS SSSQISFSQI PSSQIQSSQI
PSSQIHSSQI PSSQNQSSQK SQFSFSQIPS SQIPSSQKRF FQSQNDDFVP SSQVTSLQDI
CLPQPIQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQCQ PQQQQTQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQTQQQQQQP QEDDDDYDDY DGYDNYEDFV YNEGEEGEED YEDYEQENDD
DDDEDEDDDD DDDDDDDDEE EEEESQQQHI RSRALQSRSS QSRPLLRSGF KSPISRLSQT
KTSPEYIYIS SQSNTHTNQL GQSSQQTNSP NVHFNSLQQK KKQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQS QQIIGSQSSQ SSQLPPTQPP VEVPVNLGRL IPINASHIPI NLNLKREDRI
VVGRSSSCDA RLIDNYLTIS GKHCEIYRAD NLTCLKHIPL CKDKTDCHKN FGMLIVHDIS
SNGSYINGEL IGNGKTRILR SDDILSLGHP SGDLKFIFES EFQFNFILDI KDNVNNLNEN
LDYKKLRTAY DNARIENKNC ALRDYYFVKE IGSGGYGIVY EGLYKLNGKR VAIKHIDLLK
NGSTSKSMEL VSKEYNALKN IKHRNVIEFF DIVFSSTDCF FIVELATNDL SNLLRKRCVD
EDDIKRICKQ LLLGFNYLHN LGIVHRDLKP ENILYNEFKQ GFSIKITDFG LSSFVEESQY
LQTFCGTPLF FAPEVIANNF FSNGYGKSCD LWSIGVTLYL SLCKYKPFIV DCRDLYHSFI
NGNLGFTSKK WAKISNYAKD LVRRLLVIDP EHRITIKEAL NHPWFTQDRR FFKKYPKHYK
SRAQPKTQFF VECFNVYYDL KSETGFICFR EHFDNLETNY ALFKQNFDNN NNNNNNNNNN
NNNNNNNNNN NNNINNNNNN INNNNINNNN NNNNNNNNNT NTNNINNNNN NYNNSHNHNN
NNHNHNHNLN NHNHNNNHHH NHNHNHNHNH NHNHNHNHNH NHNHNHNNHN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNY YNNNINNINN NINNNINNNN NYHQQYTQHT
TM
