STK4L_DICDI
ID STK4L_DICDI Reviewed; 1105 AA.
AC Q55FS2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein kinase 4 homolog B;
DE EC=2.7.11.1;
DE AltName: Full=Kinase responsive to stress B;
DE AltName: Full=STE20-like kinase krsB;
GN Name=krsB; Synonyms=krs2; ORFNames=DDB_G0267978;
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 -!- FUNCTION: Probable serine/threonine-protein kinase.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase C2
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73442.1; -; Genomic_DNA.
DR RefSeq; XP_647461.1; XM_642369.1.
DR AlphaFoldDB; Q55FS2; -.
DR SMR; Q55FS2; -.
DR STRING; 44689.DDB0216375; -.
DR PaxDb; Q55FS2; -.
DR EnsemblProtists; EAL73442; EAL73442; DDB_G0267978.
DR GeneID; 8616268; -.
DR KEGG; ddi:DDB_G0267978; -.
DR dictyBase; DDB_G0267978; krsB.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_282613_0_0_1; -.
DR InParanoid; Q55FS2; -.
DR OMA; ATWKDNP; -.
DR PRO; PR:Q55FS2; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; ISS:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0012501; P:programmed cell death; ISS:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISS:dictyBase.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF01067; Calpain_III; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00720; calpain_III; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49758; SSF49758; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1105
FT /note="Serine/threonine-protein kinase 4 homolog B"
FT /id="PRO_0000327886"
FT DOMAIN 23..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 348..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..1105
FT /note="Calpain-like cysteine protease-like"
FT REGION 641..668
FT /note="Domain III 1"
FT REGION 791..830
FT /note="Domain III 2"
FT REGION 836..972
FT /note="Domain III 3"
FT REGION 1076..1103
FT /note="Domain III 4"
FT COMPBIAS 411..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1105 AA; 123745 MW; 9C42E5CC6446C2C0 CRC64;
MEESGQLSDF KLPEGIKDPS LEFDLIECLG RGSFGSVYKA TYKKTGNIVA VKLVPINEDF
QEILKEINIM KQCKSKYVVQ YYGNYFKDET CWIIMEYCAF GSVSDMMNIT NRVLNEEQIA
LVCYSTLKGL YYLHRNSKIH RDIKPGNILV SEEGECKLAD FGVSGQLSER TRKRNTVIGT
PFFLAPEVIQ EVGYDNKADI WALGISAIEM AEFHPPYHDL HPMRVLFMIP TSTSPTLKEP
HKWSPEFSDF IALCLAKEQS QRPSAKDLLK HSFFEKKLKG SYVMKSLSET AQMVIERCGG
REEAVKAAAE RKSKQSGVSV DFIHCESVDE PDSSDEEDLL ERNNKRLSTQ IQQKKEQQAQ
QQQQQAQQQQ QQQQQQQQQY QPPSPNNNNR TTTKNNDINE LDSLLNNMMM SSSASASTSP
SPSSISSNGN KSGTTTNDYH TGNGRTSSSS PQFGLQHQNS SNSFPSSPNT VPSVESKPRQ
PASELDDLLE EMMNPSFGNR ARNSSGGGGG LTPIGSPITK RPTPTMQSST TTTTSSSSLP
LPMSPSVYLS PTRVSGIWSG ESAGGCANTT LWRKNPQYLL QITATTTIRI TLRQTGDKLV
HIGFYFARSN TGANDQFRRR ITLTKEYLVP GLDITFLKST EVSAKITMEP GYYVIIPATF
EPNQEGSFEL DVTATSDNIG GQYNSNNNIK LSEIKGDRDW RIISDRFEWR GSSAGGSFSG
SSATWKDNPK FFFETTQTSN TTIVLGKLSD IPKETYIGFY IFKADKNCPF ISLTANNLYS
KTSFVNGIEV VHTQQQMPPG CYIIVPCTYD SRQEGSFTLT CYSDCQQGSI YKLDLSEQIL
TVHGEWRGAT SGGCLNHTTW RNNAQYLIHN TSSSPTKVTI MLEQLEKMDN QQLPFVGFYV
AKSPTPNLDK KLFSLTPKDI VGNTEFINDY QVHFTSIMEP NTSYIIIPST FTPGIEYPFN
LRVITNQHNV IQISRLPEWS TRKLSGEWRG QSCGGRYSNT SSSWTLNPRF RFNLPRGGRF
TIILAQAEKP SYNGIGFYYF KTLQDGTLRE FVCKSGFICG KEIVLESSIN EGVTGVVIPS
TFEPNIQDSF NLTIYSEFDL DFYNN
