SEPA_DICDI
ID SEPA_DICDI Reviewed; 1167 AA.
AC Q8T2I8; Q551J3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Serine/threonine-protein kinase sepA {ECO:0000250|UniProtKB:Q5B4Z3};
DE EC=2.7.11.1;
DE AltName: Full=Septase A;
GN Name=sepA {ECO:0000312|EMBL:EAL69186.1}; ORFNames=DDB_G0276465;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000312|EMBL:EAL69186.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69186.1};
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).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT model organism.";
RL PLoS Genet. 2:E38-E38(2006).
RN [4]
RP GENE FAMILY.
RX PubMed=17557329; DOI=10.1002/prot.21444;
RA Miranda-Saavedra D., Barton G.J.;
RT "Classification and functional annotation of eukaryotic protein kinases.";
RL Proteins 68:893-914(2007).
RN [5]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19479821; DOI=10.1002/cm.20386;
RA Mueller-Taubenberger A., Ishikawa-Ankerhold H.C., Kastner P.M.,
RA Burghardt E., Gerisch G.;
RT "The STE group kinase SepA controls cleavage furrow formation in
RT Dictyostelium.";
RL Cell Motil. Cytoskeleton 66:929-939(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the spatial and
CC temporal control system organizing cortical activities in mitotic and
CC postmitotic cells. {ECO:0000269|PubMed:19479821}.
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 Evidence={ECO:0000250|UniProtKB:P41892};
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; Evidence={ECO:0000250|UniProtKB:P41892};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19479821}.
CC -!- INDUCTION: Down-regulated by Pseudomonas aeruginosa, PAO1 strain and
CC up-regulated by PA14 strain infection. {ECO:0000269|PubMed:18590548}.
CC -!- DISRUPTION PHENOTYPE: Prominent defect in cytokinesis and an impairment
CC of multicellular development. In multinucleate sepA-null cells nuclear
CC division proceed normally and synchronously. However, often cleavage
CC furrows are either missing or atypical; they are extremely asymmetric
CC and constriction is impaired. Null cells form fruiting bodies, but
CC these are smaller than the wild-type ones.
CC {ECO:0000269|PubMed:19479821}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000015; EAL69186.1; -; Genomic_DNA.
DR RefSeq; XP_643141.1; XM_638049.1.
DR AlphaFoldDB; Q8T2I8; -.
DR SMR; Q8T2I8; -.
DR STRING; 44689.DDB0229896; -.
DR PaxDb; Q8T2I8; -.
DR EnsemblProtists; EAL69186; EAL69186; DDB_G0276465.
DR GeneID; 8620547; -.
DR KEGG; ddi:DDB_G0276465; -.
DR dictyBase; DDB_G0276465; sepA.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_1_1_1; -.
DR InParanoid; Q8T2I8; -.
DR OMA; NIARDKY; -.
DR PhylomeDB; Q8T2I8; -.
DR PRO; PR:Q8T2I8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IMP:dictyBase.
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:0036089; P:cleavage furrow formation; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031272; P:regulation of pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1167
FT /note="Serine/threonine-protein kinase sepA"
FT /id="PRO_0000393368"
FT DOMAIN 18..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1167 AA; 129682 MW; 88935093F596F1B4 CRC64;
MSKKEPEEIK KNVTVGNYNL GVVIGKGGFG TVYQGLDIED GDFVAIKQIN LTKIPKDQLQ
GIMNEIDLLK NLNHANIVKY IKYVKTKDNL YIVLEYVENG SLSGIIKKFG KFPETLVCVY
IRQVLEGLVY LHEQGVVHRD IKGANILTTK EGKIKLADFG VATKFDDTSA AAVVGTPYWM
APEIIELNGA TTKSDIWSVG CTVIELLTGS PPYYDLGQMP ALFRIVQDDC PPLPEGISPP
LKDWLMQCFQ KDPNLRISAQ KLLKHKWIQA SIKKKPVENG AGGVGNGTDS LGAPANIDDI
AKNITDYNER INKKPSHQRK PSIHPKSPKG KVFLPPPEEE EDEWGDDFSN TPKSIKLPDK
KSPLKLTNNK PSTPLKQQPT NNTPVQQQQQ QQQPPPLKLA VPKQPVIEND DDWGDDFNTV
SDLSKAVGSL NFNNNKKNET PKPNIKKPTF SEDEDEDDDD DGFGSGGDDE DDDFGDIPTS
IKLNPKFGSN IKGNSSGSAN TTNSSSTVVQ QPKLTVSNNN NNNNKKLPLS PRQPSSGNVK
EGINHGSTGS KSGGVIIDQW GEDGEEDNDW GDVATVNFDP KVIRKGTVNK PDLSTRLKNR
IALSETALSN SFNNNGNDDE DEDIFADDFD EDDDEDFDLD KNLMKDNYAR MSSEILKLMN
LLTPEQPEEV ISSACTQLIT MFKENSEQKT LLIRRHGVIP IMEMLEVSNI QSHVLCSILK
VVNQIIDNNM EIQENLCLVG GIPAIMKFSG PEYPASVRLE TASFISKMCS TSTLTLQMFI
ACKGLPILVD FLLSPYAESK RLVWMAVDAI VNVFELQSPT PKNDFCRLFS KCGLLKTLPI
VLRDSIADGE AAATYPDRII NLFIMFSAAD SVVRKTMSAV EVIRPILDTL SQLMPEQLAK
VLKSIKQLSM DHNTLANLQN AGAIRFMVPF LGRRTGAFVA EIHNHVLNTM FHLCRIDPER
QYQAAIDGII PHLQYFITSH SPLNQFALPI ICDLAHSKKA RSELWKNNGV AFYLSLLEER
YWQVNALDSL AVWITDETHK VENIIATNEN IKKLIQLFTN AESQSFAGIL EPLLKIIQIS
IPVNILLGTS NFITKIIDKL GHTNPQVRLN LLKIITSLYE CHPNAKKMIQ EFKLIPIIQK
IADTDKSVLV QKMASKLLEA FNANTVI
