ID SPKUL_DICDI Reviewed; 1887 AA.
AC Q8SSY6; Q551N9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Bifunctional serine/threonine-protein kinase/NEDD4-like E3 ubiquitin-protein ligase;
DE Includes:
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0276527;
DE EC=2.7.11.1;
DE Includes:
DE RecName: Full=Probable NEDD4-like E3 ubiquitin-protein ligase DDB_G0276527;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase DDB_G0276527;
GN ORFNames=DDB_G0276527;
OS Dictyostelium discoideum (Social amoeba).
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]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. CAMK Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000015; EAL69217.1; -; Genomic_DNA.
DR RefSeq; XP_643080.1; XM_637988.1.
DR AlphaFoldDB; Q8SSY6; -.
DR SMR; Q8SSY6; -.
DR STRING; 44689.Q8SSY6; -.
DR PaxDb; 44689-DDB0219986; -.
DR EnsemblProtists; EAL69217; EAL69217; DDB_G0276527.
DR GeneID; 8620484; -.
DR KEGG; ddi:DDB_G0276527; -.
DR dictyBase; DDB_G0276527; -.
DR eggNOG; KOG0583; Eukaryota.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_236105_0_0_1; -.
DR InParanoid; Q8SSY6; -.
DR OMA; CGEIITI; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8SSY6; -.
DR Proteomes; UP000002195; Chromosome 2.
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; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45982:SF10; HDC11342; 1.
DR PANTHER; PTHR45982; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 6.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1887
FT /note="Bifunctional serine/threonine-protein kinase/NEDD4-
FT like E3 ubiquitin-protein ligase"
FT /id="PRO_0000368227"
FT REPEAT 206..260
FT /note="RCC1 1"
FT REPEAT 262..314
FT /note="RCC1 2"
FT REPEAT 356..409
FT /note="RCC1 3"
FT REPEAT 411..470
FT /note="RCC1 4"
FT REPEAT 472..528
FT /note="RCC1 5"
FT REPEAT 529..581
FT /note="RCC1 6"
FT DOMAIN 1158..1437
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1501..1887
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 19..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT ACT_SITE 1855
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT BINDING 1164..1172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1887 AA; 213011 MW; 6E0D63ED31793F65 CRC64;
MSLFFKSIKS KIEETLNHTP QVNLFNNSNN GGNNSNNGGN NSTPTLTKTP STTNFPYNDY
KNYTYKYVYD NTDNYNFNNN NNNNNNNNNN NNNNTKENNF KSIRESASIY KNNEEINNDD
NNTIINKKKI EEEEDETNFD TSLIPKLGHE DKDELESDHY ITIWGNGIRN YKNCNMSSIG
FSEMYNQQKI VLISTGAIHS SFITDQGNLY TFGDGLLGKL GHGNLESYSS PKLVEFFQTK
PSLRVVSIAN GGKHSLALTI CGKVYSWGGN DSCQLGLGNG SSSSYYSLPQ LINFNISYNN
NNNNNNNNST NNNNNNNNDG AQQQFSLSQN SSSNNNKIKI VKLSCGTNRS AVITDKGLLF
TFGRGDHGRL GLGEQSLLMQ STPKLVQSLQ GHFIIDMSSG GGHSLVLTNK GLVFSFGRND
QGQLGIGCFS NQQTIPKQIQ WFQTSQQQQQ QPINIIKVSA GGYHSIAISD NNDTYAWGRS
DYGVLGTSID VQGDRNLPVL INSNSVVVDN VKFIDVSSGF QHNVAMSIDG SLYSWGCNAG
QRLGFKSDEN QLTPKKCFIN SKDSKPLLFT CGEIITIIVE KRFKEPIIKT ELQLPSSTQS
QQQTELSLPS SVNSSSDSNF NKSIIDNSST TTIIKQTNNN IKSTTTTIIT RPSSPTPSFL
SLANEGKDLL NSTQSNFIEW MTLISKSKGL LNLIQMKATS SLPNLGLSIE KKNKDFDDIN
RQLKLLVNSN LSLSPLPDNI QSEIDRLVLS RNQLGLGLVS EYQTSIDYWL EIKQQKDLTF
LNLSKLLNLS TITTTTTSNT TTTTTATTTT TTTTTTNLIN KKVLVHQDEK QQQREKSETE
LEEEQDEEEE DSEIKNGTLT AIEIQQQSFY LVERLNQGLG NFCNNIMDST TMVQPLTTAT
ASSTTATATA TTTTANTTNS SGIINKNFGE SLRLSMEEIQ LIVLETQKYA IKYHSLLSQQ
LQQCDDLINI HRGKLVEVQD FLNKSKLAQS LLEQREKLKS DYRFCKRNSI ELSKKIEVIE
LDYDQNLCDD DDNNHENNSV NNNSNNNNNN NNNNNNNNNN NNNNNNNIDN NINSNSINDS
SNNNNNNNNI EKLKNELIKL KKDEQKLLSN QQEINELIIE ILDKYVPEFK IKLRANDKIS
SRIKDTGLLV TDRKFQHYDI IKTLSTHPHN VYLANFNDQL VVLKEFGIGD AFGKQIFERQ
VSLLKQMNHK CIMPIQAVFY DRNAFMQMEY ISGGNLLDWC RNNNNDNENN KRRQPWEIQK
IFQQIIQAIA YMHSNCIIHR DLKLENVLIR QDGTPVISDF DLSKDISANV NVTVFNINGG
TELYKAPEMK EQNVKGSYST DIWAFGVMLY KCIFQFVNNN NNGNNGKNNN SDGNENDNNN
NNNFLIIREP FLLPEENNLP LPANHSDQRL ISLLSSIFQR NPKLRPTAHQ IAVHPYFVTS
LVEDLLSSRT LIDCREKIAA FRAHISSLSE MAEEMSESLQ LTVRREHLVL DFFQFFFKKI
ESNKLFCRLE VSFQGEKGLD LGGLSSEMYS LLFSDNQIID NSNNSNNSVS YSIPKNSLFS
KKFNLFENSG TESPFYLLNS NDLFNNNNNN NEENNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNEENP LLILKNEFTI FKILGKIFLK SIIDGKPIPD CFPTSFFKYL LGVKVNLRDL
EIYDPQLAQS FKKVLVLDNI EEYLSTTFEG LIEGGESIPV TDLNKEEFIQ RNIERVLVGC
RQSKLEAFKS GFMSIDSLNA HFALFSPTEL QLLMCGNTLV DSSVLQKNFK FIGFPDTSST
PKDFRRAVDE MNQDEIRLFL RFVTGMVALP LSGFEKSISI IQVPLSQKLP CAHTCSYQLD
LPDYNDFDTT KKKLIKMLEY VDGFAFI
//
