TBCK_DICDI
ID TBCK_DICDI Reviewed; 1033 AA.
AC Q55G97;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=TBC domain-containing protein kinase-like protein;
DE AltName: Full=RabGAP/TBC domain-containing protein;
GN Name=tbck; ORFNames=DDB_G0267760;
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 -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000003; EAL73333.1; -; Genomic_DNA.
DR RefSeq; XP_647287.1; XM_642195.1.
DR AlphaFoldDB; Q55G97; -.
DR STRING; 44689.DDB0231329; -.
DR PaxDb; Q55G97; -.
DR PRIDE; Q55G97; -.
DR EnsemblProtists; EAL73333; EAL73333; DDB_G0267760.
DR GeneID; 8616093; -.
DR KEGG; ddi:DDB_G0267760; -.
DR dictyBase; DDB_G0267760; tbck.
DR eggNOG; KOG1093; Eukaryota.
DR HOGENOM; CLU_011160_0_0_1; -.
DR InParanoid; Q55G97; -.
DR OMA; ENENDAC; -.
DR PhylomeDB; Q55G97; -.
DR PRO; PR:Q55G97; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1033
FT /note="TBC domain-containing protein kinase-like protein"
FT /id="PRO_0000362074"
FT DOMAIN 72..425
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 657..844
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1033 AA; 118086 MW; 90E61199BB8B8603 CRC64;
MMKSDEGVSG NSNNNNNYKF KDNTFRKYGV EVVAYDNNNN NNNNNNNNDD NNTVTVNSRG
FHISIHPFSF RNKLTINQNN GSIGGSSSSS STSNSVSTPK PQSFYVDDAG IAKQLNQSVF
DILSRSRYLS SLSHENLAEF IAAEPSQKHH DQMLIVSEDY KNSLEKQIEI QAKRQTPIPS
NTIGRYAYQI LKALSYLHSQ DLTHRSLSLD NIKLDDNNQI KLTNYGLYYL SDHGENVSFP
IGNLLYLSPE SILRGAKGSS NTKADVWALG CILLHICLGY CIWQDNNPSI VTNRILHLSG
YSTTQSFNSI SKSFEQCELK KTIINEKQHE EYEEYDDDED ISEEEKEKRI KDIKLNNRDN
MNNFINSLKR EEKENSDSNS GSSNSNIGIG LNGLGKELIE IIEQCLIPNP MDRPDSETLL
DHPYFNEYKN IDPYQLQWII KPFTKSWDLP DSLESLTLKE IESYGHIGSD NNGGGGGGGG
ESDSDIYSGK EIYYFWKLLG GNIEKELVNK GFAKASPSVH KLPLYVPVKA SLTESTNSGL
NSPQPYQHQH HQHQHQHQHP NIIKSKNSTV YNNEFCLVEL SNVFLKIKES FKLYGSKVFE
EGIEQSNNNN NNRFNNIENN IELQIIIIRE FHKLLYQYQY DDPTLSQPKI YRLAKLFVPP
ILRGDIWSSI LGVNEREAKQ LYNSINLDVK GPNDKQFELD IPRCHQYHPL LSSRQGHVQL
FKILKAWSLL NLEKGCYWQG LDNVASPFLV HHFFNEPIAF ASLKAFVDKY LSILYVPNNH
AALSEIMLIY QQLLAYHDPE LLNHLMDIQL DPNLYSIPWF ITVFAHILPI DKLEILWDSI
LLCPSSLPNF IAASMIIQFR DSILKMNFED GITMMSMIPS VDVHKCVSDA LSMFNKTPLS
TTVTKFVSNT DQELWWMQEV PFEKRKLELF PRIDIHDLIN DQQKVILDIR TPLQFQQIHY
PSSINVNPKL SKLQQQMEQY KGQQIVVIAP KDQGVDFTNQ LIQWKFPFVS MLNGGMDSLE
HGAHSLLIIS NKN
