SLOB2_DICDI
ID SLOB2_DICDI Reviewed; 574 AA.
AC Q54WZ5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Probable inactive serine/threonine-protein kinase slob2;
DE AltName: Full=Slowpoke-binding protein 2;
GN Name=slob2; ORFNames=DDB_G0279303;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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:0000305}.
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DR EMBL; AAFI02000030; EAL67800.1; -; Genomic_DNA.
DR RefSeq; XP_641782.1; XM_636690.1.
DR AlphaFoldDB; Q54WZ5; -.
DR SMR; Q54WZ5; -.
DR STRING; 44689.DDB0229843; -.
DR PaxDb; Q54WZ5; -.
DR EnsemblProtists; EAL67800; EAL67800; DDB_G0279303.
DR GeneID; 8621979; -.
DR KEGG; ddi:DDB_G0279303; -.
DR dictyBase; DDB_G0279303; slob2.
DR eggNOG; ENOG502QWJ5; Eukaryota.
DR HOGENOM; CLU_475245_0_0_1; -.
DR InParanoid; Q54WZ5; -.
DR OMA; IHYEIRC; -.
DR PRO; PR:Q54WZ5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IBA:GO_Central.
DR GO; GO:0043271; P:negative regulation of ion transport; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF02205; WH2; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..574
FT /note="Probable inactive serine/threonine-protein kinase
FT slob2"
FT /id="PRO_0000362073"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 166..346
FT /note="Protein kinase"
FT REGION 366..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 574 AA; 64025 MW; 9E488DCCE606D4CC CRC64;
MEYYYYIIIA AVGGFAILTF IIIVVLRLKK SQKMREPLLP KEKGNVFVYK RDTQVQEKEE
QVMMNARLYL RSTIYSLQDK IPKFGSRSDK VYFGVLGNSL NKLENDRIMA MVPVSKHWPI
PLNSEAGRTT FRTIIKSLEI HPFISVPLLV DFIPEKHVAV SVRPFYADRG SLRDFIHKSK
PKMPYADKYD THLQLNEKIV SKFGRQILEA LIFLKNHNFP YFHLNSANVL VDDQICLISD
YENSFLGLEP RFSDFIRQHN EKIDPDVLSF GLVLFEMACG YEMENPHSVD ISIPAHCYPE
VRKVLEAIFK PFYGTPITLE ELSKMDFFSY HKFKNLPLHR LTYTSRERDM MDAVIKLNKT
FLSTNSKPNS KDLSQPKLKD LKKQKKRKQL VFTQSFEPIK MESQNGGGAA GGEYGNEGGY
AISTSSSLPS NFLANVKPAN STSYSLLSNT TTNTTNTSTS SSLNSSFNSN VSTSYSNATT
TTNTTSASSV SPPISSPPPP PPPPPPSKSS GPPPPPPPPP KSSGPPPPPP PKSSPPPPAD
GSRKGLLSSI ESFSSSKLKK TKTVDKSGPL LKKS
