SLOB1_DICDI
ID SLOB1_DICDI Reviewed; 585 AA.
AC Q54TC3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable inactive serine/threonine-protein kinase slob1;
DE AltName: Full=Slowpoke-binding protein 1;
GN Name=slob1; ORFNames=DDB_G0281863;
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:0000305}.
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DR EMBL; AAFI02000043; EAL66491.1; -; Genomic_DNA.
DR RefSeq; XP_640466.1; XM_635374.1.
DR AlphaFoldDB; Q54TC3; -.
DR SMR; Q54TC3; -.
DR PaxDb; Q54TC3; -.
DR PRIDE; Q54TC3; -.
DR EnsemblProtists; EAL66491; EAL66491; DDB_G0281863.
DR GeneID; 8623279; -.
DR KEGG; ddi:DDB_G0281863; -.
DR dictyBase; DDB_G0281863; slob1.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_466485_0_0_1; -.
DR InParanoid; Q54TC3; -.
DR OMA; EVICFGH; -.
DR PhylomeDB; Q54TC3; -.
DR PRO; PR:Q54TC3; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; 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 GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51082; WH2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Actin-binding; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..585
FT /note="Probable inactive serine/threonine-protein kinase
FT slob1"
FT /id="PRO_0000362072"
FT DOMAIN 108..478
FT /note="Protein kinase"
FT DOMAIN 542..562
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT ZN_FING 21..82
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 426..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 585 AA; 64874 MW; FA33D9EFF8AC6E9C CRC64;
MDSSTANSSG TAISKAEWKP DQSSLECNDC QLPFTLIRRR HHCRKCGSIF CDSCSSFYSI
LPIEYGYTGQ QRLCRSCNNS FEQKKQYFET DALVAQFQLR STAQFEYSKP LQDIGHTKHG
LRKSYCMAKN SMGGGEECVV SIITPTPSSC PWSMSNEKKK RKFEKTLLSL KHPYILTPIN
VEVSGANDKI LVIRTFFKQG SLRDQVYKSK PLSPYDTKYI YKQPKSSSSS SSSSSSSSQS
QSVLPIKSIQ KYCKQILESL LYLKSKGIQF SHLHLSNILI NQSNDTCQLV DIENCLLGMK
PLFNDYIYGI GLPQSFKDNL EVICFGHCLF EMIIGIPLGD HSNINSFIPL FPDKVFLLLQ
QIFSEKTPTL EELVKNPWFE VTTTIEQQSL QNGKLKKSQL TFIKDNSNKF ESPKVSLSGS
FSSSNISKLS SSSSNNNSNN NNNNNNNSNT FNNISSNDDK RKSMKLPSST SLLNNSFNLS
NNNNPSSPST STISPNSSLI SSPPKTPILQ TFTPPPPPPP PKSAPPPPPP PSSSKLPPSS
SSRNSLLESI RNADNAKKLK KTTPNTKPKS SIGPHSLKPS STKKK
