ID D9W4K2_9ACTN Unreviewed; 769 AA.
AC D9W4K2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFL19830.1};
GN ORFNames=SSNG_07082 {ECO:0000313|EMBL:EFL19830.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL19830.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL19830.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL19830.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
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; GG657751; EFL19830.1; -; Genomic_DNA.
DR AlphaFoldDB; D9W4K2; -.
DR STRING; 253839.SSNG_07082; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0790; Bacteria.
DR HOGENOM; CLU_000288_63_44_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11102:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 13.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00671; SEL1; 14.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF81901; HCP-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 11..288
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 286..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 769 AA; 83889 MW; 4FA8E53253F8937A CRC64;
MYRGMELAGR YRLDSRLGHG GMGEVWAASD LRLRRTVAVK TVLTSHLRDE RLAAQVLARF
RREGEAAARL NHRNIAVVHD LGEHRQTSAD GQVEVSPFLV MEFLEGRDLA TVLHEYHPGG
LPLEQVVEYG AQVCDGLAAA HTRNIVHRDI KPANLMLLDD GTVKICDFGI AQVQDGTIGL
TMTGALLGSP LYMAPEQLRG QTPTHSADLY ALGASLYELL TGRPPFTADS AYAVIAMHLS
TAPEPPSTHR PAIAPGIDTL ITSLLAKDPV DRPPTAKDVA ARLRSAHLAP GPTNGPAAEA
PETDEERHQR AAEAGNSDAM FSLALLLAEA DRIDEAETWY RKAADAGDSG SMHNLGILLA
NTGRTNEAET WYRKAADSGN SGSMNDLGLL LEDTGRSNEA ETWYRKAADA GQINAMNNLG
ALLQETGRTT EAEPWYERAA DTGHTGAMNN LALLLQNTGR ETEAEPWYQR AADTGHTGAM
NSLALLLENT GRTTEAERWY ERAANTGHTD AMNNLGALLH NAGRETEAEP WYERAANAEN
TEAMNNLALL LQNTGRETEA EHWYERAANA GHTNAMNDLG ALLHNTGRET EAQPWFQRAA
NAGHTNAMNN LALLLHNTGR ETEAQPWYER AANAENTEAM NNLGVLLQNT GRETEAEHWY
RRAVDAGHTN AMNNLGVLLV NTGRETEAEP WYRRAADAGH PDTMNNLALL LVNTGRETEA
EHWFQRAANT GHTNAMNNLA VLLRDTGRET EAEAWYQRAA GTPDGEIRA
//
