ID A0A225D4B1_9BACT Unreviewed; 1240 AA.
AC A0A225D4B1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=FRUB_08994 {ECO:0000313|EMBL:OWK36431.1};
OS Fimbriiglobus ruber.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Fimbriiglobus.
OX NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK36431.1, ECO:0000313|Proteomes:UP000214646};
RN [1] {ECO:0000313|Proteomes:UP000214646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA Mardanov A.V., Dedysh S.N.;
RT "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT Planctomycetales with confirmed chitinolytic capability.";
RL Submitted (JUN-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK36431.1}.
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DR EMBL; NIDE01000017; OWK36431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225D4B1; -.
DR OrthoDB; 9795554at2; -.
DR Proteomes; UP000214646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
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; IPR005181; SASA.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF03629; SASA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:OWK36431.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000214646};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:OWK36431.1};
KW Transferase {ECO:0000313|EMBL:OWK36431.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..341
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1240 AA; 133676 MW; 579F6948CD65CB38 CRC64;
MPPVTPPAST ADLLNLLRGS GIHKPGFLGE RLGEFADLPQ EPNRAADVLV RKGLLTRFQA
KLLLAGRHKG FRLGPYIIRD QLGQGGMGTV YLAEHETLRR RVALKVLQPK QKGDHRVNVE
RFLREARAAA ALDHPNIVRI HDVSQDGGIH YLGLEYVEGQ TLEQLLTRGG PITPSLAVGY
IAQAAAGLQH AHEKGFVHRD IKPANLMLTK DGTVKILDMG LARSETATDS LTELIDKGAV
VGTADYISPE QALGNTTVDI RADIYSLGAT FFVLATSRPP FEGNTSQKLV QHQMKAAPNL
TDRDRTFPPE LAKIIAKMLA KKPADRYQTP ADVIAALAPW LSDDGGQKVV IGLSGMDQGS
SSRLQETLNE IATKRIKRPE AKPEAEPQTP PQPIRRGSGK LVGAIAGAVV AALAIIGVIA
YAAWPASKPT ETAAAHPAPV PAQPASAQPA QALPAPAQPA PPQPAPPQPA NVAPAPVPED
VKPAAPKPAG VASKVSIKAG VDGFYVQTPK YEAVIDKLDG CLSSFSASGV EFLRCGAGLA
ANKTTARGGY FYSEKNGHQG LVKLTDIQQP APNVIVATGG SFSVRYEFGV NQLTVTGQNA
TDDTVPYYLL IDSAAVQDVI NEKAEELSVP VARKQGDPLD PKWRTTTWVA DKASLKVTDL
SGDGTARIWG PFSEFQSQVW EADAKTYNNV QFTLEPVNGP ERPKAVLKPG GVLITRSGSS
RRVRTELYEA TVDANACMPS LRVDGVEVLK ANIDVSKGVY FLPGFPLPPF DIKQPSTTTI
SAQSDKAAVQ YDFGPNKMTW TVENRSDQGM PFFVVMDTTV TGVCNDKDVW AKTPTGGPPN
TNWATSTWYA GRAKFKMTGG SRIWGPWQDK YQVWEASLAP KEKRTVTVEL GLTDATEAAK
LGEITGTKPL LATALTLDAP MDYQVFQRKT KFEGAMTLNG RVRSDYDRLE VRTIGKSLQG
AVPDQWREVP LPETTRSFET TVPTPAGGWY KVEVRAFKDG KVIGQMAVDH VGIGEVFIGA
GQSNSTNCGQ EKIRQNSGMV SSFSGTNWQL GDDPQPGVHD NSAGGSFWPA FGDAMFEEYQ
VPIGVASTGH SGTSVNQWAP GSDLCRWTTG RMNQLGKNGF RAVLWHQGES DVSMPADEYA
RKMTALIKET RRGAGWDVPW FVAQVSYHNP NQITFPLPRA AQKKLWESGT AFEGPDTDTL
TGDNRDEGGK GIHFSAKGLK AHGKMWAEKV AVQLDKELAK
//
