ID A0A2U0H9E6_9MICO Unreviewed; 952 AA.
AC A0A2U0H9E6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DEA06_07020 {ECO:0000313|EMBL:PVW05477.1};
OS Microbacterium sp. Gd 4-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2173179 {ECO:0000313|EMBL:PVW05477.1, ECO:0000313|Proteomes:UP000245623};
RN [1] {ECO:0000313|EMBL:PVW05477.1, ECO:0000313|Proteomes:UP000245623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gd 4-13 {ECO:0000313|EMBL:PVW05477.1,
RC ECO:0000313|Proteomes:UP000245623};
RA Spirina E.V., Kuleshov K.V., Rivkina E.M.;
RT "Genome sequencing and assembly of Microbacterium sp. Gd 4-13.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVW05477.1}.
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DR EMBL; QEIJ01000002; PVW05477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U0H9E6; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000245623; 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:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR025519; DUF4407.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF14362; DUF4407; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000245623};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 606..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..477
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 746..773
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 952 AA; 102793 MW; 6EC28FAC3AE66FEA CRC64;
MRVQPWMPFL KPPWTTARAT TSPSPCSSST SRRGRHPGSS SRPTRANARP PTTRTSCSSM
RRSPLQRRHP ACARRASRKR RCQTATRAGA PVARYSDVAR VARVTTGPRD RCPTELHRPP
PRLLPTADLK GLLMSQPLPP ASPNDDTPDE PGDLPTAPLP TSDGEKSHTP TAPLPDSPVT
RAFAITPDRI LEELPAESGE TASEALHYIA FASRDGRLDR VGLGTYSDVY AGHDRDGAPV
AIKMFRGDDA EAIRPLVAKE WRASQRDFGP RVVHSYAAYL VSNDLGDRAW ALIMNLVPGQ
NLAQVMTDVA LGASLDHETQ VRWLRAALDG LQVLAAAQHQ LRDVKPENIG LDHEDLEQAL
PVFFDHGAAK REGTMTLMYA GTPAYAAPEW TRRTEDGDLS KVDIYSLGAS LIDVFTGGQG
FEGGVMDDER GLVGRPRLDD LRLSPDVARV LRGALVKDPA LRPGVDELLD VLTIPTLTTP
PWDPYRPYAA GAGTAAPEAT TPLLADRAEA SSESDTAPLP DLHGAASGFT TTPSPPLPTG
LQGRPDPVRV PAAQPASPLA DVRLLPLTEE IASLEQRGTM TPVRGRWLEK FAGVDPRYVV
KRSNRVVYNI VGLLLIIYAV YATSAITALV TMATGDTSAW RVVVGILIGA LVATVVVSVD
RSIMAMSSAN LKDLDDPALD DNPMGKRVSA TMILRVLFAV LFAVLVGEAA NQVIFERDIT
AHMADVNEAR VAERQAGISA DYAAERANQE AKIAAADAAI ADYQSQIDAA QARAAGEAAG
TFGTMAAGCE EQCLLHLNQA SALIAGQATF NELRNGEIVD ARAELDTLDA AAASDLDEAR
VDIGNDDGLL SREEALWEML TADPWMLARY ALVSLLLLFV ELAAVLIKFA TRGNNYERAL
ARALRQEERA DRLRHGMLRN LARRRARDNE KALADADRAF YTSPARRTAT WG
//
