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Database: UniProt
Entry: I0REK3_MYCXE
LinkDB: I0REK3_MYCXE
Original site: I0REK3_MYCXE 
ID   I0REK3_MYCXE            Unreviewed;       752 AA.
AC   I0REK3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=MXEN_20265 {ECO:0000313|EMBL:EID09556.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID09556.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID09556.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID09556.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
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:EID09556.1}.
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DR   EMBL; AJFI01000108; EID09556.1; -; Genomic_DNA.
DR   RefSeq; WP_003923071.1; NZ_AJFI01000108.1.
DR   AlphaFoldDB; I0REK3; -.
DR   PATRIC; fig|1150591.3.peg.4073; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000003584; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EID09556.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003584};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          153..395
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  82676 MW;  DE4D806DD59BB7DA CRC64;
     MAEPRDRGRE EQGLHDEGPG TQPADSASMR RAMSTRAIFR PEFDDSERTS VPTVDIEPPQ
     RLPTTATRTV PPVRKLGGGL VEVPRVPYTD PLEALMQNPV VPESRRFCWN CGRPVGRSGP
     DGRAASEGWC PYCGSPYSFL PQLNPGDIVA GQYEVKGCIA HGGLGWVYLA FDKNVNDRPV
     VLKGLVHSGD AEAQKMAMAE RQFLAEVVHP SIVQIFNFVQ HPDRHGEPVG YIVMEYVGGQ
     SLKRAKGEKL PVAEAIAYIL EILPALGYLH SIGLVYNDLK PENIMLTEEQ LKLIDLGAVS
     RINSFGYLYG TPGYQAPEIV RTGPTVATDI YTVGRTLAAL TLNLPTRNGR YVEGLPDDDP
     VLAKYDSFAR LLRRAIDPDP RRRFVSAEEM SGQLMGVLRE VVAQDTGVPR PGLSTIFSRS
     RSTFGVDLLV AHTDVYLDGQ VHSEKLTAKE IVTALQVPLV DPADVAAPLL QATVLSQPVQ
     TLDSLRAFRH GSLDDEGIDL SESVELPLME VRALLDLGDV GNATRKLDDL AERVGWRWRL
     VWYRAVSELL TGDYDSAIQH FTEVLDTFPG ELAPKMALAA THELAGTGEQ EKFYRTVWQT
     DNGVISAAFG LARALLATGD RAGAVRTLDE VPATSRHFTT ARLTSAVTLL SARSRKEITE
     EEIRDAARRV EALPPTEPRV LQIRALVLGT AMDWLENHEA STNHILGYPF TRHGLRLGVE
     ASLRSLARVA PTQAHRYTLV DMANRVRPTS TF
//
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