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Database: UniProt
Entry: A0A0X3UZB0_9ACTN
LinkDB: A0A0X3UZB0_9ACTN
Original site: A0A0X3UZB0_9ACTN 
ID   A0A0X3UZB0_9ACTN        Unreviewed;       651 AA.
AC   A0A0X3UZB0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=ADL22_20520 {ECO:0000313|EMBL:KUL37840.1};
OS   Streptomyces sp. NRRL F-4489.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL37840.1, ECO:0000313|Proteomes:UP000053256};
RN   [1] {ECO:0000313|EMBL:KUL37840.1, ECO:0000313|Proteomes:UP000053256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL37840.1,
RC   ECO:0000313|Proteomes:UP000053256};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KUL37840.1}.
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DR   EMBL; LLZI01000232; KUL37840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3UZB0; -.
DR   STRING; 1609095.ADL22_20520; -.
DR   Proteomes; UP000053256; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 4.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KUL37840.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053256};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KUL37840.1};
KW   Transferase {ECO:0000313|EMBL:KUL37840.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          383..449
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          450..517
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          518..584
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          585..649
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          270..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  68163 MW;  C588D3F6C4635D58 CRC64;
     MLDGRYRVEG RIAAGGMATV YRAVDTRLDR VLALKVMHPS LAVDGAFVDR FIREAKSVAR
     LSHPNVVGVF DQGTDGTYVY LAMEYVAGCT LRDVLRERGA LRPRAALDIL EPILAALGAA
     HRAGLVHRDM KPENVLIGDD GRVKVADFGL VRAVDTHTTS STGSVLGTVS YLAPEQMEHG
     TADARVDVYA CGVVLYEMLT GGKPHTGGSA AQILYSHLHD DITPPSELVP GLAPELDALV
     AAAAARDPEE RPQDAVALLA SARAARARLT DEQLDLDPPQ ARPVSADDER TDVLPRPAGV
     QLALPGAEEG AGLDRTSRLE VPPAAAADAD GRTTRLRPPP DGPAAPAAPS GPGSRVRRRR
     LAAVLAAVLL VLGLGTGVWY INSGQFTRVP AVLDMPQAKA EQTLRGEGLR VKVTRGYSPN
     VRRGHVMATD PATGKRIRGN GTVTLIVSRG PETVTIPDLA GTPVADARRK LRDLGLVPGT
     ETRRFSDEVA KGSVISTDPA AGSTRHPDTA VALTVSRGAP VDVPDLTGKS RDDAANALRE
     AGLRVAFADQ PVFSPQDKDT VARQSPGAGA TLGTGDTVTL TLSKGPEMAT VPDVGGKSTA
     DATRALTAAG FKVKVDRPFL FPQDSVASQS VDAGEQAPKG STITIRLKGA L
//
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