ID   A0A2G5J5C9_9ACTN        Unreviewed;      1573 AA.
AC   A0A2G5J5C9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:PIB11972.1};
GN   ORFNames=B1C81_01875 {ECO:0000313|EMBL:PIB11972.1};
OS   Streptomyces sp. HG99.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1958787 {ECO:0000313|EMBL:PIB11972.1, ECO:0000313|Proteomes:UP000231274};
RN   [1] {ECO:0000313|EMBL:PIB11972.1, ECO:0000313|Proteomes:UP000231274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HG99 {ECO:0000313|EMBL:PIB11972.1,
RC   ECO:0000313|Proteomes:UP000231274};
RA   Li Y.;
RT   "Diversity and bioprospecting of biosynthetic gene clusters of culturable
RT   actinobacteria from Tibetan Plateau, China.";
RL   Submitted (FEB-2017) 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:PIB11972.1}.
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DR   EMBL; MVDM01000001; PIB11972.1; -; Genomic_DNA.
DR   Proteomes; UP000231274; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011528; NERD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   NCBIfam; NF033442; BREX_PglW; 1.
DR   PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF08378; NERD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50965; NERD; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:PIB11972.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231274};
KW   Transferase {ECO:0000313|EMBL:PIB11972.1}.
FT   DOMAIN          12..122
FT                   /note="NERD"
FT                   /evidence="ECO:0000259|PROSITE:PS50965"
FT   DOMAIN          200..497
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          546..834
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          505..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..891
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1573 AA;  172310 MW;  8EEF177C616A87A3 CRC64;
     MLDGRWTTVT ESGYEHERRG LEAIRKRLPD EEPWRAWSNF SFTANSGHVR EVDLLVVAPA
     GVFLVELKDW HGSVHGGGND WVQTTPNETT RRHGNPLHLS NQKAKELAGL VNGVAGRPGD
     RSRIWVGEAV CFTDDRLQVQ LPAADMNGVF TVKKLVEMLA VPPGDGRRRV TAETSRRVDA
     ALKQLRIAPI RRQHEVGSYL LDAKAFDSGP TWADYLGRHS QLQDLARVRV FLSERGASDE
     ERRSVERAAA REAAILSRFK HPGAIQLKTY LPSGHPAGPA ILFDYHPETL RLDDYLVQHG
     ELLDLQGRLA LVRQLAETVR SAHSRRIHHR TLSAHSVHVI PRDRGPRGRE LGEEQRWLRP
     WPQIADWQIA TGQSVSRGRP LTLAPTNVSG VHVSGQADPY LAPELRIPKA DPVRLDVYGL
     GVLTYLLVTG QAPGASQSEV MARLEGGETL RPSALVDGLH PDVDDLVEAS TAYEPGRRLS
     TVDDFLEMLE YVEQAFVEEI ADSSDAAAGA GGDGNGGSAA SDGEEQAKPE KDPLEAVAGD
     VLGRRWEVVR RLGTGSTSRA FLVRDLEGEP RRSGALPVAV LKVALSEAKH TVLDREADVL
     GRIHRDSSII ALYEREPLTL AGRRVLVLDY VGDSRELKDQ DASADKGPRR REDTVARQLR
     DNGRLGMDQL EAYGKYLFGA VEHLEAEGIW HRDLKPDNIA IRIRPNGTRQ LVLIDFSLAG
     YPAKEIEAGT EGYLDPFVGI ITRGSYDGHA ERYALAVTLH EMAANELPRW GDGSVTPRQT
     DAKEWPFPQL AADAFEPAVR DGLVAFFRKA LARDVKDRFS DLKPMERAWQ RIFLDAQRTT
     APSSGHSEKP SRGAKGGADA VAQPATEPRI GREDDDVSAE QVRDQQAERA DRKTPLSVAG
     LTVSAQSQLF AMGLNNVGDV LEYSAKKFLT APGMGSRTRE EIQRRQKEWN VRLGKAAPSP
     LSAAALKAAN QERTALERAA ADAIAAAGVD VTAPQVLSGL SLDALAARLV PRPSGGNARS
     NAKEREAVRL LLRLPDDEGR LPGGLAWVRQ RDVAEAVGLT AGRIPQIVKK ARERWYEDAA
     LGLLRDELVE LLAERGRVAP VIELADALIV RRGTQHVERR DRRALALSLL RALVERESRA
     LVERESGDDE SPQLFRYFHA RMPKGADPVI GLLALDVREG VDGPDTPSLP ALQEYALNLG
     ARADRLAALE SLPTASTVLT ELDAVRRPLG SLGWDERRTA EIAVAASTRA ALTPRLEIYP
     RDLDLVRALR ITQAGVVAVQ PGVEEDRLPG LTVDALHKRV ATRFPDLGTD PLVPRELPTG
     SALVRALKEA GFELKLATRY DKVLRLVPDR RSGDATAGLT SASWGASAAR RSAPTQYDAD
     AAVAAAVKAN QRLTHSARQD GFRVLTVPQR RAEDAVRWLT GEPFGARPVS LTGLFVDELR
     SVVGEAARPT WETVLKADAA EPGSRPHQQL RIRTDKAWGR IEPQLRERLA EARGPLLLTD
     TAVLARYDAL DLLGRLTEEA RQGGNPLWLL VAQSDPARAP RLAGQSVPYQ AGFDEWIVVP
     DAWVARKHLA LDA
//