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Database: UniProt
Entry: A0A1Q5MGI4_9ACTN
LinkDB: A0A1Q5MGI4_9ACTN
Original site: A0A1Q5MGI4_9ACTN 
ID   A0A1Q5MGI4_9ACTN        Unreviewed;       720 AA.
AC   A0A1Q5MGI4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Kinase {ECO:0000313|EMBL:OKK13330.1};
GN   ORFNames=AMK33_00305 {ECO:0000313|EMBL:OKK13330.1};
OS   Streptomyces sp. CB02400.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKK13330.1, ECO:0000313|Proteomes:UP000185993};
RN   [1] {ECO:0000313|EMBL:OKK13330.1, ECO:0000313|Proteomes:UP000185993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02400 {ECO:0000313|EMBL:OKK13330.1,
RC   ECO:0000313|Proteomes:UP000185993};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC       {ECO:0000256|ARBA:ARBA00007476}.
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:OKK13330.1}.
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DR   EMBL; LIWB01000001; OKK13330.1; -; Genomic_DNA.
DR   RefSeq; WP_073930637.1; NZ_LIWB01000001.1.
DR   AlphaFoldDB; A0A1Q5MGI4; -.
DR   Proteomes; UP000185993; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OKK13330.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185993};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OKK13330.1}.
FT   DOMAIN          96..193
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          440..501
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          641..715
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  78037 MW;  73B8AFCE99C158DF CRC64;
     MNAEAVNPAT PGPVTSGHVT PTGSRRKSRP RLDLRRLGRA ALLGPAARDR LPDAIGHVVD
     AHRAHHPDAD LEPLRRAYLL AESSHRGQMR KSGEPYITHP LAVTLILAEL GAETTTLTAS
     LLHDTVEDTE VTLDQVGEQF GEEVRYLVDG VTKLEKVDYG AAAEPETFRK MLVATGNDVR
     VMSIKLADRL HNMRTLGVMR PEKQERIAKV TRDVLIPLAE RLGVQALKTE LEDLVFAILH
     PEEYGHTREL IVRNAARADD PLAEVADDVR KVLREADITA EVLIRPRHFV SVHRVSRRRG
     ALRGADFGRL LVLVNEDADC YGVLGELHTC MTPVVSEFKD FIAVPKFNLY QSLHTAVAGA
     DGQVVEVLIR THQMHKVAEA GVVALGNPYA APPEEQSASD GERVDPTRPG WLSRLLDWQR
     AAPDPDTFWS TLREDLAQDR EITVFRPDGG TLGLPEGATC VDAAYAQYGE DAHACIGARV
     NGRLATLSTV LKDGDTVQLL MGQDAASEPS REWLEHAHTP AARIAIQRWL TAHPAQDEAS
     GAVPEEAARP LTDDPAPSPA PDAPAPGRPT AAQVLADRAG ATVRLAGCCT PVPPDEVTGF
     AVRGGAVTVH RVECAGVERM KSAGRAEVGV RWGEGAECRV TLVAESFVRP HLLADLTEAM
     ALEGAEIVSA TVEPPDRQQV RHTYTVQLPD AAHLPVLMRA MRNVAGVYDV SRAQRQAPGV
//
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