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Database: UniProt
Entry: A0A1C6PYP1_9ACTN
LinkDB: A0A1C6PYP1_9ACTN
Original site: A0A1C6PYP1_9ACTN 
ID   A0A1C6PYP1_9ACTN        Unreviewed;       733 AA.
AC   A0A1C6PYP1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SCK48474.1};
GN   ORFNames=H181DRAFT_04354 {ECO:0000313|EMBL:SCK48474.1};
OS   Streptomyces sp. WMMB 714.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1286822 {ECO:0000313|EMBL:SCK48474.1, ECO:0000313|Proteomes:UP000182206};
RN   [1] {ECO:0000313|Proteomes:UP000182206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMB 714 {ECO:0000313|Proteomes:UP000182206};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC       {ECO:0000256|ARBA:ARBA00007476}.
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DR   EMBL; FMHJ01000012; SCK48474.1; -; Genomic_DNA.
DR   RefSeq; WP_045866225.1; NZ_FMHJ01000012.1.
DR   AlphaFoldDB; A0A1C6PYP1; -.
DR   STRING; 1286822.GCA_000964305_04331; -.
DR   Proteomes; UP000182206; 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:SCK48474.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182206};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SCK48474.1}.
FT   DOMAIN          67..164
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          405..474
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          654..728
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  78659 MW;  13DAC4CB7669543C CRC64;
     MRSLRRLSHA ALLGQGPRRD GLPDAMEHVA KVHRAHHPEA DLAALRRAYV LAESSHRGQM
     RKSGDPYITH PLAVTLLLAQ LGAETTTLTA SLLHDTVEDT DVTLNQVREE FGEEVSYLVD
     GVTKLEKVDY GAAAEPETFR KMLVATGNDV RVMSIKLADR LHNMRTLGVM RPEKQVRIAK
     VTRDVLIPLA ERLGVQALKT ELEDLVFAIL HPEEHALARE LIAEHAKEPD PLTGMATSVR
     RVLREAGIIA QVLIRPRHTV SVHRLRQKRG ELGPCDFGRL LIMVEEDADC YAVLGELHTC
     FTPIVAEFKD FIAAPKFNLY QSLHTAIADE EGRVAEVLVR TRQMHRVAEA GVIALGDPHG
     VPSGGDGSDT EPGPGWLSRL LKWQSHATDT ETFWTELRDE LAQDREITVY CASPGAAPAP
     SGGALPLPAG ATCVDAAYAR YGEAAHRCIG ARVNGRLTAL STVLRDGDAL QLFLEPAASA
     PSGPSPEWLD HARTPAARIA IRHWLAAHPV AAEAEPKQEL TSVGATGNGG GHARQAGDGG
     SRAVAPCSTA APVSPPDPAD PGGRSSREDS TGPSPDSGRA TETASVVAED PHAVVRLARC
     CTPVPPDSVT GFAVRGGAVT VHRESCQTVT RMASTGRRPV PVSWRQGAAG CRVTLRAEAL
     GRPHLLADLT EIIAAQGAAV VAADVEPPRE QRVLHTYTLQ LPDAAGLPDL MRAMRRVPGV
     YDVTRASRPL PAR
//
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