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Database: UniProt
Entry: A0A1Q5DGG8_9ACTN
LinkDB: A0A1Q5DGG8_9ACTN
Original site: A0A1Q5DGG8_9ACTN 
ID   A0A1Q5DGG8_9ACTN        Unreviewed;      1112 AA.
AC   A0A1Q5DGG8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Sporulation protein {ECO:0000313|EMBL:OKI94845.1};
GN   ORFNames=AMK18_28655 {ECO:0000313|EMBL:OKI94845.1};
OS   Streptomyces sp. CB01249.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI94845.1, ECO:0000313|Proteomes:UP000186839};
RN   [1] {ECO:0000313|EMBL:OKI94845.1, ECO:0000313|Proteomes:UP000186839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01249 {ECO:0000313|EMBL:OKI94845.1,
RC   ECO:0000313|Proteomes:UP000186839};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC       {ECO:0000256|ARBA:ARBA00010378}.
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:OKI94845.1}.
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DR   EMBL; LISW01000008; OKI94845.1; -; Genomic_DNA.
DR   RefSeq; WP_073865116.1; NZ_LISW01000008.1.
DR   AlphaFoldDB; A0A1Q5DGG8; -.
DR   OrthoDB; 9806903at2; -.
DR   Proteomes; UP000186839; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR43392; AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43392:SF2; AAA-TYPE ATPASE FAMILY PROTEIN _ ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17866; AAA_lid_6; 2.
DR   Pfam; PF13229; Beta_helix; 2.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00710; PbH1; 11.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186839}.
FT   DOMAIN          596..737
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          878..1018
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          525..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1112 AA;  116360 MW;  B20FC00FC4B40117 CRC64;
     MRQVLTICPE GTGDARTIAE ALARARGGAV LSVRPGTYEE NLVVTTRVTI VAEQSRGSVR
     LAPRTGTVIS LRADALMLTD LVVQGQDEEA PVVDASHGQV AMQSCDVSGA SWATVLARNS
     GSLAMRECRV SSRTGAGVVV TSGSESSLES CTFEHLGTSG VVIGERGRAT VRGCTVRDAR
     GNGLLANGDA QVSVEDCDLS STDKPALALE ERSAVRVLRT VIHDTAIGAH LTSAARVELD
     DVRVNGTTGQ GIVVSHGADP VLRRCRTSRT AGNGLFVTDR SRGTYEDCWL SGAQAPALRV
     AGSSSPTLTS LTVRDGEAEA VLLEEDSAAE LDRVEILDVR GTGVVVRGGA NPLVRRARIT
     GTGGTGVSVT DGGRGRVEDC SVESPGGAGV TVASGGNVYL AGLQVTGPGG AGLEIGGEGT
     AALRDGELVS AGGCGVVVDS GGELTATRVR AAAATDYGFL VREGGRANLN GCEAAGNGRD
     GIRVETESPV SVVGCTVREN KGGGLVQSRA SGRLAVENLN STGNEARDAW GYGEAEGTDP
     AGTVPESDGP GRPDGPMAAL ENLIGLDNVK EQVRTLVNLT QLARRRAQLG MSAPPMSRHL
     VFAGPPGTGK TTVARLYGTI LAELGTLRSG HLVEVSRADL VAQVIGGTAI KTTETFERAL
     GGVLFIDEAY ALTSDSRGSG ADFGREAVDT LLKLMEDHRD DVVVVVAGYS GEMRGFLGSN
     PGLASRFSRT VEFENYSVPE LVEIVESMCG RHQYVLNDET RTALAAHFDR IPKDAGFGNG
     RAARQVFEEM VDRQAVRLAS LAQVTEEDLT LLLPQDISEE AARHSEAGPD GADAGDDALS
     RLDALVGLSA VKRDVTDLVN LVSTARQRAA AGLPVPRLSH HLVFTGPPGT GKTTVARLYG
     ELLVSLGVLP RGQLVEVSRA DMVGRYVGHT AQLTKEVFER ALGGVLFIDE AYTLTPREAS
     GADFGREAVD TLLKLMEDHR DQVVVIVAGY TSEMEGFLAS NPGLHSRFSR KIEFADYSSD
     ELVTIVRQHA LLAGYECGTG LGSVLRHHFD TLPRDRSFGN ARTARQVLER MMTRQAGRLS
     RVAAPSLDDL RLLLPEDLAD PVSASASGGA GA
//
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