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Database: UniProt
Entry: A0A1Q4YIJ4_9ACTN
LinkDB: A0A1Q4YIJ4_9ACTN
Original site: A0A1Q4YIJ4_9ACTN 
ID   A0A1Q4YIJ4_9ACTN        Unreviewed;      1013 AA.
AC   A0A1Q4YIJ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=PLD phosphodiesterase domain-containing protein {ECO:0000259|PROSITE:PS50035};
GN   ORFNames=A6A29_19240 {ECO:0000313|EMBL:OKI34399.1};
OS   Streptomyces sp. TSRI0281.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI34399.1, ECO:0000313|Proteomes:UP000186952};
RN   [1] {ECO:0000313|EMBL:OKI34399.1, ECO:0000313|Proteomes:UP000186952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI34399.1,
RC   ECO:0000313|Proteomes:UP000186952};
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   -!- 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:OKI34399.1}.
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DR   EMBL; LWLE01000035; OKI34399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4YIJ4; -.
DR   STRING; 1718998.A6A29_19240; -.
DR   Proteomes; UP000186952; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09126; PLDc_C_DEXD_like; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR043764; DUF5710.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF18974; DUF5710; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186952}.
FT   DOMAIN          873..900
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          126..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..434
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        923..947
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  111309 MW;  C643D39E92D53580 CRC64;
     MDELLRAAQL EIAAELRSDG GNKPKASLRE GRRLSVSGPQ HEYEFSFKRW PEALNGMPLL
     VRPSRSQGPW TPAEVTRLPD NKVRFVTEAD LGHAPGQVQL RADESQTWKV LAERLASVGE
     ADHPVRPESA GWITGQGSPK VGREADPGRW VADWPSLRLN PPQRQAVEQA LASEVTFLWG
     PPGTGKTDVV AHIVEGCSRQ GLNVLFLAPT KVAVDQALER ICDLLSGEQG FDTGLVQRAG
     GIDVESLRER YGAYVDPEQV AARLSAHLQS ELTQLTSALT TVRSGIALHE RLRSLHEDLV
     AARAAYGSAG AARQKAGQAS SDALEIADAM GARIRRIGTP SGFFADQKQA KLDAARTDLW
     KASQQALEAN EARDAAKTAQ DKAARDISRI GTDITDQNAK LEGVEPLRTL TERTDVLQKQ
     INAAEKELRR ISDAVRANCR VLGATVAKAA QSRSLLERTD VVVIDEAGMI NLPMAWYVAG
     LAGKRVVVAG DFRQLPAVNK AADDRGASEE DKAHARQWSA TDAFRAAGLV TAAGTVRQDP
     RLVALSTQYR MREPICDLVN AVAYPDAPLR TGRDNESRIP FSPLVNAPVI LIDTSGHCVP
     GPNHRTNPVH QAAVHELVRG LQYDGVLPPR KWENVPPGER ATDRLAVIAP YKDQVKGLKR
     VLTERLGADY DGLVESVHRF QGSQRPVVIL DTVAGAGDYP GHFYRGTGLD SETCRLLNVA
     LSRAQDHLVV IADVAFLRKK LPQRSEARTM LDHLESRAQS ISVDQLIPIR SAAELAALPD
     EELTRPAFFP AEQVDRAVHW DIERARESID IYTFLLAVPR VKRWLALLEE KAAAGVRVVI
     HTRSPEEQRE DSVVERHRGL VDQLKEAGCT VEYRERMHEK VFIVDGTVLW HGSLNLLGNL
     GPTDLMMRLE DADSCAQARR VMDQARRESP VYRGGGRPHR DSGSSRKGNP KAAEGVEVGA
     TVWGRLYLNV SYQEKDEAKR LVSARFDGDN KLWYTDAAQV IPQGKQGWLR PKH
//
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