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Database: UniProt
Entry: A0A443Q8C5_9ACAR
LinkDB: A0A443Q8C5_9ACAR
Original site: A0A443Q8C5_9ACAR 
ID   A0A443Q8C5_9ACAR        Unreviewed;       575 AA.
AC   A0A443Q8C5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=NAD(+) ADP-ribosyltransferase {ECO:0000256|ARBA:ARBA00012020};
DE            EC=2.4.2.30 {ECO:0000256|ARBA:ARBA00012020};
DE   Flags: Fragment;
GN   ORFNames=B4U79_09772 {ECO:0000313|EMBL:RWR99228.1};
OS   Dinothrombium tinctorium.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombidioidea; Trombidiidae; Dinothrombium.
OX   NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWR99228.1, ECO:0000313|Proteomes:UP000285301};
RN   [1] {ECO:0000313|EMBL:RWR99228.1, ECO:0000313|Proteomes:UP000285301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWR99228.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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:RWR99228.1}.
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DR   EMBL; NCKU01016289; RWR99228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443Q8C5; -.
DR   STRING; 1965070.A0A443Q8C5; -.
DR   Proteomes; UP000285301; Unassembled WGS sequence.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd17747; BRCT_PARP1; 1.
DR   CDD; cd08001; WGR_PARP1_like; 1.
DR   Gene3D; 3.90.640.80; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR049296; PARP1-like_PADR1_N.
DR   InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
DR   InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR   InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR   InterPro; IPR036930; WGR_dom_sf.
DR   InterPro; IPR008893; WGR_domain.
DR   PANTHER; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF112; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF21728; PADR1_N; 1.
DR   Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   SMART; SM01335; PADR1; 1.
DR   SMART; SM00773; WGR; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF142921; WGR domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS52007; PADR1; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51977; WGR; 1.
PE   3: Inferred from homology;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          137..210
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          305..405
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          426..544
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   NON_TER         575
FT                   /evidence="ECO:0000313|EMBL:RWR99228.1"
SQ   SEQUENCE   575 AA;  65096 MW;  7B392C45E234FBDF CRC64;
     MKRTDIVRLL EYNNQHVPES NSSKYERLAD CMVFGALEKC PECKNGQLVF RIAGYICTGH
     ISEWTTCLYQ TQTPARKSFK IPEDIRDSYD FLSTYEFKEH KRVYNKVEAP TSAVNHIERA
     MQPSTSSTSA IENGTDVAKL PLKGHKVAYV GKMKLSKRAL KEKILSLGGK LVDEIDRTVL
     FIISTQKEVE KEGAKIAKAK TCGVTVVSED VFDALNEKVD ICDLIKRNTI SPWGGDVSKK
     HKTLVDKDKL KSGSGEPILC TDTGLTFSFL GMKSGSGSSK SEPKIQSFKM KAGLVVDPDS
     GLDHVAHVYK DHNGPYSVVL AKVDIVSNKN SYYKIQLLES DEAKKKHQYW VYRAWGRIGT
     DIGGDKLEKF KLKSNAIDNF CEVFLEHTGN EWKKKKEFKK LPGRYHIVET HYGNSLDDDK
     KLVVGNSCLP LPVQDLITMI FDISRMKHQM QEFHLDLAKM PLGKISKDQV MSAYAVLNEI
     SCMIETNEKS LTKMLDASNR FYSLIPHDFG TDNVIVIKNK ELLQEKLEML DSLLEMELAF
     ELVSDIKEEG EDVLKQHYDR LDANIEVLDK NSEEF
//
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