ID A0A0V0VXI5_9BILA Unreviewed; 843 AA.
AC A0A0V0VXI5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE Short=PARP {ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN ORFNames=T09_8722 {ECO:0000313|EMBL:KRX68198.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX68198.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX68198.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX68198.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00033987};
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:KRX68198.1}.
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DR EMBL; JYDN01000002; KRX68198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VXI5; -.
DR STRING; 181606.A0A0V0VXI5; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 6.20.320.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 8.
DR PROSITE; PS50088; ANK_REPEAT; 9.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114}; NAD {ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 8..43
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 48..76
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 77..109
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 179..211
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 212..244
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 245..277
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 333..365
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 366..398
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 399..431
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 532..595
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 603..826
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 92645 MW; D93246B439BABCE2 CRC64;
MYFGHPYTGQ NALHVLCEAT HANCLSMVEA VISVGVSIDE RNKHLLGPLH VAADRDALEL
VELLLLRGAN INLFDGEGQT CLHRCAKKGL VAMCKLLLDH GIDASSVNLH GLTARQLAVG
MVVQVLEEHP TVVSRRARES LEHRLLEASK AGDLEMVKVV LNQSDDKQSL INCRDVEGRH
STPLHFAAGY NRLEVVKFLV QSGADIHAKD KGGLVPLHNA CSYGHYEVTE FLVQQGADVN
AADLWKFTPL HEAAAKGKFD ICKLLLANGA DKTRTNRDGH TPLDLIKDSE NDDVADLLRG
DSAILDAAKT GSLEKVKKLV TAENVSCRDG QGRNSTPLHL AAGYNNYDVA EYLISMGADV
NAQDKGGLIP LHNAASYGHL EIAHLLIQNK GDVNAQDLWG FTPLHEAAQK GRTHLVTLLL
NHGADPTIRN QENQIPLELA TADDVRVLLQ DAMPSTGRLD TVLIASPDEL LPVVSSFTAI
PSGENSTNAV DNFSTTFSSN SADQSTEKYP IKQQQQQNRA RDFLHQERDK PLAEMSVPLF
LKSIGLECLK DLFYKEQITL DVLVEMSHED LKAIGVSTYG MRHKLIRSIE KLTIGQPIGC
SMPGFPSTPV GFNGAVLVPL PADHLEFLAV EDEMQSTIVP HSDPAGAGGV FTKYNISKVQ
KVFNRRLWER YIRRRDDIAE ENSGQHNEKL LFHGSPFVNA IVQKGFDERH AYIGGMFGAG
IYFAEHSSKS NQYVYGIGGG TGCLPHKDKS CYVCHRQLLL CRVILGKSFG HTTAMKLAHA
PPGHHSIIGK PSGYGLTYPE YVIYRGEQVF HFSIMHVCLS DVYILQAYPE YLITYQIAPP
ENE
//
