ID A0A0V1DER2_TRIBR Unreviewed; 1185 AA.
AC A0A0V1DER2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN Name=TNKS {ECO:0000313|EMBL:KRY60039.1};
GN ORFNames=T03_3435 {ECO:0000313|EMBL:KRY60039.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY60039.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY60039.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY60039.1};
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 -!- 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:KRY60039.1}.
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DR EMBL; JYDI01000008; KRY60039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DER2; -.
DR STRING; 45882.A0A0V1DER2; -.
DR Proteomes; UP000054653; 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; 5.
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; PTHR24178:SF45; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 5.
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; 19.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 14.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 62..94
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 95..127
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 128..160
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 215..247
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 248..280
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 281..313
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 368..403
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 408..436
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 437..469
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 539..571
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 572..604
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 605..637
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 693..725
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 726..758
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 759..791
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 892..955
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 963..1185
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY60039.1"
SQ SEQUENCE 1185 AA; 129511 MW; 372C029F9BD984B1 CRC64;
LLGKMSCRIN RGQRPKISLS AVGRVISDSN RDLFEACRDG DLGRVKKLVN AKNLNCHDTV
GRKSTPLHFA AGFGRKDVVE ILLLAGANTE VRDEGGLVPL HNACSFGHAA VTKMLIKNGA
DPNAVDHWGY TPLHEAALKG KVDVCIVLLQ NGANPLVQNL DGKTPLDIAD SVVKEVLTGE
YRKEELLEAA RNGNEEVLLS LVTPLSVNIH ANDGRKSTPL HLAAGYNRTQ IVQLLLQFFA
DVHVQDKGGL VPLHNACSYG HLEVTELLIK HGANVNATDL WQFTPLHEAA IKGRTEVCIC
LLAHGANPTV KNSNGKTPID LAPTVEMREL LTKEYQGHSL LNACTSGDIN KFRTFLSSET
ASFRHPYTGQ 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 EYLINMGADV
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 YVIYRGEQAY PEYLITYQIA PPENE
//
