ID C5KAW0_PERM5 Unreviewed; 555 AA.
AC C5KAW0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Pmar_PMAR005192 {ECO:0000313|EMBL:EER18286.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER18286.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG671811; EER18286.1; -; Genomic_DNA.
DR RefSeq; XP_002786490.1; XM_002786444.1.
DR AlphaFoldDB; C5KAW0; -.
DR EnsemblProtists; EER18286; EER18286; Pmar_PMAR005192.
DR GeneID; 9048940; -.
DR InParanoid; C5KAW0; -.
DR OMA; KTENAWP; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd07997; WGR_PARP; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
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:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 34..140
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 171..301
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 309..552
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 61760 MW; FEA0907AFE5F6A22 CRC64;
MMITVVGKKR RLPPEEGSPA LEVDEDVDAA VGRDAQVYVD NANNVYHVMC TKTDTSTNVN
KFYKIQVLVH GSSRNRYAVL RKWGRVGGSD SKANDAMTVR CGSGKAARQE AIDTFLTKFT
ELTGTDWRER DSFEQRPGRY NMVEIMGTTS DSSKRRTTQA VAEEHDKAGV LCTLVPAVRS
FVSLIFDEKV IEEHMSKVLH IDMRKMPLGA LSAAQLRRGL EVLSELSSLL RLDEATKRAT
HGFDLRIRDA TNRFYSLVPH TISKSTAAAA KAKLNTLKKV EKAVDDVTDL LSIVDFTDAR
DRAATGHGHV LDRQFDALGV TLDVVPTESP TFDVIKECMV TTHAPTHDGY SLEIVSLLEV
RREEEWARFD SYPVCSHNRR LLWHGSRLTN WVSILSKGLK IAPKEAPVTG YMFGKGLYFA
DCSSKSANYC FANKESPYGV LVLCEVALGD QYKRVAAEYE AKKSCRKAKA HSTWGMGKSA
PDAARETKLP SSSEVSVPMG PLIDATELVN VEADIEGEAA SLLYNEFIVY NTAQVRMRYI
LHVKFNFNET TGGYW
//
