ID A0A061DQM5_THECC Unreviewed; 560 AA.
AC A0A061DQM5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=TCM_004671 {ECO:0000313|EMBL:EOX95109.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX95109.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX95109.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: Involved in the base excision repair (BER) pathway, by
CC catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor
CC proteins involved in chromatin architecture and in DNA metabolism. This
CC modification follows DNA damages and appears as an obligatory step in a
CC detection/signaling pathway leading to the reparation of DNA strand
CC breaks. {ECO:0000256|ARBA:ARBA00024945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000256|ARBA:ARBA00000438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000256|ARBA:ARBA00000459};
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; CM001879; EOX95109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DQM5; -.
DR EnsemblPlants; EOX95109; EOX95109; TCM_004671.
DR Gramene; EOX95109; EOX95109; TCM_004671.
DR Proteomes; UP000026915; Chromosome 1.
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; cd08002; WGR_PARP3_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 2.20.140.10; WGR 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; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_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; PF02037; SAP; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50800; SAP; 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:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 58..92
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 139..236
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 266..384
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 392..560
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 64544 MW; 51578679EA99B1B2 CRC64;
MVQRLEEALL KEKKKEEENK ENDANNAIEN NKKRRGSESN HNNNDDEDSK KIKAVEEFRE
MNVKQLREQA TLRGLSTVGT RKELIERLCE DAEKNSLDEV FKEEEEKEKD SGKEEKIVTA
TKKGAAVLDQ GIPDHTKAHY HVLQQGDNIY DAMLNQTNVG HNNNKFYVIQ LLESDDWKTY
MVYNRWGRVG VKGQTKLHGP FTSQQAAIVE FESKFFNKTN NYWSNRKDFV CYPRCYAWLE
MDYDEKEKES DLEEKTGSSV GAQLRETKLE QRIAKFISLI CNISMMKQQM MEIGYNADKL
PLGKLSKSTI LRGYDVLKRI ADVIGQSNRS KLEQLSSEFY TVIPHDFGFK KMRDFVIDTP
QKLKKKLEMV EALGEIEVAT KLLTDDTMME EDPLHYHYQQ LHCELIPLDD DSEEFAMIAK
YSRNTHAKTH SQYTVDIVQI FKVAREGEIE CFKKFSATKN RMLLWHGSRL TNWTGILSQG
LRIAPPEAPV TGYMFGKGVY FADMFSKSAN YCYTSSSFTT GVLLLCEVAL GDMAELLQAK
SDADKLPDGK LRFVKFYVND
//
