ID A0A398AJZ4_BRACM Unreviewed; 614 AA.
AC A0A398AJZ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BRARA_B02605 {ECO:0000313|EMBL:RID75566.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID75566.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID75566.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM010629; RID75566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398AJZ4; -.
DR Proteomes; UP000264353; Chromosome a2.
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 GO; GO:0006950; P:response to stress; IEA:UniProt.
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; 2.
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:SF109; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF02037; SAP; 2.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00513; SAP; 2.
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; 2.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50800; SAP; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 2..36
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 71..105
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 137..234
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 264..382
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 390..614
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 69875 MW; BFD40B44DD01313A CRC64;
MAKKLKVNEL RAKLAERGLV TTGLKAVLVE RLEEAIAQDA KKVKSKSRRK RNRDSSDSTH
DSNKLIAVGE FRAMNVKELR KEASKRGLAT TGTKKEVLER LCNDETQDDK NGLEEEKSTK
KGAAVLDQWI PDHVKSEYHV LQRGDDVYDA MLNQTNVRDN SNKFFVLQVL ESDNRKTYMV
HFRWGRVGVK GQSKLDGPYN SCDPAMEIFS NKFYDKTRNH WSDRKEFILH PKSYAWLEVD
YGKEENDSVV NDIPESSSKV TRDESKLDPQ VAKFISLICS VSMMAQQMME LGYNAKELPL
GKLSKSTISK GYEVLQRISE MIERYDRARL EELSGEFYTV IPHDFGFKKM CQFVIDTPQK
LKQKIEMVEA LGEIEFATKL LSIDQGLQDD PLYYHYQQLN CELTPVGADS EEFSMVAKYM
ENTHAKADSG YTVEMIQLFR ASRAVEADRF QQFSSSKNRM LLWHGSRLTN WVGILSQGLR
IAPREAPVTG YRFGKGVYFA DMFSKSANYC YANSGSNDGV LLLCEVALGD ENELIYPDYE
ADNLPTGKLS TKGVGKTAPN GSEAKTLEEG VVVPLGKPED HSSTMGMLLY NEYIVYNTEQ
IKMRYVIQVK FNYK
//
