ID A8NF82_COPC7 Unreviewed; 702 AA.
AC A8NF82;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 70.
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=CC1G_04200 {ECO:0000313|EMBL:EAU88494.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU88494.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU88494.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU88494.2}.
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DR EMBL; AACS02000002; EAU88494.2; -; Genomic_DNA.
DR RefSeq; XP_001833221.2; XM_001833169.2.
DR AlphaFoldDB; A8NF82; -.
DR STRING; 240176.A8NF82; -.
DR GeneID; 6009716; -.
DR KEGG; cci:CC1G_04200; -.
DR VEuPathDB; FungiDB:CC1G_04200; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_2_0_1; -.
DR InParanoid; A8NF82; -.
DR OMA; QGENDRF; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000001861; 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; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 2.20.140.10; WGR domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; PF16589; BRCT_2; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 3: Inferred from homology;
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:UP000001861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 33..102
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 210..309
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 344..473
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 482..702
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 96..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77809 MW; FB1CB10356A4E45D CRC64;
MRPSQDHRVQ YRLNGAFPTL PLLPVGRIEA TIKIEALVAD NGGTFSKTVD STTHLVSTEA
DVKKNSAKVK AANNAGTPIV TLEWLLDSIE GGKKEDETSY LLSSGPPPPP APSTRPKRKA
AAPAVATADD ADSDEPPAKK VKTTAAPKGN AKGKAKPRSK AKVVSEDEEM EDVEDEEEEE
KEPTPPPPKM KTVIRKGKAP VDELCPLAGS HHVYVDETGV AWDATLNQTD IGRNNNKFYY
CQLLERDNSP MTYAVFCRWG RVGDRGQSKM YAESVSLPAA KSVFDKQMKA KTGKSWAQRK
EALGGNKKYA YLERNYDDDD DDEEEETTPT SNKPGAEDSK PPPKPTIAPE LVRLMELIFN
SSFMQQTMAS MSYDSNKLPL GKLSKDTILR GFNLLKQIGE VIGDPANAVQ NFSEYGNSYQ
QILSQLSSRY YTVIPHNFGR SVPPVIGDQS MLKREAELVE NLIDMKISTE IMTASVKDSD
VHPVDKQFAS LGLNEAIPLD KTSSEYKYLE AYVKKTQGHT HYMKLQVEEI FRIRRDSEEA
RWKEKKWHEY ENDNRMLLWH GSRTTNFSGI LSQGLRIAPP EAPVSGYMFD KGIYLADIVS
KSANYCYPQI SANTGLLLLC EAQLGDPMYE SKGADYYAAT NSKKSGAIAT KGLGRTVPLE
WEDASIIHED LEGVQIPKVS SKKDNITGNS SDSGLYLQYN EF
//
