ID A0A165Q9B3_EXIGL Unreviewed; 626 AA.
AC A0A165Q9B3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=EXIGLDRAFT_759147 {ECO:0000313|EMBL:KZW03275.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03275.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW03275.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03275.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425884; KZW03275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165Q9B3; -.
DR STRING; 1314781.A0A165Q9B3; -.
DR InParanoid; A0A165Q9B3; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000077266; 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 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; 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:UP000077266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 112..209
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 239..376
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 384..626
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 68824 MW; D3A367BD999351E5 CRC64;
MPPRRAAAAK AAAANKPASK SKKPASTAKP KSKGKRKRDE VSDAEEDGDD NADEDKADDD
ADAATDGPGP SKKVKKGTAP VDKFSGMDSA FKLDRGGARN VLLKFVVMDL GTHKVYVGKD
GEIYDATLNQ TNIGNNNNKF YCLQLLHPEK SSATCVLFTR WGRVGENGAS QTKGPFPAEV
AVKEFQKQFK NKACCHLDAR TAKPKEEKYT WIDMQYDDEE DESAKADGGA AKPREKTPDS
VLDKPVKDII DFIFNENYIS QHLGSFNYDA NKLPLGKLSK DTVANGYSVL KEIAEALENK
DSGTDAASGS SGPKRGAAKK KAGNVFVELT NRYYSIIPHA FGRSKPTVID TQDLLKQEVD
LVGTLAELEE TSGIMSGHVS KKEHPTDANL HSLELDEIAP VDVETDEFKA LEAYCKETYA
YGNYGQKMTL ENMFRIERRG ERQRWLEGGW DDLPNAEDGT SPRLLLFHGS RSSNFGGILK
NGLKIAPPEA PHNGYLQRTT SDTLLDMLKL SAGYTYSGLS DNVGLVLLCE VAAKPYLHRI
KNTQFAADEC KAAKKTLFKT EATDHAEWVD AGKATGNSKI DGVLMPDVSN IQERAKSEPW
WSDNMYVAYD VSQVRLRYLL KMKFGS
//
