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Database: UniProt
Entry: M2V3N5_COCH5
LinkDB: M2V3N5_COCH5
Original site: M2V3N5_COCH5 
ID   M2V3N5_COCH5            Unreviewed;       656 AA.
AC   M2V3N5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=COCHEDRAFT_1191475 {ECO:0000313|EMBL:EMD94638.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD94638.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD94638.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR   EMBL; KB445571; EMD94638.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2V3N5; -.
DR   STRING; 701091.M2V3N5; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   HOGENOM; CLU_004841_2_0_1; -.
DR   OMA; QGENDRF; -.
DR   Proteomes; UP000016936; 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; PF00533; BRCT; 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:UP000016936};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          12..105
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          166..260
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          294..413
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          423..656
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  71786 MW;  4D2748825633CA8D CRC64;
     MPRKAATKAT PQAAPPLDGC SVATSGRFPG TSQSALQSRL TSLGATIASS VTANTTHLIA
     TEKDYESNST KTKAAAAHNV PVVTIEWLDE CESKGSKVDE TQYLLSSGTA PAQKNGSNKR
     PASTTPPAPS QEKKPKIKED AKVGDGQNAK SKTIAISIDE HCPLANYQVY IDSNGTIYDA
     SLNQTNAGAN NSKLYKCQLL VNGTDYKTWT RWGRVGERGQ SAVLGSGSLL EAMREFEKKF
     KDKSGLKWEN RSAEPKSGKY AYVERSYNPD SDDEDEDDTG AGADDEKKDV KPAECTLDKP
     TQDLMKLIFN QDYFDATMSA LNYDANKLPL GKLSKGTIAR GFQALKELSV ILDNTDAASR
     AEVERLSNHY FSVIPHAFGR NRPPVIRDND ALKKEIELLE SLSDMKETAA MLKSQLKDDS
     GIHKLDKQFQ GLGMEEMTPL DHKSQEFVEI DQYLNCSKGK THAVNYQVQD IFRIERKGEF
     ERFDKSKFSK ISSNRRLLWH GSRVTNFGGI LSQGLRIAPP EAPVSGYMFG KGIYLADMSS
     KSANYCASYN SGGTALLLLC EAELGNPMHQ LTHASYTAGE DAVKNGMYST WGMGSTGPSK
     WKDASCINPA LKGCTMPDVS TPAGKTNVSG ATLLYNEYIA YDVAQVKLRY LLRVRM
//
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