ID A0A094JAK5_9PEZI Unreviewed; 1194 AA.
AC A0A094JAK5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=V501_07819 {ECO:0000313|EMBL:KFZ06008.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ06008.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ06008.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFZ06008.1}.
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DR EMBL; JPKD01002229; KFZ06008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094JAK5; -.
DR STRING; 1420914.A0A094JAK5; -.
DR HOGENOM; CLU_271487_0_0_1; -.
DR Proteomes; UP000029315; 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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd07997; WGR_PARP; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 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; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
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 InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_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; SSF51197; Clavaminate synthase-like; 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; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000029315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 275..400
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 411..456
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 496..589
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 694..790
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 826..951
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 961..1194
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 132830 MW; FA960FC6CAD28109 CRC64;
METFISRKRR RSSVSNEVPP RDPKCDLRGS TDFNEDESTD YKLSILISLH PDKDEGTLLE
TLLASEGSVE RALECLKLPP KKRPAASATS YQSSLSSITR TGKDGAAIKQ LTKRGKTVHL
YTPKDIEAHT PCSIIYNFLP SEEADALLQE LVDESPTYKT NTFQLFDRVV SSPHTFCLYV
DSWDDAEMQK TQYVYDGKNV EVSLLRLLCA IGLSQPLLSC PGHPTDGLQD VRRSLPRMRD
ASHKVRETVN QEITRRIRSS PTGQKLHHQS PHPWVPNTAF VNCYDGPRES VGYHSDHLTY
LGPRPVIGSL SLGVAREFRV RKIIATEDDD SGDSDAARKR ADAKADAQGQ LSIHLPHNSL
LVMHASMQEE WKHSIAPART ISPHPISGNK RINITYRHYK ANLHPRFTPK CGCGVPTVLR
VVQRQAGSRG KYMWMCYAGY VPGKEGCKFF EWAVFDEDGD PPWAEEAKGS EKQCFDAEEK
LPGEMHTMPP KKKAQPQPQP LIGCNIALSG TFSAGSHGVI QVQLAGLGAD LAGSIADSTT
HLVTVQRDYD KPSVKVKAAL EKNVQIINYD WVKECVASNS KVPEKNYLFT PLLVDVPSQS
NGLLKREPSA DISADENVKP PTKKQKSSND SKTVGKVDVK AKTAGKADVK VKTQTKLKAE
VKSETEAKSG RITDGQVAKS LDVKIPLDDG CNLSYDVYIH DDGIIYDASL NQANATANNN
KFYRVQVQRN RNGGDFKTWT RWGRVGEHGQ SAYLGSGTLE DAIRHFEKKF KDKSGLAWTD
RRKDPKPGKY AFIERNYFSD SDDDDEDDAK TNGVKNEPDD ELVIPESTLH PATQQLMELI
FNQQYFDATM SDLNYDANKL PLGKLSKATI TRGFQTLKDL AALLDDPTLA ASYDMNYNDA
TEHFSNLYYT VIPHAFGRNR PPIIRSTELL KKEIELLESL GDMKDAALIM KPKDRDAEQI
NLLDRQFQGL GIQEMTPLGP KSSEFGELKN YLLSTRGSTH NLNCKVEQIF RIEREGEKER
FEKGDFAGVA GDRRLLWHGS RCTNFAGILS QGLRIAPPEA PVSGYMFGKG IYLADMSSKS
ANYCCPYISG GHALLLLCEA ELGKPMQALT DASYSASEDA TSKGLLSTWG QGMTGPKAWK
DANCVNPSLD GILMPDTTIM PGATDVKDAY LMYNEYICYD VAQVRLRYLF RIKM
//
