ID W5NI63_LEPOC Unreviewed; 760 AA.
AC W5NI63;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Poly [ADP-ribose] polymerase 12-like {ECO:0000313|Ensembl:ENSLOCP00000020322.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020322.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020322.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; AHAT01033545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NI63; -.
DR STRING; 7918.ENSLOCP00000020322; -.
DR Ensembl; ENSLOCT00000020356.1; ENSLOCP00000020322.1; ENSLOCG00000016450.1.
DR eggNOG; ENOG502QSC4; Eukaryota.
DR GeneTree; ENSGT00940000154649; -.
DR InParanoid; W5NI63; -.
DR OMA; GHCIHED; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000016450; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR45740; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR PANTHER; PTHR45740:SF15; ZINC FINGER CCCH TYPE DOMAIN CONTAINING 1-LIKE; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 81..106
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 137..169
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 285..312
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 371..457
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 488..701
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT ZN_FING 81..106
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 137..169
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 285..312
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 698..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 87250 MW; D11101835D975F7D CRC64;
MAASTITKIL CSNNGAMDYN ELVFNIGSGF SSSNTVLQKT LENNPNFLIV TSDGKRKIIA
KTKVRLCRAR ICDQDCNNLH LCKFFLYGDC KYNKGRRKCR FSHDMNSEQN AKVLKQNDLH
ELDRRELCQL LLQNDNSLLP PVCNSYNKGN GPYGNCTEQE SCTRLHVCEK YIRGTCLNCT
RFHNFDVAHP LKTLEERGLP KELISSVFSV YQNILSMKYD NNSKMPEKGP ENSSLIVLNE
RYTIMVLSLY TKLKCIKWLL VQYLNTDLSI TDWKKRMKGG NASLKDKTEI CMYYVWKDCK
HGDKCNRVHF NMPYKWEVWD GVGWSHLSDN EGIEKDFCDP IKLYSSGLDR VCFDTMTKGS
AKVRRLSTVS SVTQPSFVLT TEWAWYWEDE SGNWIQYASS DGIHGASSIT SEDLEKKYLE
DKNGVVEFTA GRQTYELSFQ DMIQTNKRYG TKRLVRRRPV FVSPSDAQLI RTRKKGLNKG
ISHDFKAVPS YWDKSSLLET GYKKILLQKS TAEYQKIENL FKKTMIGFTI SRLERIQNKS
LWEVFQWQKE QMKKNNARQN VNEKLLFHGT DTAYVDAICR QNFDWRICGT HGTAYGKGSY
FARDAKYSHS YTGSSATKTM FVSWVLVGQY AKGSSSYLRP PSKDGGDTIF YDSCVDNIYD
PSIFVVFEKH QIYPEYLVQY SEDIVQSDPL YTMYSYPNST AVPTPQPKPR PAPSSYRNQY
PKPTPAPSTY RNPYTYVSTS PSSISDSSTT TSSVYSFSTN
//
