ID   A0A9B0TSW7_CHRAS        Unreviewed;      1801 AA.
AC   A0A9B0TSW7;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   02-APR-2025, entry version 12.
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   Name=PARP14 {ECO:0000313|RefSeq:XP_006869486.1};
OS   Chrysochloris asiatica (Cape golden mole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Chrysochloridae; Chrysochlorinae; Chrysochloris.
OX   NCBI_TaxID=185453 {ECO:0000313|Proteomes:UP000504623, ECO:0000313|RefSeq:XP_006869486.1};
RN   [1] {ECO:0000313|RefSeq:XP_006869486.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_006869486.1};
RG   RefSeq;
RL   Submitted (DEC-2024) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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   RefSeq; XP_006869486.1; XM_006869424.1.
DR   GeneID; 102830749; -.
DR   CTD; 54625; -.
DR   OrthoDB; 6133115at2759; -.
DR   Proteomes; UP000504623; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+-protein poly-ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:TreeGrafter.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:TreeGrafter.
DR   GO; GO:0070212; P:protein poly-ADP-ribosylation; IEA:TreeGrafter.
DR   CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR   CDD; cd02903; Macro_BAL-like; 2.
DR   CDD; cd12300; RRM1_PAR14; 1.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   FunFam; 3.40.220.10:FF:000010; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 3.90.228.10:FF:000008; Poly [ADP-ribose] polymerase; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 3.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR052056; Mono-ARTD/PARP.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR054596; PARP14_WWE.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004170; WWE_dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14453:SF89; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP14; 1.
DR   Pfam; PF23084; KH_PARP14_1; 1.
DR   Pfam; PF23248; KH_PARP14_2; 1.
DR   Pfam; PF23249; KH_PARP14_3; 1.
DR   Pfam; PF23251; KH_PARP14_4; 1.
DR   Pfam; PF23252; KH_PARP14_5; 1.
DR   Pfam; PF23253; KH_PARP14_6; 1.
DR   Pfam; PF23254; KH_PARP14_8; 1.
DR   Pfam; PF01661; Macro; 3.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF23222; RRM_PARP14_1; 1.
DR   Pfam; PF23245; RRM_PARP14_2; 1.
DR   Pfam; PF23085; RRM_PARP14_3; 1.
DR   Pfam; PF22005; WWE_1; 1.
DR   SMART; SM00506; A1pp; 3.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 3.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS51154; MACRO; 3.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 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   Reference proteome {ECO:0000313|Proteomes:UP000504623};
KW   Transferase {ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          789..976
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          1002..1189
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          1216..1387
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          1523..1601
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          1605..1801
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          90..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1801 AA;  202653 MW;  DFC12746B2D3FA9E CRC64;
     MAEPDSFPLL VKGSWGLDPP KNLRNKLHVY FQSSKKSGGG DCVVRAEPGN QSHFLVIFSR
     ENVRQKVLAR ENHELVWPDK GTFKLTVQLP TSQDETQDVT RRQIPKTESK TKEDASVPDS
     DISEEPDTEL SLNRTAEKME AIPENISSLV AFENLQESMS DIVLTLLVEN ISGLSAHNND
     FQVELIQDIH AGVVTFHRHL DTRKFIDDCF RYHSAKHLNI SVRLLEVTRV LRVENLPPGV
     EEYYLTLFFE NPKHGGGTVD SVKYLPRESS ALIEFSDRKV LDTIMTKKLV FNNMPLSVFP
     YYPSLGTALY GKEKPLIKLP APLEVPLPLP VCKFIQKKDQ LIEKINSDMG HCHCELTWLL
     HDGVVTIRPA ATLINQGRQK IYNWDEDAST AFSAVTSKFQ VSTFQVEPTV WDTIKNDFKD
     DEILIEYDTL EETVIIVGKS ENVQSIEPQI RNSTEMITQK IRREKQSLKE KVSVSPGKYF
     LLRHYGLLER LHKVCSEVEI SYDADTRHIF LKGLQADVYK LKCEIQEQVH TLVQKSIQVT
     HEIFQFLKQV NSEEFSESLF IAKKVFAVYE LEHAGVLLTS CSPEDLLKAE QQVANAFNYK
     CIEVEDREVL KDKRWKGHIL NLHKKHNSSS KTVIIDELTS DTTAQVIITG CVREVNEVYD
     LLFDFVEKHT KIERLIEIKP FLLAQYLKTE KKSIWSKMKD VRLNFNPENK QKGIVLTGPK
     TKVLEGIKII QELQDSIYIK SICIDKPGAS DFFQDKERYY KGEARRQFGC FIELHKDQEK
     EDDDAGGKRC YAWAELAPGV SLLVQKGDLT RFPVEVVVNA ANENLEHTSG LAGALLKAAG
     PELQSNCDDI VKMKGKIQAG SAVITKAGKL PYYHVIHAVG PRWRVNEAPK CEFLLRRVVE
     ESLQLAEKHR YKSIAIPAIS SGVFGFPLHQ CVKTIVLAIK ETFQYNRKGS TLKEIYLVDV
     SVKTVEAFAE IVKTMFKDTV SGNVSLHSVP TANQPTMRTD LGNSNPLLSP EGLRIHLLEG
     HVQDVRTKVI VNSIPLDLEL GRGPLSKALL DKAGPKLQDE LNISGQSMIV NVGSVLRTSG
     CNLHCQCVLH VVCPEWRNGS TTSIKIMKDI IKECLEVTEK LSLKSITFPA IGTGNLGFPK
     AIFAELIISE VFKFSSKNQL KALEDVYFVL HPSDDENIQV FSASFARRAN GNLAIDKVPK
     ADEDTQVFYG IISSPDLGVH EMKIGPIIFQ VASGDIIKEA ADVIVNSTSN TFNLKTGVSK
     VILEAAGPDV EGECILEAKK ANKGYIITKG GLLGCKNIIH VIGGNDVKKS MTCVLQECES
     RKYESICLPA IGTGRANQDP DKVAKAMIDA IEDFVQKGSV HSVKKVKVVI FLPQVLDVFY
     TNMKKREGSQ SSASPSIMSK IASFLGLSQQ PPKKQTPLVL EKKTVSATFL VCGENERNVG
     NTITWLQDLI KKEQFTYNNE DENIKNFDEK EYQELNKLQK NLNITIALDT RKSFIEVKGI
     SRDVVKATSA IEEMIKRVRV TKEQASQADC ISEYIEWQYS ENNTFYSFDK ISNMQLENAK
     RAKQKTVQVK IHDQNCTVDL QACTATDARG RSLSIQRLTK SEVEVPMNWS DMKQQSSCVV
     ELKPSHAEYI LVANKFNQTC STFKIQKIER IQNLDLWNCY QAKKKTMDAK NSQTNNEMLL
     FHGTDEGSVP HVNQKGFNRS YAGKNAVAYG KGTYFAVNAN YSANDTYSRP GSNGMKHMYY
     VRVLTGIYTV GNSSLIVPPS KNSQDPTDLY DTVTDNTQNP SLFVVFYDYQ AYPEYLITFT
     R
//