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Database: UniProt
Entry: A0A2K6MXC2_RHIBE
LinkDB: A0A2K6MXC2_RHIBE
Original site: A0A2K6MXC2_RHIBE 
ID   A0A2K6MXC2_RHIBE        Unreviewed;       749 AA.
AC   A0A2K6MXC2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Poly(ADP-ribose) polymerase family member 9 {ECO:0000313|Ensembl:ENSRBIP00000040421.1};
GN   Name=PARP9 {ECO:0000313|Ensembl:ENSRBIP00000040421.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000040421.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000040421.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000040421.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   AlphaFoldDB; A0A2K6MXC2; -.
DR   STRING; 61621.ENSRBIP00000040421; -.
DR   Ensembl; ENSRBIT00000064452.1; ENSRBIP00000040421.1; ENSRBIG00000043630.1.
DR   GeneTree; ENSGT00940000158837; -.
DR   OMA; LSCQYVY; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR   GO; GO:0072570; F:ADP-D-ribose binding; IEA:Ensembl.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0140802; F:NAD+-protein-C-terminal glycine ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0097677; F:STAT family protein binding; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0060335; P:positive regulation of type II interferon-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR   CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR   CDD; cd02903; Macro_BAL-like; 1.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 2.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14453:SF70; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP9; 1.
DR   Pfam; PF01661; Macro; 2.
DR   SMART; SM00506; A1pp; 2.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 2.
DR   PROSITE; PS51154; MACRO; 2.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180}.
FT   DOMAIN          107..296
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          306..487
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          522..745
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
SQ   SEQUENCE   749 AA;  83780 MW;  F597F86C0C1E18A7 CRC64;
     MDFSTVAGAA AYNKKSGRIT SLSLLFQKVF AQIFPQWRKG NTGECFPYRC SGTDAVREKY
     SSRIPINHND FKIFKNNERQ LCEVLQNKFG CISTVVSPVQ EGNSKSLQVF RKMLTPRIEL
     SVWKDDLTTH AVDAVVNAAN EDLLHGGGLA LALVKAGGFE IQEESKQLVA TRGKVSTGGI
     AVTGAGRLPC KEIIHAVGPR WMESDTQGCI RKLERAIVSI LDYVFYGNTH IKTVAIPALS
     SGIFQFPLNL CTETIVETIW VHLQRKPMMS NLKEIHLVSN EDPTVAAFKA ASELILGTSE
     LGQETTPSFN AMVINNLTLQ IVQGHIERQT ADVIVNSVDP RDITVGPVAK SILQQAGAEM
     RLEFLATKAK QFQQSQLVRV TRGFNLSCQY IYHVLWHLEF PKLQILKHAM KECLEKCIEQ
     NITSISFPAL GTGNMEIKKE TAAEILFDEV LTFAKDRVKH QLTVKFVIFP TDLEIYKVFS
     AEMAKRSKML SLNNYSVPQS TREEKRENGL EARFPAINLM GFNMEKMWEA LTWIQRILSL
     QNHHIIENNH ILYLGRKEHD ILSQLQKTSS VSITEIIKPG RTQLEIKGAQ ADLIEVVMNI
     EDMLCKVQEE MARKKERGLW SLLDPKYGAG IYFTKNLKNL AEKAKTISAA DKLIYVFEAE
     VLTGSFCQGH PLNIVPPPLS PGAVDGYDSV VDNVSSPETF VIFSGMQAIP QYLWICTQDY
     VQSQDDSLGP VRPFAQHPWR GLTSGSPVD
//
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