ID   A0A0F8ALJ1_LARCR        Unreviewed;       874 AA.
AC   A0A0F8ALJ1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Poly [ADP-ribose] polymerase 12 {ECO:0000313|EMBL:KKF22414.1};
GN   ORFNames=EH28_07095 {ECO:0000313|EMBL:KKF22414.1};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF22414.1};
RN   [1] {ECO:0000313|EMBL:KKF22414.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSNF {ECO:0000313|EMBL:KKF22414.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KKF22414.1};
RX   PubMed=25835551;
RA   Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA   Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA   Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA   Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT   "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT   Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL   PLoS Genet. 11:E1005118-E1005118(2015).
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   EMBL; KQ041811; KKF22414.1; -; Genomic_DNA.
DR   RefSeq; XP_010736181.2; XM_010737879.2.
DR   AlphaFoldDB; A0A0F8ALJ1; -.
DR   GeneID; 104924514; -.
DR   KEGG; lco:104924514; -.
DR   eggNOG; ENOG502QSC4; Eukaryota.
DR   OrthoDB; 5490222at2759; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
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; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          78..104
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          375..402
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          462..548
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          572..785
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   ZN_FING         78..104
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         375..402
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          220..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  98622 MW;  EFF8B2A5D93E469D CRC64;
     MMEADILKLI CSCQGAMDTQ DLLCNLGSVD LTSVSEIICN QEKFVTCVPY GQPKVVARSR
     LRLCRLKDCP GQCRGLHLCK NFLFSGSCRY SQQRRGCNFS HDLHSAHNER ILREHELESL
     NRTELCTLLM QSDDGLLPPI CYDYNNGDGE FGRCQEGIVC KRLHICERYL NRECNCTRNH
     DFSAPQTLKN LQGRGVPDNL IYSIKSAYAN KLALKYADRG GDKSNFEQRG GNRGHRGNRG
     NRGNRGNRGN RGNRGSTGNQ GNGQPMQRAA STSDILAGIN AFYVHDDNAL NSSNSDISSA
     ANDPDASSDD GHKQTGNPPK TSTAVRGRGG IHGNRGNRGN YQPLDRTHST NDLFAAVNDD
     ANSEDGRRER KRPVRDKTEI CMYFIKGHCK HEDRCYKHHD KMPYRWQIRE NDEWTAMPSN
     EMIEKDYCDP KNTYSSSSSP AVHFDTMTCG TNKVRRLSTI NSLLEPDFIH TTEWAWYWED
     EFGKWTMYAS MDGGHKQADM DSSKLEQMFM ANNKDEVEFT AGSQSYSLSF QDMIQTNKRY
     GTKRVVRRRP RFFSAEDVQA RRVRPRANLA AVPDHWDKTQ VTQTGYKRVP LLRTTDEFKE
     IEALFCKTMK GFDIIKIERI QNKALWEVFQ WQKTQMRTKN SGRMVTEKKL FHGTDSKYVD
     VICHTNFDWR ICGTHGTAYG KGSYFARDAK YSHNYTGDSD VRSMFISRIL VGNYTKGSSS
     YVRPPSKDGG DINFFDSCVD DVMDPSIYVV FEKLQIYPEY LLEYKTTHLF DGLFGVASVP
     APKPVPAPKP VTVPKPAPYS TSSYQPSTSS YQPSTSSYRP STSSYQPSTS SYQPSTSSYQ
     SNTSSVNFSS SSTSTKSTPY SSSSSSKGDS CVIA
//