GenomeNet

Database: UniProt
Entry: L5KD86_PTEAL
LinkDB: L5KD86_PTEAL
Original site: L5KD86_PTEAL 
ID   L5KD86_PTEAL            Unreviewed;      1847 AA.
AC   L5KD86;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=PAL_GLEAN10010683 {ECO:0000313|EMBL:ELK09307.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK09307.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   EMBL; KB030834; ELK09307.1; -; Genomic_DNA.
DR   STRING; 9402.L5KD86; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   InParanoid; L5KD86; -.
DR   Proteomes; UP000010552; 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   CDD; cd01437; parp_like; 1.
DR   Gene3D; 3.90.228.10; -; 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; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR031273; PARP4.
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; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR46530; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP4; 1.
DR   PANTHER; PTHR46530:SF1; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP4; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF08487; VIT; 1.
DR   Pfam; PF13768; VWA_3; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00609; VIT; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          128..221
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          361..496
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          495..699
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   DOMAIN          733..861
FT                   /note="VIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51468"
FT   DOMAIN          1002..1169
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          55..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1553..1572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1847 AA;  204085 MW;  A45150695F748D62 CRC64;
     MLSKASPWPP GKDRTIDGAL DLQRKIMETF KWQHHHPLFP NSDSGVTLIA HILPGRRNRK
     TPPPGAGAER DSPQRPSQKC PRSGIPGGGR GSGPPTGSRL ASSPQPESRR RKRREQRESG
     GAGSSGRMTM GVFANCTFCL NIKHLPRQQK KKLQTDIQEN GGNVSFILNS QCTHIISDSA
     GDLSKYHLNY IQKNHIHIAN PDFIWESIKE RRLLDVKNYS PNKSLDSTLP LYQGASSSEV
     KTDDGCLDNS AETGGVELTK FYTENVEIPH FPQDFEVAKY NALEKVGTEG VQDIAVLELQ
     CPQDPGHPTF RISACFHPTG VTETRRQFLV RPTSADASEC YENYIEELKK QGFQLREHFT
     PEATQLASGK LQAWLLEEDI RSSALSQEVS DLVEMVWAEA LGHLEHTLLT PANRISLNDV
     SKAEGILLHV KAALKSGETE EQLQKMMSEF YRLIPHRGST TEEVNLRLLA KKEDLCQLIR
     DMANVNETNL SKRNPPSLAK YRALRCKIEH VEQNTEEFFR VRKEVLQNNR SQSPVDILQI
     FRVGRASETT AFLSQLGNVT SLLHGSPVRS FVGILSRGLL LPKVVEDRGV TRTDVGNLGS
     GIYFSDSLST STKYSHPGDT DGTRLLVVCD VALGKCLDLH KKDFSLTEAP PGYDSVHGVP
     GTATVTTDFE DDEFVVYKTN QIKMKYIIKF CLPGDEIKDF HPCNNIELEE YTPEISNFPT
     VEDYRLPDSG PSSSLGAGLQ DASGNSVPLE DVCIKGKIID FVAQVIVFQT YTNQSHVPIE
     AKYVFPLDDK AAVCGFEAFI NGKHIVGEIK EKEAAHQEYR EAISQGHGAY LMDQDAPDVF
     TVSVGNLPPK AKVLIKITYI TELSIQGTVA VFFMPATVAP WQQDKALNEN IQDTVKKISI
     KEIGSKQSFS LTMSIEMPYV IEFISSDTHE LKKKSTDCKA VISTVEGSTL DSSGFSLRVG
     LTDAHLPRMW VEKHPEKESE ACMLVFHPDL GSAFSDTAER SEVVICLDCS SSMEGVTFLH
     AKQIALYALS LVGMEQKVNV IRFGSGYQEL FSYPKCLTSD SVAAEFITSA SPTMGSTDFW
     KVLRYLSLLP PSQELRNVLL ISDGHLQSDS LTLQLVKRHV QHTRLFSCGV GSTANRHLLR
     TLSQHGVGAF EYFNSKSKYS WKKQIEDQMT RSRSPSCHSV SVTWQRLSPE APEPLQAPAQ
     VQALFHGDRL LVYGFIPHCT QATLRALTQE EEFSTMVSTT ELQKTTGTMI HKLTARALIR
     DYEDGILHDD ETNHEMKKQV LKSLIIQLSK ENCLITQFTS FVAVEERDGN ESPFPNTPNI
     LELVAKDVDI LPYMSWQEVQ PCGFNAPCGS AWQPLSASSD WHGEFHLSKR KQKPSTVEVF
     GVLEGLSLAS KAPEKHFRSG WKCTHAETPL DLSQMEPRTC KGAGTPLATA ISPQMAVCRS
     FATPRPAASP AALGSVSFSH PCPPREPPHS SLFSFCSAEL SGPATSDLIP EAGCSINVFP
     EQDSALRGLP PNPPVESFIG PAFAGGLFGS RQCSLPTNYK GLQALGNAGT FLEVDSSPQP
     SPPFSSPSLS PPFSAADSTL LPPSDFSTFN FLESATPLST SYMQPAHLLG LGYHGYGASP
     SNLPARNAVS RQGLRSAVPR SFGTENDETR GFLRITPFKK VAKSHVAGRE FTASSQAWEN
     QGPGICQQSQ RSSVPWTGLF RLQTEDGFWK LTPELGVILN LNIDILNSFL EQKGILSLGV
     KGRERLLDLI ATFLVLQFLR TQLEQKGIVF KSLMKLDDAA VSRDIPWASE KIKKASEWVR
     RTEGQYPSIC QRLELGKDWD SATKQLLRLQ PVNTTSPLHR VLNYGQG
//
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