ID V9KGR0_CALMI Unreviewed; 770 AA.
AC V9KGR0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 22-FEB-2023, entry version 30.
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};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO97201.1};
RN [1] {ECO:0000313|EMBL:AFO97201.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFO97201.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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 EMBL; JW864684; AFO97201.1; -; mRNA.
DR AlphaFoldDB; V9KGR0; -.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
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; IPR003903; UIM_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:SF94; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP10; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50918; WWE; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 482..562
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 567..770
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 158..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO97201.1"
SQ SEQUENCE 770 AA; 86522 MW; 402580C387B16F31 CRC64;
QVQVSHSGDR VHLLTLGEFR AEAEKRLEDY FGETGLQESV IVMESGKLRF LQDNYHEVLA
GIGQVSIVPL EGNDITGLRI SGSASACQPA DELLRSIISS ICSSTVMLQH PGIARFLLEE
RGRNILKQLE TKYRCTFGLE RVRWLPLEPE HSLDSSEKWI TPNFQRSGSG GRERSIQSHQ
QPPVSVTDPN GNRLDLGMIT NLIASIDGNE PMATSVETGN EAGEIPAARG SAATSEASSP
EEDLYTEPLA QTMSMAREEE ELEIIEMDTV TQQEGGNEGD GDGERLEDSG MMLVASDKDL
EFATKLSLET FQTERNLDED AQLLLALQCS MDNRSREDEE LQKALELSMV ESHRSMELEM
SNNMESSGAS AMEDVLQMSI QDAVEASNSA QLTVYGNCDL DFRRVKAELE KIIQSNLRRE
EIENDCLQEL SSEHERYLSH LQRQHGVTIT RRGAVLQVYG FADYTMRAST GVNRLVNRAL
REQKAQVEEA EVARSVKWVR YGAEEGATPV PYPASANAFI EQAFQHKQKK VEVMFDHKPY
TVNLDRMEEY NIGAAKALRI ERQTLGSPTD QEVLTLASGN IELVRVNEAT DEYRKLIRPF
YDTLQDFYNK IRIVKVEKVN NPLLYQQYML KKAKLQAVLG QTNVERVLYH GTNEESAKEI
YVHGFNRSFC GKNATLYGQG VYFATNAVMS AQDNYSPPNE QKHKFIFVVN VLTGAYAKGE
SSMKAPPLKQ DSTMPLRYDC VVDDCRNPTI FVIFNDTQAY PQYLITCLRN
//
