ID A0A2Y9QMP3_TRIMA Unreviewed; 1667 AA.
AC A0A2Y9QMP3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC101350264 {ECO:0000313|RefSeq:XP_023580609.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023580609.1};
RN [1] {ECO:0000313|RefSeq:XP_023580609.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_023580609.1; XM_023724841.1.
DR Proteomes; UP000248480; Unplaced.
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; cd17726; BRCT_PARP4_like; 1.
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:UP000248480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 3..96
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 244..372
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 371..575
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT DOMAIN 609..738
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 823..993
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1445..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1667 AA; 187678 MW; FDB52516D1C9D9C4 CRC64;
MGMTVGIFAN CTFCLKVKYL PRQQKKKLQT DIKENGGNFS FSLHPQCTHI ILDNADVLSQ
YQMKSIQEKH IHIVNPDFIW NSVKERRLLD VKNYNLNNSL EISLPPGQKE SSSDVETDDP
SLVNSTEKEN IVEFAKFYTD NVEIPHFSQE FEVAKYDTLE KIETEGRKEI VVVEMQCFQE
HWDCPFLITA CFLLADGIET RRQFSGKKTS ADASEYYENY IEELKKQGFL LRENFTPEAT
QLASEKLQAL LLEEVINSDT LSQEVSDLVE MIWAETLGHL EHTLLKPVNK ISLNDVSKAE
GILLLVKAAL KNGETAEQLQ KMLTEFYRVI PHKGPTTEEV NLRLLSKKED LCQLIRDMVN
VCESNLYKPN PPSLAKYRAL RCKIEHVEQN TEEFFSVMKE VLQNNHSRSP VNILQIYRVG
RVNEATEFLS KLGNVKSLLH GSPARNIVGI LSRGLLLPKV VEDHGVKRTD VGNLGSGIYF
SDSLRTSIKY SHPGEIDGTR LLVICNVALG KCMDLYKKDF SLTEAPPGYD SVHGVSQTAT
VITDFEDDEF VVYKTDQIKM NYIIKFCIPG DQIKDFHPCG NTELEEYVPE FSSFPKAEDY
QLPDTKPFSN IKAGLQDTSG NLVPLEDVHI KGRVIDVVAQ VIVFQTYTNQ SHVPIEAKYI
FPLDDKAAVC GFEAFINGKH IVGEVKEKEE AHQEYQEAIS QGHGAYLMDQ DAPDTVEKIC
IKEIGTKQSF SLSMYIEMPY VIEFISSDTH KLKQKHTDCK AVISTVEGSS LDSNGFSLHI
GLSDAYLPRM WVEKYPDKES EACMLVFQPD FNITLPETAK RSEVIICLDC SNSMKGEAFL
QAKKIALYAL SLVDKNQKIN IVKFGTSYKE LFSYPKYITS NEMPTEFIMA ASPTMGNTDF
WKTLRYLNLL YPSQGLRNIL LISDGHIQNE SLTFQLVKRN VQHTRLFTCG TGSTANHHIL
RTLSQCGAGV FEYFNSKSKH SWKTQIEDQM TRLHSPSCHS VSVKWQQLST NLPEPLQAPA
WVQSLFHNDR LLVYGFIPHC TQATLCALIQ EKEFCTMVST TELQKTTGTM IHKLTARALV
RDFEYGILHE NETHHQMKKQ ILKSLIIKIS KENSLLTQFT SFVAVEKRDE NESPFPNIPN
ILELIAKEDV DFLPYITWQE EQSGASMTQI ISASSEWNED LQHKSLTERK VKSPKPEVSE
DVEVFNLATQ LPVQPLILNS ECGLVAKPLD LSWMNSLKKK KIKAQFRKSS LHTKNDVFKP
SLSLGAAPIL PGASHVDSGF LSPPVSPQNS LFGSPGSLKQ FGPSKYDQDL ETGSCTDVSL
KLDFPSRLPP QNPPFRSPAC SPFSAASFGS KQIDRSKIYQ DREICGTGIS LGTYSTPRPR
LFLSLPRLPP PVSAVGFSVP SPLHFQNSLD PLSANYKQPI DLLGFASSES GVSFPLNISA
GTALSDPPLH DLQTASSHES SSEMKSNERS VLQASRFSKR VAKSDETRSD FTSSFQAQND
EDDKVCKQSW RNFVPWTKLF SLQTEGGFWK LTPELGFILN LNTNFLNSFL EQKGIQSLGI
KGQECLLNLI ATLLVLQFLC TKFKEEGIVF KSLMKLDDTS ISRNIPWAIE GIKKASEWVR
RTEGQYPSIC QRLELGKDWD SATKQILGIQ PIDTTSPLYG VLNYSQG
//
