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Database: UniProt
Entry: A0A183BTT2_GLOPA
LinkDB: A0A183BTT2_GLOPA
Original site: A0A183BTT2_GLOPA 
ID   A0A183BTT2_GLOPA        Unreviewed;      1696 AA.
AC   A0A183BTT2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000401800};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_000401800}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC         Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173115; EC=2.7.7.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00024620};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC       {ECO:0000256|ARBA:ARBA00010912}.
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DR   WBParaSite; GPLIN_000401800; GPLIN_000401800; GPLIN_000401800.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR048840; PolA_pol_NTPase.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF10; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1576..1599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1606..1624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1630..1651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1412..1524
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          1561..1629
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   REGION          1182..1258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          644..671
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1182..1257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1696 AA;  198903 MW;  E8E10ABF9DCE8BF7 CRC64;
     MSKKGKFQRK LECFGRSPRH GVSENEQFEA IIDRSYLEEL LEQLEIESER NQQNICFLYQ
     FGVSVHQYME LFGLNNSEWT NLLRKLQIHD AIQVHMNQSV DCDDADEVAK IFLFLFGQRT
     IHTIFEYNIV KFLKMYEQLR HFFCHEIEPH SLKTELEHKL LTPASIVNLE DEFPEIFRID
     LMFTATLKER CRRMLMNRSD SELYSKTYTY WAMGWLIGEL RQACAQDDSM QNVLSAHAIA
     VLQKRVDDEC AIALNEMMSG RQMCVLERLV SFLINLKPKD VRAFEKRIKK WTAADECSDG
     KRRADTLDQF KRDSFAKTIV KFINTAFLLH AGLNSQFLQL VRISGAKTRL FKLLGNSKER
     LAELKDGRGQ LLSRFYEEDV FSQNDRLRGH YVIALADDDD DWFRFSRTLA ADVVAFMRWI
     KRELGEQRLG AVYDKIRIHI DEHLYDPLFD KNAEELKKSE KFLKKMFFET KNLLAMASAK
     GTKEMFFNKW KKIVEIGTKT NLSEEQLQEE QFWMAQLHFG EFIGLMEEAV DRHDALIYEY
     LKKVTGNATA PSAVAGDENQ QKLITCPPKS VSVKMLRHID KENNVAFLHF LSAQCMEYLS
     NHFEQIRTFK DGGHILKVQM YAILWYLSEV GAKLVKRADE LKPLGNDQNR KQKLHLEVAK
     LRRNLAQLTD ITKNNGQEEL VVLKTLELRL FKMYKFVERI AVNKQFMENS SGWHQIIQQE
     TNLEMLNNVP SDVDEDEMPT IYMELFEPEQ LFKITFFFIY DLLVRFTELQ KFFCDLSGVE
     QREKVQARLE YAFGEQHLHT FEELVPEIMQ FDMPSPLTAA ISFKYLLCEK VGTDQFQIAE
     ARLSLPRLLN EKKGWEIRTL KFDQCARKSV QQRVLQQQRK EMLPIHALFL SLILEKNAFA
     FNDFVKDNRG NYHSKLIEPE MFHGERLRQL YLDALFGDDI GTRVVGKLSV FIAIFVRWMD
     AELSDHPNIT IGLRQVGNMV WKNKTRPFLE DIFDELVDDS LDELEEKSYL LKELVKSLKQ
     FVEEKRDLRD LDKLDMRMAS KGKQKSKLRT KTGKNMLVPM KSNNLAEEWQ QMMAEAWRKA
     EEMRKAGTRE KELGEEQEEQ QLNLWLQQTQ WATIIELLED DNGRELFRNG FALCPLSEER
     LTDFFSLEMA EEILELLNME NNVDIKERLK VMKQKYKEEK KEVGKANEKE QKETADRNME
     EMIREEEERM RELKARIEKM QEEKRREKAE QRDRDKKEKE AKEERTKNNR KENTEFQIES
     GSDTNLQVEL APVEIADFGS DDFLEGKYFD FFKNPSKSQR ELLDIGVFVN EINVAKSNVL
     TRFAEHIENW RNLLAQQALD KKMFDQFSSH ITNKKLQLEN MHGMHEYMQQ IYFQDSEDKQ
     KDKMLDHFLE ENGYMRKELP LNVMNEVKAT ISKWSKGEAR LIVTGSQLLG TQTPGSDIDT
     ICIVPQKLTG INSYQRSCED ESLYCQFCRN SKVEEMTKIP SAYIQMLQLK LSGIKFDISF
     VLVPGTEYLP DDPLDVDDVE LMMEVLATQH RPPQAMLRSL SSYLTNQGIM TLLNLKNREK
     FRTLSLALKI WAKNNYIYGS IFGFFNGISL SIMATKIILL YPNGSVLFLL EKLLFVFTIW
     NWPMPVKYRH FVIISCIVGI AQHIVQFCLF VERKIRLQLA HFGKIMDKTV EYGHVMPTKE
     LAIQNKCPAT LXYSLS
//
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