PAP1_MIMIV
ID PAP1_MIMIV Reviewed; 584 AA.
AC Q5UQS6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 23-FEB-2022, entry version 56.
DE RecName: Full=Putative poly(A) polymerase catalytic subunit;
DE EC=2.7.7.19;
GN OrderedLocusNames=MIMI_R341;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP SIMILARITY.
RA Abergel C.;
RL Unpublished observations (SEP-2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP LOCATION.
RX PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT "Mimivirus giant particles incorporate a large fraction of anonymous and
RT unique gene products.";
RL J. Virol. 80:11678-11685(2006).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC {ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC -!- SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic
CC subunit family. Highly divergent. {ECO:0000305}.
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DR EMBL; AY653733; AAV50610.1; -; Genomic_DNA.
DR RefSeq; YP_003986843.1; NC_014649.1.
DR PDB; 4WSE; X-ray; 2.84 A; A/B=1-584.
DR PDBsum; 4WSE; -.
DR SMR; Q5UQS6; -.
DR GeneID; 9924958; -.
DR KEGG; vg:9924958; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR045355; PolyA_pol_cat_su.
DR Pfam; PF19244; Poly_A_pol_cat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; mRNA processing; Nucleotide-binding;
KW Reference proteome; Transcription; Transferase; Virion.
FT CHAIN 1..584
FT /note="Putative poly(A) polymerase catalytic subunit"
FT /id="PRO_0000253421"
FT REGION 522..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 19..41
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 182..203
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:4WSE"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:4WSE"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:4WSE"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4WSE"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 377..393
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 397..421
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 445..459
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:4WSE"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4WSE"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:4WSE"
SQ SEQUENCE 584 AA; 68247 MW; D14A33890DE87406 CRC64;
MLKNKTRAEK YQTYYTTNEY QIVKEKLPDI IRDAEIKASE VLEPTIYEKR AIMEVIKDFI
RDHQRKVYGG TALNEALKQV NPKDAIYDNY SFSDIEFYSP TPVQDLVDLC NILYRKGYKF
VQGKDAQHEE TYSIFVNFQL YCDITYSPTR VFYGIKTIEI DGINYTDPHF MLIDYLRMVN
QPLTAAGQRW EKAFERMYRL LKDYPIEDFD KRLDIPEPPE EIQSYISRIK TEFLSDNKLN
ESFLISGIEA YNFYIRHAAS SKDEEQMART NRNVVNLNNF IANVPFSELI SVNYREDVKN
TYNFLRMIVE DKEKISVDEY FPLFQFTGYS TVIKYDDHPI IRIYEGDGYC IPNVKTVKTV
ENDNGTKTKY EYKYVSFQYV LMILYINKFR AHLDKNKPMY FNYGIAISNL VKARNIYLDQ
TGKSVLDNTV FKEFRTNCTG NTISFTRMNR LRLLEKRKQG KQTSFVYTPE DFFKKDLETQ
AKLDPSKARF KNTSGNKIMV PKYLLFKIDN NGNIEDNIHS EEAEISEKEE TSGGSSISTD
KSFEESPNSS PNSSPNNSLN NSIDISTNNY DDRSENSLDS LTSD
