(data stored in ACNUC7421 zone)

SWISSPROT: Q2IMM3_ANADE

ID   Q2IMM3_ANADE            Unreviewed;       549 AA.
AC   Q2IMM3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Poly(A) polymerase I {ECO:0000256|HAMAP-Rule:MF_00957};
DE            Short=PAP I {ECO:0000256|HAMAP-Rule:MF_00957};
DE            EC=2.7.7.19 {ECO:0000256|HAMAP-Rule:MF_00957};
GN   Name=pcnB {ECO:0000256|HAMAP-Rule:MF_00957};
GN   OrderedLocusNames=Adeh_0279 {ECO:0000313|EMBL:ABC80055.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80055.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which
CC       usually targets these RNAs for decay. Plays a significant role in
CC       the global control of gene expression, through influencing the
CC       rate of transcript degradation, and in the general RNA quality
CC       control. {ECO:0000256|HAMAP-Rule:MF_00957}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine
CC         ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:11128,
CC         Rhea:RHEA-COMP:14647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:83400, ChEBI:CHEBI:140626; EC=2.7.7.19;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00957};
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000256|HAMAP-Rule:MF_00957,
CC       ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00577624}.
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DR   EMBL; CP000251; ABC80055.1; -; Genomic_DNA.
DR   RefSeq; WP_011419338.1; NC_007760.1.
DR   STRING; 290397.Adeh_0279; -.
DR   EnsemblBacteria; ABC80055; ABC80055; Adeh_0279.
DR   KEGG; ade:Adeh_0279; -.
DR   eggNOG; ENOG4105D4J; Bacteria.
DR   eggNOG; COG0617; LUCA.
DR   HOGENOM; HOG000256526; -.
DR   KO; K00970; -.
DR   OMA; FMAKLDM; -.
DR   BioCyc; ADEH290397:G1G5W-286-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   HAMAP; MF_00957; PolyA_pol; 1.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR010206; PolA_pol_I.
DR   InterPro; IPR025866; PolyA_pol_arg_C_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12626; PolyA_pol_arg_C; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   TIGRFAMs; TIGR01942; pcnB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMM3.
DR   SWISS-2DPAGE; Q2IMM3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00957,
KW   ECO:0000256|SAAS:SAAS00415369};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_00957};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00957,
KW   ECO:0000256|SAAS:SAAS00415411};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00957,
KW   ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00468387};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00957};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00957,
KW   ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00468438}.
FT   DOMAIN       71    200       PolyA_pol. {ECO:0000259|Pfam:PF01743}.
FT   DOMAIN      228    289       PolyA_pol_RNAbd. {ECO:0000259|Pfam:
FT                                PF12627}.
FT   DOMAIN      354    458       PolyA_pol_arg_C. {ECO:0000259|Pfam:
FT                                PF12626}.
FT   ACT_SITE     89     89       {ECO:0000256|HAMAP-Rule:MF_00957}.
FT   ACT_SITE     91     91       {ECO:0000256|HAMAP-Rule:MF_00957}.
FT   ACT_SITE    170    170       {ECO:0000256|HAMAP-Rule:MF_00957}.
SQ   SEQUENCE   549 AA;  59951 MW;  AF67217716B456C2 CRC64;
     MHEPSTKNDL FRPAYPAEDL EENRDRRPPP GLALDPPEAP PPEHPPEIPV DRLDGDALKV
     IARLRHMHHQ AYLVGGCVRD LLLGATPKDF DVATDAHPGE VRAIFRNCRL IGRRFRLAHV
     YFRAGKVIEV ATFRKNPTDV AEDVGEGEGD LLITRDNVFG TAEEDSVRRD FTVNGLFYDV
     ATGEVIDYVG GRADLEAHRI STIGDPEIRM REDPVRALRA VRFAARLGFT IAPDTFEAMR
     RTAGELARCA PARVLEETFK LLRCGGSARA FELLRACGAL PVILPALGAA LETWDDGRRR
     AFFAHLAALD RLVRSGAEVS EAVLLGALLM HLGADAPRAG RPDADAGAPR WDEADAFLAS
     LVQTARLPRK VAERIRLALQ AQRQLEEPGK RRRRRGRGPA GQTYFQDALQ LLEIRVRATG
     SGGEALERWT AEAPHAHPAA ERPGRAGPRE DRRDHRREGA APRRPDRDEG AVREVVIPVE
     AAEAADEAGE EVREVESSAA GDAGEGEASQ GGRRRRRRRG GKRRRRRGAG ASGPDGGAQV
     PPAEAGGQG
//

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