ID A0A0K1EN39_CHOCO Unreviewed; 525 AA.
AC A0A0K1EN39;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Polynucleotide adenylyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CMC5_064920 {ECO:0000313|EMBL:AKT42269.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT42269.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT42269.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT42269.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|RuleBase:RU003953}.
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DR EMBL; CP012159; AKT42269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1EN39; -.
DR STRING; 52.CMC5_064920; -.
DR KEGG; ccro:CMC5_064920; -.
DR PATRIC; fig|52.7.peg.7139; -.
DR Proteomes; UP000067626; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 165..290
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 318..379
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 58976 MW; 3E2DE717ED51B664 CRC64;
MGRPTPIPVK NDPSAVSDDV LTSTSTVAAR APRSSDPPLD DFPDASTQTA GFEDDEQLAA
VEDELEFEPD DFDDFSASGS EPLLDPDPDL EAEHVAFADE PDASAPPPRP LDPESLAAVK
NPFQVELVSE TIPEPRRYHV VFDDVRLDPD VQKVVRRLTR HRHEAYLVGG CVRDLLLDRR
PKDFDVATSA RPEEVRDLFR NSRIIGRRFR LVHVLFGGGK VIEVATFRRN PKEEGEEASE
LLIRNDNVFG AAHEDALRRD FRINALFYDL EARQVLDWMG GMEDLRRQVV HTIGDPETRF
REDPIRILRA LKFAGRLGFG ITPDVYDAIV FCRDVLALAA RPRLSEEILR LMRGGQARRT
IYLAWETGVL DVLLPEVSAL IYDDRGDDGP GQRLWRLLDF ADRRTAEGRP LDDTVLWTLL
LLEPMKEVCE GARDRAGAVA DFLEPLIERL AISRRYADGM RRIVAVLPRL VSGRAGRFAR
TEIFQSSVEV AAADLAARGL STEPVDRFRA APAPRRYRSE GPFGR
//
