ID A0A0A2VY49_BEABA Unreviewed; 1355 AA.
AC A0A0A2VY49;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA polymerase III subunit delta {ECO:0000256|ARBA:ARBA00017703};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=BBAD15_g2993 {ECO:0000313|EMBL:KGQ11292.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ11292.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ11292.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ11292.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- SIMILARITY: Belongs to the DNA polymerase HolA subunit family.
CC {ECO:0000256|ARBA:ARBA00034754}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ11292.1}.
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DR EMBL; ANFO01000228; KGQ11292.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2VY49; -.
DR HOGENOM; CLU_257387_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd18138; HLD_clamp_pol_III_delta; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR032780; DNA_pol3_delt_C.
DR InterPro; IPR010372; DNA_pol3_delta_N.
DR InterPro; IPR005790; DNA_polIII_delta.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR007485; LPS_assembly_LptE.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR01128; holA; 1.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF14840; DNA_pol3_delt_C; 1.
DR Pfam; PF06144; DNA_pol3_delta; 1.
DR Pfam; PF04390; LptE; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 39..183
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..572
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 618..652
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 699..822
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1033..1202
FT /note="DNA polymerase III delta N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06144"
FT DOMAIN 1226..1349
FT /note="DNA polymerase III subunit delta C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14840"
SQ SEQUENCE 1355 AA; 152947 MW; 1C21C6F6D9A66C9A CRC64;
MQEQYRPEEI ESNVQQHWQE NRTFEVTEDE GKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNINYMKN QLKTLGFGYD
WSRELATCTP EYYRWEQQFF TQLYNKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
TKVERKEIPQ WFIKITAYAD ELLNDLDTLD HWPDQVKTMQ RNWIGRSEGV EITFDVENSA
EKLTVYTTRP DTFMGVTYLA VAAGHPLAQQ AAVNNPTLAE FIEECRNTKV AEADMATMEK
KGVATGINAI HPLTGESVPV WVANFVLMEY GTGAVMAVPG HDQRDWEFAT KYSLQIKPVI
LNADGSEPDL SASAMTEKGA LFNSGEFDGL DFQQAFNAIA DKLAAKGVGE RKVNFRLRDW
GVSRQRYWGA PIPMVTLEDG TVMPTPEDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
MPALRETDTF DTFMESSWYY ARYTCPQYDK GMLDSKAANY WLPVDIYIGG IEHAIMHLLY
FRFFHKLMRD AGMVTSDEPA KQLLCQGMVL ADAFYYTGVN GERNWVSPVD AIVERDDKGR
IVKARDAEGR ELVYAGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
SGVEGANRFL KRVWKLVYEH TNRGGAPALD VAALSEDQKA LRRDVHKTIA KVTDDIGRRQ
TFNTAIAAIM ELMNKLAKAP QDGEQDRALL NEALLAVVRM LYPFTPHVCF DMWQSLGGEG
DVDNAPWPQA DEQAMVEDSR LVVVQVNGKV RGKVTVPADA TEEQVRERAG QEHLVAKYLE
GVTWAKRRRK RATSLCHPVP SEMKTLILNS GDPNGPLTRE IRKQLRLNGV TIVDDTGTGV
RKDIPSLRVG ALGLSQDTAS VFQNGQTAEY QMVMTVNAQV LIPGHDIYPI SAKTYRSFFD
NPLTALAKDA EQDLIIKEMY TNVAQQLIRK LLAVHTADLE ATKDEEKPVN APMIRLYPEQ
LHAQLNEGLR AAYLLLGNDP LLLQESQDAV RKHAQQNGFE EHHTVQIEAS TDWQALFSIC
QALSLFASRQ TLLLLLPENG PNAAINAQLE TLVSLLHDDI LLLVRGNKLT KAQENATWFT
QLANRAVLVT CQTPEQANLP RWVSQRAKQM NLTLDDAANQ LLCYCYEGNL LALSQALERL
SLIWTDGKLT LPRVEQAVND AAHFTPFHWV DALLAGKSKR ALHILQQLRL EASEPVILLR
TLQRELLQLV NLKRQSATTP LRMLFDQQRV WQNRRQLVTE ALNRVSSEQL YQAVRLLTRI
ELTLKQDYGQ SVWDDLEGLS LLICHKALPE IFIDV
//
