ID A0A2S2CW11_9PROT Unreviewed; 421 AA.
AC A0A2S2CW11;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DEW08_21055 {ECO:0000313|EMBL:AWK88590.1};
OS Azospirillum thermophilum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88590.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC untargeted mutagenesis. Copies undamaged DNA at stalled replication
CC forks, which arise in vivo from mismatched or misaligned primer ends.
CC These misaligned primers can be extended by PolIV. Exhibits no 3'-5'
CC exonuclease (proofreading) activity. May be involved in translesional
CC synthesis, in conjunction with the beta clamp from PolIII.
CC {ECO:0000256|ARBA:ARBA00025589}.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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DR EMBL; CP029355; AWK88590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CW11; -.
DR KEGG; azz:DEW08_21055; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000245629; Chromosome 4.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR CDD; cd01700; PolY_Pol_V_umuC; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR025188; DUF4113.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11076:SF34; PROTEIN UMUC; 1.
DR Pfam; PF13438; DUF4113; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00023199};
KW Reference proteome {ECO:0000313|Proteomes:UP000245629};
KW SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 5..189
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
SQ SEQUENCE 421 AA; 46050 MW; 98B0401866238147 CRC64;
MARTLALVDC NNFYVSCERV FRPDLEGVPV GVLSNNDGCF VARSAELKAL GVRMGQPLFE
VRDLVRHHHV RVFSSNYALY GDMSARVTDC LRGFTPALEI YSIDESFLDL TGIGGDLSGY
GAEIRQTVKR WTGIPVCVGI GPTKVLAKLS NHAAKKALLD DRGVCDLRDA DAREHVLRAV
PVEEVWGIGR RSAEKLSLLG VRTAADLRNL DPRLARQALT VVGERIVYEL QGVACLSLDL
VPPSRKTIAV TRSFGQPVTD WEPMREAVAA YATRAAEKLR AERLAAEALQ VFMHTSPFRP
GPTYSNAVTV ELRPATDDTF ALIAAAAAAA RRIWRDGYAF SKAGVILPGL VPLERVQPDL
LAAADRQRGT RLMKALDAIN STMGKDTLVP AATMGRAWRM RQEQRSPSYT TRLADVPVVQ
A
//
