ID A0A3A5MI22_9MICO Unreviewed; 351 AA.
AC A0A3A5MI22;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=D6T64_14500 {ECO:0000313|EMBL:RJT87559.1};
OS Cryobacterium melibiosiphilum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=995039 {ECO:0000313|EMBL:RJT87559.1, ECO:0000313|Proteomes:UP000272015};
RN [1] {ECO:0000313|EMBL:RJT87559.1, ECO:0000313|Proteomes:UP000272015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hh39 {ECO:0000313|EMBL:RJT87559.1,
RC ECO:0000313|Proteomes:UP000272015};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Cryobacterium.";
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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:RJT87559.1}.
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DR EMBL; QZVS01000089; RJT87559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5MI22; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000272015; Unassembled WGS sequence.
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:UniProt.
DR CDD; cd03586; PolY_Pol_IV_kappa; 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 Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR022880; DNApol_IV.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR11076:SF33; DNA POLYMERASE KAPPA; 1.
DR PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000313|EMBL:RJT87559.1};
KW Transferase {ECO:0000313|EMBL:RJT87559.1}.
FT DOMAIN 1..180
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
SQ SEQUENCE 351 AA; 37374 MW; D217909572B9CBA9 CRC64;
MLHVDLDQFI AAVEVLRHPE LAGRPVIVGG RGDPTERAVV STASYEARKF GVGSGMPLRI
AARKVPDAVI LPVDREAYLE ASDTVMAALR AQPGATVQVL GWDEAFLGVV TENPEGYARQ
VQAAVFARTQ LHCSVGIGDT LVRAKVATGF GKPAGVFRLT AENWLDVMGA RPTRDLWGVG
SKVSGRLAAL GITTVAQLAA CDPRALVPEF GPKMGPWYAS LARGDGASVV DGTPWVARGH
SRETTFQQDL TEPAQVDAAV RELAAAVFQD VLAEGRPVIG LTMKVRYAPF VTTTRARKIP
ETSDSSVILA RALDLAAEID AGRPIRLLGL RAEMPMPDDA RTGHTPTRGG W
//