ID U5VX19_9ACTN Unreviewed; 657 AA.
AC U5VX19;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=UmuC domain-containing protein {ECO:0000259|PROSITE:PS50173};
GN ORFNames=AFR_09880 {ECO:0000313|EMBL:AGZ40265.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ40265.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ40265.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ40265.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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 -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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DR EMBL; CP006272; AGZ40265.1; -; Genomic_DNA.
DR RefSeq; WP_023359974.1; NC_022657.1.
DR AlphaFoldDB; U5VX19; -.
DR STRING; 1246995.AFR_09880; -.
DR KEGG; afs:AFR_09880; -.
DR PATRIC; fig|1246995.3.peg.2015; -.
DR eggNOG; COG0389; Bacteria.
DR HOGENOM; CLU_026357_0_0_11; -.
DR OrthoDB; 5244088at2; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd03468; PolY_like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR35369:SF2; BLR3025 PROTEIN; 1.
DR PANTHER; PTHR35369; BLR3025 PROTEIN-RELATED; 1.
DR Pfam; PF00817; IMS; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT DOMAIN 31..152
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 427..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 69001 MW; B2763FAD91032C7A CRC64;
MSGVRTLLVW CPDWPVIAAE IVEGVAASGA VVVLHGNRVF ACSEAARAEG VRRGLRRREA
QSRCPQLVVV EHDAGRDARA FEAVVAAVEE VAVGVEVIRP GACALAARGP ARYFGGEEQA
AERIVEQVAQ ACSVESQVGI ADGVFAAGLA ARGGQIVAAG RTREFLAGVG VEALERPELT
DLLRRLGVKS LGDFAALPAS DVLSRFGFDG ALAHRLAGGL DYRALAVRRP PPDLEVSDTY
DEPLERVDVA AFAGRVLAER LHERLAAHGL ACTQLGIEAV TADGQELHRV WRHDGTLTAA
AIAERVRWQL DGWLTGARRG ATNRPTAGLV RLKLVPDGVI VHLGLQPGLW GDVGAEKERA
HRALSRIQGL LGPEAVVTAV LGGGRSADDQ VRLVPWGDER VPARAAGEAA TPLPATDALV
VAPLAASPAL APPPRDGEGE APEHTRRALR AVPDAESRTG VIGPSWTGEA SGTETRAKTI
QLGKRLAAPV NPAGREDAGE QQNSASERSP AHQGPAAHEG LAAQEGAVDR AVGEGRGKRG
RGVRKPVPQP PWPGRLPRPA PALVLPQALP AVVLDGEGQA VGVSARLELS GEPALLFIEN
GGPVEITGWA GPWPVDERWW APGEARRRAR FQVVVADGRA LLLSLVAGHW AVEAIYD
//
