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Database: UniProt
Entry: A0A0D2DWM2_9EURO
LinkDB: A0A0D2DWM2_9EURO
Original site: A0A0D2DWM2_9EURO 
ID   A0A0D2DWM2_9EURO        Unreviewed;       664 AA.
AC   A0A0D2DWM2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=UmuC domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_00167 {ECO:0000313|EMBL:KIW47473.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47473.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW47473.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47473.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN847332; KIW47473.1; -; Genomic_DNA.
DR   RefSeq; XP_016267689.1; XM_016400636.1.
DR   AlphaFoldDB; A0A0D2DWM2; -.
DR   STRING; 215243.A0A0D2DWM2; -.
DR   GeneID; 27352241; -.
DR   VEuPathDB; FungiDB:PV06_00167; -.
DR   HOGENOM; CLU_012348_7_1_1; -.
DR   OrthoDB; 118267at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070987; P:error-free translesion synthesis; IEA:UniProt.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR041298; UBZ3.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR   PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF21704; POLH-Rev1_HhH; 1.
DR   Pfam; PF18439; zf_UBZ; 1.
DR   PIRSF; PIRSF036603; DPol_eta; 2.
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.
DR   PROSITE; PS51907; ZF_UBZ3; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          43..305
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   DOMAIN          582..616
FT                   /note="UBZ3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51907"
FT   REGION          613..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  73955 MW;  C4628768C70C0CC1 CRC64;
     MSSSQPFQPS SPLAGGKRRK SRFTYKHLHL LGQSSTTCPL RVIALIDYDA FYAQCEMVRL
     GVVESQPLAV QQWQGLIAIN YPAREYGLSR HVPITEAKAK CPEIVIQHVA TWREGDTKWA
     YRDDAASHIQ TDKVSLDPYR LESRKSLALV KEILPPPPIQ KVEKASIDEV FLDLSAQIHQ
     ILLERYPELK YAPYDDPTEH LPLPPSTALD WQADALVDLD SAETEDDDPD WDDVAMNIGS
     EIVRGVRATI RERLKYTCSA GVARNKMMAK LGAGYRKPNQ QTIVRNRAVQ HFLSGYKFTK
     IRNLGGKLGD QVVDTFNTDE VTELLKIPLE QLKSKMGEET GTWLYGTIRG EDHSEVSSRT
     QIKSMLSAKS FRPSINTTDQ ANKWLRIFVA DIYARLVEEG VLENKRRPKT ITLHHRQGGQ
     TKSKQLPIPS GKKIDETILF ELAKTLLGQV VVDGRAWPCA NLSLSVGGFE EGVAGNKGID
     MFLLKGEEAK AAIEAPSRSN TTTPNIEDLI PAKRRRLNDA PTNIARFFAK GESTEEASES
     ADEDIVAQEH HLEANNDGNG NGDEVYHDEG PDQHLTHAMQ ERDIATYFCQ ECQKSINEPD
     RGEHEDWHFA KQLQAQDAPA VTGPSNSRPP GPLHTNKTKR GGTGSNSRGR GSKPEKGQSR
     LAFG
//
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