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Database: UniProt
Entry: A0A1S4DS83_CUCME
LinkDB: A0A1S4DS83_CUCME
Original site: A0A1S4DS83_CUCME 
ID   A0A1S4DS83_CUCME        Unreviewed;      1130 AA.
AC   A0A1S4DS83;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA repair protein REV1 {ECO:0000256|ARBA:ARBA00020399, ECO:0000256|PIRNR:PIRNR036573};
DE            EC=2.7.7.- {ECO:0000256|PIRNR:PIRNR036573};
GN   Name=LOC103482574 {ECO:0000313|RefSeq:XP_016898828.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016898828.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_016898828.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC       dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC       dependent reaction. May assist in the first step in the bypass of
CC       abasic lesions by the insertion of a nucleotide opposite the lesion.
CC       Required for normal induction of mutations by physical and chemical
CC       agents. {ECO:0000256|PIRNR:PIRNR036573}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036573}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000256|ARBA:ARBA00010945, ECO:0000256|PIRNR:PIRNR036573}.
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DR   RefSeq; XP_016898828.1; XM_017043339.1.
DR   AlphaFoldDB; A0A1S4DS83; -.
DR   OrthoDB; 169741at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IEA:InterPro.
DR   CDD; cd17719; BRCT_Rev1; 1.
DR   CDD; cd01701; PolY_Rev1; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 6.10.250.1490; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR012112; REV1.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1.
DR   PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   PIRSF; PIRSF036573; REV1; 2.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|PIRNR:PIRNR036573};
KW   DNA repair {ECO:0000256|PIRNR:PIRNR036573};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|PIRNR:PIRNR036573};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR036573};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR036573};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036573};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          93..184
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          435..616
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1130 AA;  125183 MW;  F0F6B9E639E25B19 CRC64;
     MNSDSSRSAN SSAQRSKRIL DNSSPSNPSG TGGNKKKRIN QKTLGVAWGA NSISSSRKSP
     FSDFGSYMVE KNRKLHNQFN FDASSASHSG VNSGNQIFQG VSIFVDGFTI PSSQELRGYM
     LKYGGRFENY FSRRSVSHII CSNLPDSKIK NLRSFSRGLP VVKPTWILDS VASNKLLSWV
     PYQLDQLVSN QPRLSEFFSM KKGPTVEKPK ICMTSEKKYE TEDSLSSVAM NLKDTTVLEV
     NESIGYRAEM HSDSVMNLQV NADAEMNEKS SDDLEAAKLK DTSISDVDVS IEYKPHFCES
     FEMLPQKDAD VEVHKGPSNE KYNYVDEEPG IVDVGQSSEE NISSFHGLSA STHNGSSNSY
     HSDGSSSSMA AGSSKLQHST LENPDFVENY FKKSRLHFIG TWRNRYYKRF PRLANGSNSV
     TSHINGSSHH QSATIIHVDM DCFFVSVVIR NIPKFKDRPV AVCHSDNPKG TAEISSANYP
     ARSYGVRAGM FVRDAKALCP HLVIFPYDFK SYEGVADQFY EILHKHCEKV QAVSCDEAFL
     DISGTNNVDP EVLASKIRKE IFDTTGCTAS AGISTNMLMA RLATKTAKPD GQCYIPLEKV
     DDYLNPLPIK DLPGIGHALE EKLKKRSILT CSQLRMISKD SLQKDFGLKT GEMLWNYSRG
     VDNRAVGLIQ ESKSIGAEVN WGVRFKDFKD CQCFLLNLCK EVSLRLNGCG VQGRTFTLKV
     PVATDDLEIL QRIVKQLFGF FVIDVKEIRG IGLQVSKLQN VDISRQGTKR NSLDSWLSSS
     ATTNVENVIG PSVKEVANID NEKQSNSGTL DQLSTDPISH PIQMENNQHH SEALNPVSPP
     PLCNLDIGVI RSLPPELFSE LNEIYGGKLI DLLAKSRDKN EVFSSSIRVL SQGSQGDGLT
     LSDIQGNKVQ SENKISGEGL CNLVAPLTTS GSHRIDLLPS SLSQVDPSVL QELPEPLRDD
     ILKQLPAHRG KELSLEHAVK NHRESGSAVE NTSGSLDPLM ENDLWSGNPP LWVDKFKASN
     CLILELFAEI YTESGLPGNL YGILLRTLSQ SWHPSAADSD GWDGAIYGLC ELLKQYFKLK
     IELDIEETYV CFRLLKRLAM KSQLFLEVFN IIDPYLQGAV NEIYGGSLKV
//
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