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Database: UniProt
Entry: A0A1R3GYW1_9ROSI
LinkDB: A0A1R3GYW1_9ROSI
Original site: A0A1R3GYW1_9ROSI 
ID   A0A1R3GYW1_9ROSI        Unreviewed;      1072 AA.
AC   A0A1R3GYW1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=COLO4_32578 {ECO:0000313|EMBL:OMO63318.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO63318.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:OMO63318.1}.
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DR   EMBL; AWUE01021134; OMO63318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3GYW1; -.
DR   STRING; 93759.A0A1R3GYW1; -.
DR   OrthoDB; 169741at2759; -.
DR   Proteomes; UP000187203; Unassembled WGS sequence.
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; 1.
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; 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; PF21704; POLH-Rev1_HhH; 1.
DR   PIRSF; PIRSF036573; REV1; 1.
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:UP000187203};
KW   Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          91..182
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          389..570
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  118847 MW;  74BF5B4B739413F2 CRC64;
     MSLDSSRSAN SAPQNSKRSF NSNSSNNNSK KRKSNQKTLG MAWGANSLSS SRSSFRSSPF
     SDFGSYMVEK NRKLQHQFDS EASNSSHSDS STKPIFHSVS IFVDGFTVPS SQELRRYMLN
     HGGRFENYFS RHRVTHIICS NLPDSKIKNL RSFSGGLPVV KPAWILDSIA ANRLLSWVPY
     QLDQLASNQP TLSAFFTPKI SPASEGAFTN AICEVKYETD DLCLKDALKD VKSFEAGESS
     ELRNKITEEH DSLMHENSNA QVIEEPSSSY SEESGEVKVV EPSNLQEDDE RMENNGLQSS
     PEQPSASVSS HCFDNDSIKG SSRSTTSEPL KQRHSTLGDP NFVENYFKNS RLHFIGTWRN
     RYRRRFPSLS NGCKKPRSEV SVDTQKTPVI HIDMDCFFVS VVIRSRPELH DQPVAVCHSD
     NPKGTAEISS ANYPARDYGI KAGMFVRDAK ALCPQLVIVP YNFEAYEEVA DQFYNILHNH
     CNKIQAVSCD EAFLDVTDSE GKDPQVLASE IRKEIFEATG CTASAGIAGN MLMARLATRT
     AKPNGQCYIH PERVDEYLDQ LPIKALPGIG HVLEEKIKTK NIRTCGQLRM ISKDSLQKDF
     GIKTGEMLWN YSRGVDNRLV GMIQESKSVG AEVNWGVRFR DLQHAQHFLF DLCKEVSLRL
     QGCGVQGRTF TLKIKKRRKD AGEPAKYMGC GVCENLSHST TVPLATDDVE VLQRITKQLF
     GFFHIDVKDI RGVGLQVSRL ESADTSKQGK NVGGSSDVLD TDQVGDSVHR TNSTSIGEGC
     SNQISTVPPL CHLDMGVVES LPSDLLSELN EIYGGKLVDL IAKSKGQGED SYSSLCILPP
     ELARDQAESS HNSGPDSLIR TAVQMKDKQH ISEELQTVPE SGAGSNSVAI SVPGDLMPSS
     LSQVDTSVLQ QLPEELRADI FELLPAHRRP EISTMGPNAD DLHHPLGNNS TDNQPGSSGS
     RLSTDLWIGN PPLWVDNFKI SNSLTLKFFA DMYYKAKSAD NLSSILQCTI SQSLHALDAR
     CDAWSEAVHS FSELLMGYIK LKIEVDIEEI YVCFRLLKRY EVSIVEEDKI SS
//
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