REV1_PONAB
ID REV1_PONAB Reviewed; 1250 AA.
AC Q5R4N7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=DNA repair protein REV1;
DE EC=2.7.7.-;
DE AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN Name=REV1; Synonyms=REV1L;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with the DNA polymerase zeta which is
CC composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and
CC requires that REV3L is in its closed conformation. Interacts with POLH,
CC POLI and POLK. Interacts with FAAP20 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; CR861208; CAH93279.1; -; mRNA.
DR RefSeq; NP_001126930.1; NM_001133458.1.
DR AlphaFoldDB; Q5R4N7; -.
DR BMRB; Q5R4N7; -.
DR SMR; Q5R4N7; -.
DR STRING; 9601.ENSPPYP00000013486; -.
DR GeneID; 100173947; -.
DR KEGG; pon:100173947; -.
DR CTD; 51455; -.
DR eggNOG; KOG2093; Eukaryota.
DR InParanoid; Q5R4N7; -.
DR OrthoDB; 299766at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:InterPro.
DR Gene3D; 1.20.58.1280; -; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.10190; -; 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; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA synthesis; DNA-binding; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..1250
FT /note="DNA repair protein REV1"
FT /id="PRO_0000284127"
FT DOMAIN 44..131
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 419..652
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 204..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..362
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 652..655
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 708..716
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 1034..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1250
FT /note="Protein interaction domain; mediates interaction
FT with DNA polymerase zeta"
FT /evidence="ECO:0000250"
FT MOTIF 1071..1077
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 271..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1081
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 423..427
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 509..515
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT SITE 769
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 782
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1250 AA; 138304 MW; 62B55F77603E0551 CRC64;
MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT
DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
GRLLSYIPYQ LYTKQSSVQK GLSFNPICRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE
VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD
CLVPMVNSVA SRLSPASSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL
SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH
ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSLL NSPRHQSCIM
HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAD
IPDSSLWENP DSAQADGSDS VLSRAEIASC SYEARQLGIK NGMFFGHAKQ LCPNLQAVPY
DFHAYKEVAR TLYETLASYT HNIEAVSCDE ALVDITEILA ETKLTPDEFA NAVRMEIKDQ
TKCTASVGIG SNILLARMAT RKAKPDGQYH LKPEEVDDFI RGQLVTNLPG VGHSMESKLA
SLGIKTCGDL QYMTMAKLQK EFGPKTGQML YRFCRGLDDR PVRTEKERKS VSAEINYGIR
FTQPKEAEAF LLSLSEEIQR RLEATGMKGK RLTLKIMVRK PGAPVETAKF GGHGICDNIA
RTVTLDQATD NAKIIGKAML NMFHTMKLNI SDMRGVGIHV NQLVPTNLNP STCPSRPSVQ
SSHFPGGSYS VRDVFQVQKA KKSTEEEHKE VFRAAVDLEI SPVSRTCTFL PPFPAHLPTS
PDTNKAESSG KWNGLHSPVS VQSRLNLSIE VPSPSQLDQS VLEALLPDLR EQVEQVCAVQ
QAESHGDKKK EPVNGCNTGI LPQPVGTVLL QIPEPQESNS DTGINVIALP AFSQVDPEVF
AALPAELQRE LKAAYDQRQR QDENSTHQQS ASASVPKNPL LHLKAAVKEK KRNKKKKTIG
SPKRIQSPLK NRLLNSPAKT LPGACGSPQK LIDGFLKHEG PPAEKPLEEL SASTSGVPGL
SSLQSDPAGC VRPPAPNLAG AVEFNDVKTL LREWITTISD PMEEDILQVV KYCTDLIEEK
DLEKLDLVIK YMKRLMQQSV ESVWNMAFDF ILDNVQVVLQ QTYGSTLKVT
