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Database: UniProt
Entry: A0A3B4GB87_9CICH
LinkDB: A0A3B4GB87_9CICH
Original site: A0A3B4GB87_9CICH 
ID   A0A3B4GB87_9CICH        Unreviewed;      1147 AA.
AC   A0A3B4GB87;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=DNA repair protein REV1 {ECO:0000256|ARBA:ARBA00020399, ECO:0000256|PIRNR:PIRNR036573};
DE            EC=2.7.7.- {ECO:0000256|PIRNR:PIRNR036573};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000018886.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000018886.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4GB87; -.
DR   STRING; 303518.ENSPNYP00000018886; -.
DR   Ensembl; ENSPNYT00000019361.1; ENSPNYP00000018886.1; ENSPNYG00000014241.1.
DR   GeneTree; ENSGT00940000156374; -.
DR   Proteomes; UP000261460; 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   CDD; cd12145; Rev1_C; 1.
DR   CDD; cd19318; Rev1_UBM2; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 6.10.250.1630; -; 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   Gene3D; 1.20.58.1280; DNA repair protein Rev1, C-terminal 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; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR012112; REV1.
DR   InterPro; IPR031991; Rev1_C.
DR   InterPro; IPR038401; Rev1_C_sf.
DR   InterPro; IPR047346; Rev1_UBM1/2.
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; 2.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF21704; POLH-Rev1_HhH; 1.
DR   Pfam; PF16727; REV1_C; 1.
DR   Pfam; PF14377; UBM; 2.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          40..112
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          358..595
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          147..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1036
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1147 AA;  126186 MW;  175139F5F2ECB4A9 CRC64;
     MSRDGWMRKR ANGGYMAAKV SKLDEQFRLD APREKQKEGA CSSIFTGVAI YVNGYTDPSA
     DELRRLMMLH GGQFHVYYSR SKTTHIIATN LPNSKIQELK GEKVIRPEWI TDRSVHCKLI
     MFIFHILLNR NLQTSVDVSH SKMNEIQECS KEEPHLAGAS DVKDAPLTNG HTHIVNGALN
     SEDLSPQSSS QRANEKRLKP PPPTYQEAIK ATESHLFPKQ LQAPLQVDMI SEKTLSPASR
     SLSHSPVRLN GSHHNAFTSD SASLSTNNVT FKSEPPMDES SSSSSNLISE FYSHSRLHQI
     STWRSGFSEY VNELHSKRKG AGGASLPGKE RLRKSAAQRS IDTKAGDLGS QVSVKSCILH
     VDMDCFFVSV GIRNRPDLKG KPVAVTSNRG QGRGPVRPGA NPQLEMEYYQ KKYTHPQAED
     EIHTTPSQES PDSRTNGVEQ DAVALSMAEI ASCSYEARQA GVRNGMFFGK AKQLCPALQS
     VPYDFEAYKE VALNMYETLA SYTHDIEALS CDEVLIDGSA LLAEVGASPE DLAKAVRADI
     KEKTGCCASV GMGSNILLAR LATRKAKPDG QYFLKSEEVD DFIRDLPVTS LPGVGPVMGR
     KLALMGVRSC GDLQQVSLSK LQKKFGPRTG QTLFRFCRGL DDRPVRYEKE RKSVSAEMNY
     NIRFTRVDET ECFLTNLSME VQKRLQEASL RGRRVTLKVM VRKIGAPLEP AKYGGHGICD
     HLAKTVMLAQ STDSGQLIAA AVIKLFHAMK VEVQDLRGVG IQVQLLEGHQ SATQDCRGLR
     GRSIKEMLLG QASSARSNNR DALQEKTTSS TTVPTANSAP YPLSPAEPVP GTSKEQPACR
     QTPKHSRTRL NFSIEVPSPS QVDRSVLEAL PAELREQLSP LISHPASPPR PPLATVPALN
     YPPVGTLVLQ IPNQPESPGI VLELPNFSQV DPDVFAALPK ELQEELKAAY SRATGIHPQQ
     KNPLLQLKQS GAGIGSGRVK RRYKRKNAVS PLKKGASPLK KRPTTNSPAK SLPPTGKSQE
     PINNRKTENG PSTSVSKPEI PPAVVKLAAR PPPALAGACD LTDIKTLLRE WVTTITEPME
     EDILQVVKYC TDLIEDKDLE KLDLTMKYMK RLMQQSVESV WSMAFDFILD NVQVVLQQTY
     GSTLKIA
//
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