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Database: UniProt
Entry: A0A226MV83_CALSU
LinkDB: A0A226MV83_CALSU
Original site: A0A226MV83_CALSU 
ID   A0A226MV83_CALSU        Unreviewed;      1108 AA.
AC   A0A226MV83;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=ASZ78_007695 {ECO:0000313|EMBL:OXB58909.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB58909.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB58909.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB58909.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB58909.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) 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:OXB58909.1}.
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DR   EMBL; MCFN01000434; OXB58909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226MV83; -.
DR   STRING; 9009.A0A226MV83; -.
DR   Proteomes; UP000198323; 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   CDD; cd12145; Rev1_C; 1.
DR   CDD; cd19318; Rev1_UBM2; 2.
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; 1.
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; 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:UP000198323};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          71..158
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          293..506
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          317..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          975..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1108 AA;  121469 MW;  C242448128D367D7 CRC64;
     MLVWDAAEVK SPLPCKASIC VSFSMRRGGW RKRAGESDGW GGWGGYMSAK VKKLEDQFRS
     DSAIQHQRDG TSSSIFSGVA IYVNGFTDPS ADELRRLMML HGGQYHVYYS RSKTTHIIAT
     NLPNAKIKEL KGEKVVRPEW IVESIKAGRL LSHIPYQLYT KQSSVQKGLN FNSICKPEDA
     MPGPSNIAKD LNRVNHIKQC EVESEITPNG ISSWNEEEEE DSDGLGFTEL DQILPGRKLN
     GIQSHKDSTA IFNGHTHNTC TSALKTQDCL GPSSNSVASN VSVASSAKPQ SCIMHVDMDC
     FFVSVAIRNR PDLKGKPVAV TSNRGAGKAP LRPGANPQLE RQYYQNKLLN GKADALFTYF
     AVGNTVVLRQ VGIKNGMFFG QAKKLCPNLQ AVSYDFNAYK EVAQTVYEIL ASYTHNIEAV
     SCDEALVDIT EILTETRLTP DELANAIRAE IKAQTKCTAS VGMGSNILLA RMATRKAKPD
     GQYHLKPEEV DDFIRGQLVT NLPGVGRSME SKLASLGIRT CGDLQCASMS KLQKEFGPKT
     GQMLYRFCRG LDDRPVRTEK ERKSVSAEIN YGIRFTQPKE AEAFLLSLSE EIQRRLEAAG
     MKGKRLTLKI MVRKAGAPVE PAKYGGHGIC DNIARTVTLD HATDSAKVIG KETLNMFHTM
     KLNISDMRGV GIQVQQLVPI SKTTSAQSAV QSGRLPGGSH SVIDLLHVQK AKKCSEEEHK
     EVFVAAMDLE ISSDSRTCTV LPSRGTHLTA GLNSNVNKTD SAVKLNGLHS PISVKSRLNL
     SIEVPSASQL DKSVLEALPP DLREQVEQIY TIQQGETCGD SKREPINGCN TALLSQPVGT
     VLLQVPELQE PNANMGINVI ALPAFSQVDP EVFAALPAEL QAELKDAYDQ RQKQPEQQPA
     NAFVSRNPCL QLKHATTKNK KKIRKKNPVS PVKKIQSPLK NKLLGSPAKT MPATSGSPQK
     LIDGFLKQEG AAAQLEAVPS TSDASDPSAL QTEHSGSFRP QAPNLAGAVE FNDVKTLLKE
     WITTISDPME EDILQVVKYC TDLIEEKDLE KLDLVVKYMK RLMQSSVESV WNMAFDFILD
     NVQVHSSDPS SAAQGTLEAR IILKKRIT
//
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