ID A0A267DA77_9PLAT Unreviewed; 1769 AA.
AC A0A267DA77;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig012441g1 {ECO:0000313|EMBL:PAA46056.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA46056.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA46056.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA46056.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA46056.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:PAA46056.1}.
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DR EMBL; NIVC01005083; PAA46056.1; -; Genomic_DNA.
DR STRING; 282301.A0A267DA77; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 115..248
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 988..1132
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1283..1702
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 205..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA46056.1"
FT NON_TER 1769
FT /evidence="ECO:0000313|EMBL:PAA46056.1"
SQ SEQUENCE 1769 AA; 189913 MW; AD5AA53BADFF42F4 CRC64;
ARSCPAAAMS PAGASAFSMR IVSLETAMEQ PVSGLDVTYS DFRSGQCSRV PVLRVFGSTP
AGRKCCTHVH GVFPYFYVPF EGCSGPRADF LKAFAASLDK AINIAVRRSS SSTVMHVFCI
NVVLGRSFYG FHANESEFMK IHMFNPKMVK KAADLLLGGS VMNKICQPFE SHIPFGLQFL
MDFNLYGMNF LHASVARRRG CLGSDAEEEA NEEPEAEGCP GQAADPSPAP PATHCRVEVD
ISAVDILNRL EVDDNLGSNP GLTALWEEEI ERRQELLGET PPSPPSSAST STAGAARAWV
AAPDSPDREG VEPTESEDKW RRRFRRFLQE RGLINATGFE DEAPAEETAE GAQVADVKSG
LGELADAPSH AEVAEFDAEV VSFTEEDVDD FLNGSANSVD TEPVVDHSTE SAESPGSPVP
PADQDEAPKQ PPPPLVSRAS IDRVVACSQS FLADSSDSSD GSDRDAADAD SADSEATCEE
LASRMLDEFL VRSPSSSQEV GGAAAAAEDP AQVEAELNDS QRDLFAVEDY EDDNEDEEQQ
DEHRDEAEEA AGQLDAATLL QFVRLEEQDS VLAVAFDGGS DSDDEDDEDE EAGDEAGISG
PPQLDGALSS SDDSSSAGGG DDDGDFDESP CRSSARQRQG RAPQPPPPPP ARRGRRLGLS
MASRPAAGSA AAASSMSSKS PPGPTVSSKA FKPVAFRVGS GSGLSGRPML LGKRRSVAPP
SPPSPPSQPP PSSPPPLPPQ PATTQSPSSA SSLIFSQSLE LASFTTSGQR LPTSTQQHQQ
RLESSRSNQA SSNTQHLLGP NSPEPPSTLP KRQPAMAHVY APLVAPPTAS EVADSLDSFG
LFPCRNPPLR PDAAGVDDLR QFDSLAVGVA GLASFDRASA LAAASVSMST STAPLLRYRP
LIDPPSRDLV ARSLKAAAAS AADKLAKPAA ESATAAAEAT VDDAFDTVSN SSSHRAYPRP
AAAIGGIGRK ELLARIKAKV RRSLSETSAM SSSSTSMSTS AAAATTAAVV GDGLTLASLE
VATAARPGLL PDPRHDAIVA AFLTVADASE ANPTAWRQHC LFVAATDAEA DRRIRGFASA
ATRFQAVRDE AALLEALADT VRCADPDIVL GFDTQRASWG YLIDRAKQLQ GPPESGGGGL
PMAQLLSRYR LLPHQQQHRR RREPEANCSS QSQQPEDGLA GSYEAQSDSL RIGGRVVINL
WRLLRYELSK LRSNSFEACA ALVLNRRYPC YSSDVLWRMW QDGRDSWRVV EHLETRSCGS
LRMLSTLGLV SRTAEFARVF GIEFYHVLSR GSQYRVESMM LRLAKPLGLL PLSPSVQQRA
RQAAPDAIPL TLEPRSGLHT DPVVVLDFQS LYPSIMIAYN YCFSTCIGRA ASITTCDPMA
YEFGCHRLMT DPGAYQRAAG HLNFSPLGIG FVDASVQRGV ISRMVEEILA TRLMVKAAMK
RYGGNEPLLK LLDARQLGLK LIANVTYGYT AASFSGRMPC VEVGDSIVRK ARETLERAIA
LVQAEPSWRA QVIYGDTDSL FVLLPGRSRR EAFEIGQAMA RAVTAVNPKP VKLRFEKVYQ
PCLLLTKKHY AGFMYETADQ LEPTFDAKGI ETVRRDSCPA AGRILGRSLR ELLSSLDLSR
VRRVVEFELH RLHWGRSPLQ ELIIAREHRG CRNYSERAAV PGLAVVRRRL AADPRAEPPL
GYRVQFVVVR PSQPGQGLCA RARSPRSFWV LPVAGPADPS ASTGTIMPAN RFCRRSTAPC
RCSASTSSRG TPAWRSPAPW RASESAAAP
//
