UniProt: M2XIU4

Database: UniProt
Entry: M2XIU4_GALSU

LinkDB:  M2XIU4_GALSU 
Original site:  M2XIU4_GALSU

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   M2XIU4_GALSU            Unreviewed;      1070 AA.
AC   M2XIU4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=Gasu_26090 {ECO:0000313|EMBL:EME30022.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30022.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KB454503; EME30022.1; -; Genomic_DNA.
DR   RefSeq; XP_005706542.1; XM_005706485.1.
DR   AlphaFoldDB; M2XIU4; -.
DR   STRING; 130081.M2XIU4; -.
DR   EnsemblPlants; EME30022; EME30022; Gasu_26090.
DR   GeneID; 17088781; -.
DR   Gramene; EME30022; EME30022; Gasu_26090.
DR   KEGG; gsl:Gasu_26090; -.
DR   eggNOG; KOG0969; Eukaryota.
DR   OMA; CNNCRPR; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05777; DNA_polB_delta_exo; 1.
DR   CDD; cd05533; POLBc_delta; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   NCBIfam; TIGR00592; pol2; 1.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          144..442
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          506..935
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          972..1045
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
SQ   SEQUENCE   1070 AA;  121516 MW;  4DB4D5121B26B21A CRC64;
     MDSSASPIDD DSIIQESLLY DSEKQEILEP VEYTQTRSKF QHLFSSYARA GSPLLFGEDA
     GNLRILQLDV DYEIVQKDTF LEDSSSAAVL RIYGVTEGGN SVLARVHGFR PFFFIICPSQ
     FDPADLPAIK ESLEKRARAV SSMKNCQGPI IHDLEIFEGR SLLYFVPSDP LIRFLKITVA
     LPSYVRQLAQ ILERGDIDFS PYEESRYSTF EASVDFILRF MIETNMYGCS WVEMPSNRYH
     LPEKQTSHMQ FEIDIHYTHL VCHAPHGEWL KTAPIRILSF DIECAGRPGV FPEPEHDQVI
     QIANYMTETG KSEPIARTVL TLGSCAPIAG AKVLSFDSEA ELLEAWVSFL CATDPDILTG
     YNIVNFDLPY LLNRASVLHL SSFPFLGRLM GVMTKMHDTR LSSSAFGTHE SKAFTMNGRI
     IVDMLQILVR DYKLRSYSLN SVSFEFLGEQ KEDVHHSIIT ELFHGNENTR RRLAVYCLKD
     AYLPHRLMEK LMSLTNYMEL ARVAGIPLAW LLSRGHMIKV VSLLHRKAFP ESLLIPDLKN
     TSHNSSEEAE SYEGATVIEP KRGFYKMPIA TLDFASLYPS IMMAHNICYS TLVRKDRVKY
     LKPEDYIKSP SGDCYVRPSV KKGVLSKILE DLLSARKVAK RELEQATDPF LRSVLNGRQL
     ALKISANAVY GFTGASRGKL PCTEISASIT AFGRRMIETT KSLVESKFPS SVVIYGDTDS
     VMVKFRDDLT LEESMSLGQQ AADIISQSFP KPIKLEFEKC YYPYLLIQKK RYAGLLWTKT
     ETYDKMDCKG IETVRRDNCK LVANVVSKVL EKLLVERDVQ GAIDFVKKTI SDLLQNKVDI
     SLLVISKELS KAAADYDANQ AHVTLYKKLY QRDPGSAPSL GDRIPYVTIK GRKDQPAHER
     AEDPIYVLEH NLPLDTEYYL KNMLRKPLER IFEPIIGKNV SSLFEGEHTR SITVTTPSTG
     GIMRFTKVSV TCLGCRTPIP QTESKEPLCK YCKANEASIY EKILCNVREY ERQYAMLWTQ
     CQRCMGSICQ DVLCSNSDCP IFYRRRKVQK DLEDTSKQLE RFEILPPPSW
//

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