UniProt: I0Z2H6

Database: UniProt
Entry: I0Z2H6_COCSC

LinkDB:  I0Z2H6_COCSC 
Original site:  I0Z2H6_COCSC

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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)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   I0Z2H6_COCSC            Unreviewed;      2034 AA.
AC   I0Z2H6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=COCSUDRAFT_41124 {ECO:0000313|EMBL:EIE24845.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24845.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE24845.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE24845.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
CC   -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC       replication. {ECO:0000256|RuleBase:RU365029}.
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:RU365029};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU365029};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
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:EIE24845.1}.
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DR   EMBL; AGSI01000005; EIE24845.1; -; Genomic_DNA.
DR   RefSeq; XP_005649389.1; XM_005649332.1.
DR   STRING; 574566.I0Z2H6; -.
DR   GeneID; 17042846; -.
DR   KEGG; csl:COCSUDRAFT_41124; -.
DR   eggNOG; KOG1798; Eukaryota.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR   CDD; cd05535; POLBc_epsilon; 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; 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; 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; IPR013697; DNA_pol_e_suA_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR029703; POL2.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR   PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08490; DUF1744; 2.
DR   SMART; SM01159; DUF1744; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365029};
KW   DNA replication {ECO:0000256|RuleBase:RU365029};
KW   DNA-binding {ECO:0000256|RuleBase:RU365029};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU365029};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW   Metal-binding {ECO:0000256|RuleBase:RU365029};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU365029};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365029};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW   Zinc {ECO:0000256|RuleBase:RU365029};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU365029}.
FT   DOMAIN          1474..1782
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2034 AA;  228187 MW;  201AFF5A329D8C1D CRC64;
     MQGGSSGATP AFEDSRPKNE DNHELEELLG FPLIKEGTRL GWLMNLNSTT LEEKESGNTV
     AAVNCYFMSQ DGSMFKAQVP FSPYFYLQIK GDMEAEVDAY LRRKYTTAIR DVETVFREDL
     DLKNHLSGLK RKLLLVSFWT VQQLMDVKRD LMPALRRNRS KAATTDAYSA FAQDAQKPGA
     NRLQDALDAL VDMREYDVPY HMRFQIDTDV RCGLWYDVRA KGGKVSLEPR PDLLQRAEPR
     ICAFDIETTK LPLQFPNAEY DQVFMISYMI DKQGYLIINR EVVGGDIENF EYTPKPEFEG
     PFVVWNEANE EATLRRWFDH MRQVKPAVYV TYNGDFFDWP FIETRAAKLG MDMHEEIGFK
     MNSKTHESAV HMDCMHWAVT RAKLGYNPIE VDPEDMLRFA AEQPQTMASY SVSDAVATFY
     LYMTYIHPFI FSLSTIIPMP PDEVLRKGSG TLCEMLLMVQ AFQANVVAPN KHTQVQEPMF
     RGHLLESETY IGGKELIDSL DTDLRYAIEV EGKLAMDDVE NYEEVRDAIR ASLEGLRDTP
     NREECPLIYH LDVAAMYPNI ILTNRLQPSA IVTDEDCAAC DFNRPGKTCL RKMTWEWRGE
     TFSATSAEYF SIKNQLESER FAPETEGGPP RYYGQLPHEE RAKLLKERLK KYCQRVYKRV
     LDKPVTEARE AGVCMRENDF YVGTVLSFRD RRYEYKGLNK TWKGKLDAAK AEGNPIRVQE
     AADMVVLYDS LQLAHKCILN SFYGYVMRRG ARWYSMEMAG VVTYTGARII QRAAELVRKI
     GTRLELDTDG IWCALPGSFP ENFKLKSRKG KDLRISYPCV VLNVMVAQHN TNDQYQTLLE
     GDSKHYETSS RMSIEFEVDG PYKAMILPAS KEEGKLIKKR YAVFNPDGTL AELKGFELKR
     RGELKLIKVF QSEVFEQFLA GDTLEECYAA VAAVADRWLD LLDTQGTDVT DEELLEYISE
     SSTMSKAMDE YEGRKSCAIT TAKRLAQFLG DERIKDKGLN CNYVIAKRPE NQPTSERAIP
     VAIFSTEPSV ARSFLRRWCG HLSSGRGADE VPDVRAIVDW DYYRERLGSA IQKIITIPAA
     MQRVPNPVPR VKHPDWLHKK VREKEDRHQQ QKMDGFLRPR AALEAAASPS AADVDMEDMG
     VARPAAGASG QRVAKATTVQ RRPEADRENR GDARNRPAGT SGAADDEEEE EDLGPCPNRK
     EDPVGWLRHQ KRRWRTAAAA RKKRRIDTAR ERDRGQGSNP QPAPRGVFKA WVLVGARLYA
     VPLRVPRTFY VNSTRVPTDA DSPAQTLGGL KVQRSLPFGR EPFHLYQVTM AEDEFRRRDA
     EIAVVLSQPH VRDVWEERLP LALDAALSVG CVASVAPAVR SRPLSDGFDL TDLQARGTKT
     TTECSYLEAQ APDGGSLLRH VALYTSQDTA RGRAVYGLHL PPTKKCLLVV VNPAAGAGSR
     EVSVPATKRH WREAHVSGPA APDEGAGGAS QPIEIPEVEF EIAYVRTTAE AARAVQNALL
     QLRERHRGPL MVVAEAPGGT ARLTRDMPLL AEFPTCQVPA HSADGAYPSL GWQPKAARTA
     VMRLAGAALW FQDRIELARY AHLPLGNLGG DWMLDVADAH LARCLRDAGH LLWISDPALP
     DVAGRADDDA EEDALISEPA PLEVVAPGAH RSVCVQLKLY HLAVAAVEKF SDALLTNLWR
     WLCSPAAALA CSGLQRTVMG LMRKTLAQLV ADLKRLGARV VAADAHSLIL ATGKHNLTAA
     VGYVDYLLDA VGKRDLFSLL KMDPERFWHS LLFRDRYNYL GILADIPAQL QESLTNHPGA
     LTQGGAAELH VPEPDEDALE SPALDYIWTI KDYLPPKAVT EARGAAAAQE AWLKANMAAH
     FSRKLLGVED LGTPALAFVR AVCDALRLDA SIEEEVLVLR RNLLLLTHTL EFAPAAEFQE
     PCRSFVLRNE HQWSCRNCGC AYELATVEAQ LLRAVRLRAR AYQLQDLRCL KCRQVLRGHL
     RRNCDQCGGA LANTEPAAAF TEALTVFRNV ATYHGFQLLQ DATEWLLQMP SAAH
//

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