UniProt: S4RCM4

Database: UniProt
Entry: S4RCM4_PETMA

LinkDB:  S4RCM4_PETMA 
Original site:  S4RCM4_PETMA

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
All databases (27)   

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ID   S4RCM4_PETMA            Unreviewed;      2299 AA.
AC   S4RCM4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000002956.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000002956.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|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}.
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DR   STRING; 7757.ENSPMAP00000002956; -.
DR   Ensembl; ENSPMAT00000002970.1; ENSPMAP00000002956.1; ENSPMAG00000002616.1.
DR   GeneTree; ENSGT00390000010194; -.
DR   HOGENOM; CLU_000556_0_0_1; -.
DR   OMA; MLDQCRY; -.
DR   Proteomes; UP000245300; Unplaced.
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; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR10670:SF1; 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; 1.
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:UP000245300};
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          1524..1937
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1955..1984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2029..2056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1962..1984
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2042..2056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2299 AA;  259981 MW;  2C5D52291AEB8FA3 CRC64;
     PSSPTTVSAD DGGPQSAARR LERSRQVDEM DLKFGFVRLR DPGEHTGWLI NMHPTDILDE
     DKRLTSAVDY YFIREDGSRF KVALPFKPYF YVATKKGCER EVSSFLSRRF QGKLSGIEMV
     AKEDLDLPNH LVGLKRTYIK LSFITTEDLI KVRKDVFPAI RKNREREKSN DAYTSMLSSA
     LSGGNLLAED EGNSKKMSDQ MENITDIREY DVPYHVRVAI DLKIHVAHWY NVRIRGSAFP
     PEITRRDDLV ERPDPVVLAF DIETTKLPLK FPDAETDQIM MISYMVDGQG YLITNREVVS
     EDIEDFEFTP KPEYEGPFTI FNEADEAGLL QRFFDHLHET KPNIFVTYNG DSFDWPFVER
     RALAHGLDLL IETGFQKDSQ GEYKATQALH MDCLRWVKRD SYLPVGSHNL KAAAKAKLGY
     DPVELDPEEM CRMAAEEAQT LATYSVSDAV ATYYMYMKYV HPFIFALCTI IPMEPDEVLR
     KGSGTLCEAL LMVQAFHANI VFPNKQQEEF NRLTGDGHVL DSETYVGGHV EALECGVFRS
     DIPCRFKMNP GVFEELMEKV ETTLKHALEE EEKIPLDKVN NFSEVCEEVR SKLRALQEVP
     SRIECPLIYH LDVGAMYPNI ILTNRLQPSA MVDEATCAAC DFNKPGASCQ RRMAWQWRGE
     FMPATRSEFH RIQQQLESEK FPSMFPGGPP RAFHTLSRED QAKYEKKRLA DYCHKAYKKV
     RVTRMEERMT TVCQRENSFY VDTVRAFRDR RYDFKGLHKV WKRKLGSAAD SGDAAEVKRC
     RNMEILYDSL QLAHKCILNS FYGYVMRKGA RWYSMEMAGI VCHTGANIIM QARELVEQIG
     RPLELDTDGI WCALPSSFPE NFIFHTSSAE KPKVTVSYPG AMLNILVKSG YDKNMFTFWK
     LCQPKQIKPT TFTNKTLIFS GYPISIAILL TSSRKRVSHL QVFFKWYAVF NEDGSLAELK
     GFEVKRRGEL QLIKIFQSSV FEAFLKGSNL QEVYAAVAKV ADYWLDVLYS KAANMPDQEL
     FELIAENRSM SRKLEDYGAQ KSTSISTARR LAEFLGDQMV KDAGLSCRFV ISRRPEGAPV
     TERAIPLAIF QAEPSVSKHY LRKWLKSPSQ QDFDIRSILD WDYYIERLGS AIQKIITIPA
     ALQQVKNPVP RVRHPDWLHK KLLEKSDAYK QKKINELFTA SEKRQLTVKV SGQQAGAASV
     EDMEDFGASQ LTPLGPVPMA TKRKRAEVES QDRESQDLEL TQTWREILGP PPSIGTTAEE
     MATWIRFHKK KWEIQTRQRK DRSKRRRCGS GEGGPTTHGA RGPLRGGGAL NTGLGGFLMR
     AARSLLSTPW QIVQIAEGTQ AGMFRVWCVV GTELHVVKLH IPRIFYVNQR VAKPDEGPNY
     RKVNRVLPRS NPVLNLYEYT VAEELYQQHL NQINADLAAP HIEGVYETQV PLMFRALVQL
     GCVCTVSRES ARQQGALDVD TFQLEQLEMR SLAQYSYLEP GTIRHMYLYH CSQGSKALLG
     LFIPTQRKAS VFVVDTVRSN QMPNLGVVFT AERAALLASL GEELLPPPEH GFEVRVETDL
     KQAYRGLQRL LLSYKDSRKG PTLVAVESAW PSQRVRSAMP VLDNFPVVWV GGAGATSPAG
     PADDPPSLSV LDWQRQGGRH MVRAYLRVDS TLARMFDVAR YLHVPVGNLP DDVEAFGCDL
     FFARHLRRNN HLLWLSATGR PDLGGKEADD GRLACDTRDA KSFHISCPSA YHAVCAELDI
     QSLAVNAVLQ SHHINDLEGG ASGGVSFDSA PQASLADMMT SGTSSNTALA SYDEAALCSN
     TFRVLKGMVV GWVREISRFQ NAYADNQVTH FHRWVSSPAS LLYDPALHRT LHTAMKKLFL
     QCRLISEFKR LGSQIVYADF NRIIVCTRKH HIEDAIAYME YVTRSINSRE IFHSISISYS
     RCWETLLWLD SCNYAGIVGQ LPPALLEKIR KRKPSDGSNV EIDYECSEEE DDGNEDGGDD
     EEDALDESRL DNHWNLALFL PQAASCQTYF LTIVTAYIMA VYHSLQEEMK RNEPGDTPVK
     RRGHGSQSTQ AANKDGLPGT TSFCQEYVAG ELTHNLFTIT QKIQRRVTGR RNADGLSPLF
     PELPGSHLPL ANPALEFASF VCGVLSLDGA VALQVSKLRR DLLRLLDVGE FSSDAEFRDP
     CLSLVLPELI CHHCNYCRDI DLCREPALAQ DGSVLPKWQC TNCSADYDVE QVQAALVETV
     QKKIMSHVLQ DLVCEKCKGV KEANMPAFCD CAGDFQLAHP AQEFVEQLKV FRNIARHYAM
     PFLLETVNWI LQGSSVVGH
//

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