ID A0A3P8WNK5_CYNSE Unreviewed; 2626 AA.
AC A0A3P8WNK5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=REV3L {ECO:0000313|Ensembl:ENSCSEP00000027096.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000027096.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000027096.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000027096.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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DR Ensembl; ENSCSET00000027461.1; ENSCSEP00000027096.1; ENSCSEG00000017283.1.
DR GeneTree; ENSGT00940000156226; -.
DR OMA; DPTSWIR; -.
DR Proteomes; UP000265120; Chromosome 7.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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:0019985; P:translesion synthesis; IEA:InterPro.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR CDD; cd22287; REV3L_RBD; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR032757; DUF4683.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
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; 1.
DR Pfam; PF15735; DUF4683; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 397..846
FT /note="DUF4683"
FT /evidence="ECO:0000259|Pfam:PF15735"
FT DOMAIN 1866..1978
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 2044..2495
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 2538..2605
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 91..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1626
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2626 AA; 294875 MW; A8E74AD07396F309 CRC64;
MWPPGEKSLT ARALSLWRSL YKYHAYIYTE RQVGPSNAAM SSCFSYLFFF VFFCADNSQD
NAIIDLLAGL EDDGFYRTPV RPNFQSQSFT GARSYQYNSD EEEEGPDLEK EESELSVLMS
QRWDTEETVG PSLPRSALQE TEDSFSEEQR ESSDEDMEWS GENSQFINLS IPQLDGAADE
NSDSSLTDNS SSSQSSPITT EKMLGKGNLL PGETIQFDPP TSANILLKCT HSDHRPGHPL
DAEQQLEMHR ESKSAQDGGS ECSSGLKLNK QIPYIPPVKH PIPCKMPNHD APPACVKSED
IRPLYTFDKK NTINLEDTGG QTFSFSKRRQ PMYSGTKNVE TDCLSILQNH RTFSLCYSEL
RNGTSKTELE FSQKDRKSPI LMNISSSLST LDEDGFLGRQ AKEIAEENEE GDVGELKIRY
EDYQENKSES TIVAQQEAHY KFFPSVILSN CLRRKKVGSK KLIEKNDSVG KLVEAQPCRS
RLKLNKKKLG ITGQRNSPSP VEDLTVDSDV SSSLTPQNVE TEAEMSSLVQ NGETEAEMSS
LDVNSEKDEP GKEGIFTEVK IAEEEVESAQ KPAIEGTETL VEMSSSDSPT VSCLSEETKI
PVESRWDFLE DESPKVSGSK HPALFNSKYT LRAKRKMIYD RVNKEDSVST RSTKPNLDSK
QKDGNVIIRQ DVKYQKRRKK DPPIIIKYII INRFKGQKNM LVKMSKINAN ERSVLLTPER
LSLYNKIAPL KDFWPKVPES TAVRFPVIEP KVKKQSKRKT RVNYSTKKSV SNTYKPQVKQ
GRRASGTKDH VKGLRLASLP PPLPCYGELA EDHDTEYNDV MAELGYLSER SQSPTDLTPP
RCWSPSEPSM ECPEQQIIPN RKAGFVGSSI KQNKRQAARI PKSTDRKRKI KPSLGEEEPR
KEHFMQNHKR SAFRQRKKAK DDPKGVVSVT PTTSKMKRPR KKTKSTSDSS QFLSQKDDPP
PSEMFSEEVP TFQQPVNNDD GRTCPQSTLM ESKLVAQSVQ TKVDECETSV MEVNLSFTPQ
VQVKEEGCQT TAIKVESSQV ECTAPPLGDL VGEEDRKNAQ TKSFLSTGLS VGELPSGLNV
LRQLLQKRQQ AQTLQTQTVG TDGHKGPAPS IKRAKSRKVL STTPKRPKAQ KSTTPKTGKP
TTKTVARSST QTNLCMMHKD NLSDDEVLVF SEPGLDTCTL MEDSLSPELP HNYNFDINAI
DQSEFSNSYG GSQFVLTDKI LPAKFLSEVS QEADPAQMQS SAKKFDWQKR KPLSLELLDA
SENVELVSNP LNSERNEKKD WEFSPCKSHT LSPFQDFYCE RKELLFSILD PVAPLPLSSA
SFVDHEGSAL GDPLEGIDGL TSTTPSSSPR SLSSPSQVRP SQLMRGMGGG AHILKPLMSP
PSQDEIVNSL VNFEISEATY QEPFCSDPSD APGKPMEIGG CRLVVGTRLA NELAEFSGDF
STEGLLFWKT AFSAMTHPAT VTSPSRTKGV EDSKPIKDQA EAKSTSTKDS KIILLPCKNP
PNQDVVRLWL EAKKQYECLR KMRKDRELPE NTRAASDDEE KTANRTSTPT ASPCSAVKVE
LSGNVSATRV QRQGNRRNSL FTSSARNAGF QSVASQPCQG LDKSDVDCKH EKQEEEEDED
DDEIPDLPPW QESRQQSPSS PHSQSENKQS ENSLELLSPN PCSSFDRLGN YFSPLTPRAG
RKEEEDSGSP RLLHSTPFLS QRAKELKPEC GTPITAETPA SQRLQQRRRR CTGPMRRVLL
TTQMQNQFAA VNVPKKENSQ IEGPSIGNSY GFKLSIHNLQ EAKALHEVQH LTLMAMELHA
RSRHDLEADP EFDPICALFY CLSSDAALPG GDSTVITGAI VVDKDHQSSV QGDKSRAPLL
IRSGISGLQV DYATDEKMLF QQLICVIRRF DPDILLGYEV QMHSWGYLLQ RATAVGVDLC
QQLSRVTDDS KDNHYTADRD EYGADTMSEI HIIGRVTLNL WRVMKTEVTL NNYTFENVAF
HVLHQRFPLY SPRTLSDWFD HSTDLYRWKM VDHYMSRVCG IMQLLQQQDI IGRTSELARL
FGIQFLHVLT RGSQYRVESM MLRVAKPLNY IPVTPSTQQR AQQRAPQCIP LVMEPESRFY
SNSVIVLDFQ SLYPSIVIAY NYCYSTCMGH VDSLGMSDEF KFGCSSLRVP PELLHQLRND
ITVSPNGIVF VKAAVRKGVL PSMLEEILNT RIMVKQSMKS YKQDKALTKL LHARQLGLKL
IANVTFGYTA ASYSGRMPCV EVGDSIVHKA RETLEGAIKM VNDTKKWGAR VVYGDTDSMF
VLLKGATKEQ AFKIGHEIAE AVTATNPKPV KLKFEKLYLP CVLQTKKRYV GYMYESLDQK
DAVFDAKGIE TVRRDNCPAV SKVLERSIKL LFETRDISQV KQFVQHQCVK VLDGRASMQD
LTFAKEYRGS GSLQPRDCVS ALELTRQMMA YDRRLEPRVG ERVPYVIVYG TPGVPLIQLV
RRPMDVLQDP SLRLNATYYI TKQILPPLVR MFQLIGVDVF SWYHELPRIQ KASCSSAMKG
EDAGRKGTIS QYFTTLHCPV CDQLTQLGVC SSCRTEPQRV AVTLNQHIRQ WESQHEQLLK
ICRNCSCSVE RHISCVSLDC PVLYKLSRVN RQLSRAPYLR QLLEQF
//
