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Database: UniProt
Entry: A0A2K6CDH8_MACNE
LinkDB: A0A2K6CDH8_MACNE
Original site: A0A2K6CDH8_MACNE 
ID   A0A2K6CDH8_MACNE        Unreviewed;      3124 AA.
AC   A0A2K6CDH8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:ENSMNEP00000021721.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000021721.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000021721.1}
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   RefSeq; XP_011757276.1; XM_011758974.1.
DR   STRING; 9545.ENSMNEP00000021721; -.
DR   Ensembl; ENSMNET00000045973.1; ENSMNEP00000021721.1; ENSMNEG00000034577.1.
DR   GeneID; 105492089; -.
DR   KEGG; mni:105492089; -.
DR   CTD; 5980; -.
DR   GeneTree; ENSGT00940000156226; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000034577; Expressed in pituitary gland and 12 other cell types or tissues.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:Ensembl.
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:0042276; P:error-prone translesion synthesis; IEA:Ensembl.
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; 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; 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; 2.
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:UP000233120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          95..191
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          747..1133
FT                   /note="DUF4683"
FT                   /evidence="ECO:0000259|Pfam:PF15735"
FT   DOMAIN          2266..2478
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          2544..2994
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          3036..3103
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          266..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1164..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1841..1869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1958..1980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2014..2149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2211..2230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1060
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1571..1585
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1841..1868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1958..1979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2061..2093
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2215..2230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3124 AA;  352106 MW;  04DAFD18AEC7853D CRC64;
     MFSVRIVTAD YYMASPLQGL DTCQSPLTQA PVKKVPVVRI FGATPAGQKT CLHLHGIFPY
     LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER
     HFMKIYLYNP AVVKRICELL QSGAIMNKFY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV
     KFRKARRKSN TLYATGSCKN HLSRNSLAGS LFRWEQDEIP SSLILEGVEP QSTCELEVDA
     VAADILNRLD IEAQIGRNPG LQAIWEDEKQ RRRNRNETSQ ISQPESQDHR FVPATESEKK
     FQKRLQEILK QNDFSVTLSG SVDYSDGSQE FSAELTLHSE VLSPEMLQCT PANMVEVHKD
     KESSKGHTRH KVEEALINEE AILNLMENSQ TFQPLTQRLS ESPVFMDSSP DEALVHLLAG
     LESDGYRGER NRMPSPCRSF GNNKYPQNSD DEENEPQIEK EEMELSLVMS QRWDSNIEEH
     CAKKRSLCRN THRSSTEDDD SSSEEEMEWS DNSLLLANLS IPQLDGTADE NSDNPLNNEN
     SRTHSSVIAT SKLSVKPSIF HKDAATLEPS SSAKITFQCK HTSALSSHVL NKEDLIEDLS
     QTNKNIEKGL DNSVTSFTNE STYSVKYPGS LSSTVHSENS HKENSKKEIL PVSSCESSIF
     DYEEDIPSVT RQVPSRKYTN IRKIEKDSPF IHMHRHPNEN TLGKNSFNFS DLNHSKNKVS
     SEGNEKGNST ALSSLFPSSF TENCELLSCS GENRTMVHSL NSTADESGLN KLKIRYEEFQ
     EHKTEKPSLS QQAAHYMFFP SVVLSNCLTR PQKLSPVTYK LQPGNKPSRL KLNKKKLAGH
     QETFTKSSET GSTKDNSIQN NPCNSNPEKD SAFASDLTKT SRGAFENKTP TDGFIDCHFG
     DGTLETEQSF GLYGNKYTLR AKRKVNYETE DSESSFVTHN SKISLPHPME IGESLDGTLK
     SRKRRKMSKK LPPVIIKYII INRFRGRKNM LVKLGKIDAK EKQVILTEEK MELYKKLAPL
     KDFWPKVPDS PATKYPIYPL TPKKSHRRKS KHKSAKKKTG KQQRTNNENI KRTLSFRKKR
     SHALLSPPSP SYNAETEDCD LNYSDVMSKL GFLSERSTSP INSSPPRCWS PTDPRAEEIM
     AAAEKEAMLF KGPNVYNKTV NSRIGKNSRA RAQVKKSKAK LVNPSVVTKK RNKRNQTNKL
     VDDGKKKPRA KQKTNAKGTS RKHKTLKDEK IKSQSGAEVK FVLKHQNVSE FASSSGGAQL
     LFKQKDMPLM GSAVDHPLSA PLPTGINAQQ KLSGCFSSFL ESKKSVDVQT FPSSRDDLHP
     SVVCNSIGPG ISKINVQRPH NQSAIFTLKE STLIQKNVFD LSNHLSQVAQ NTQISSGMSS
     KIEDNANNIQ KNYLSSIGKL SEYRNSLESK LDQAYTPNFL HCKDSQQQIV CIAEQSKHSE
     TCSPGNTASD ESQMPNNCFV TSLRSPIKQI AWEQKQRGFI LDMSNFKPER VKQRSLSEAI
     SQTKALSQCK TPAPSAFGEG QSGLAVLKEL LQKRQQKAQN ANIIQDPLSN KHQPNKNISG
     SLEHNKANKR TRSVTSPRKP RTPRSTKPKE KIPKLLKVDS LNLQNSSQLD NSVSDDSPIF
     FSDPGFESCY SLEDSLSPEH NYNFDINTIG QTGFCSFYSG SQFVPADQNL PQKFLSDAVQ
     DLFPGQAIEK NEFLSHDNQK CEEDKHTTDS ASWIRSGTLS PEIFEKSSID SIENHRHNQW
     KNSFHPLTTR SNSIMDSFCV QQAEDCLNEK SRLNRSSVSK EVFLSLPQPN NSDWIQGHTR
     KEMGRSLDSA NTSFTAILSS PDGELVDMAC EDLELYVSRN NDMLTPTPDS SPRSTSSPSQ
     SKNGSFTPRT AHILKPLMSP PSREEIMATL LDHDLSETIY QEPFCSNPSD VPEKPREIGG
     RLLMVETRLA NDLAEFEGDF SLEGLRLWKT AFSAMTQNPR PGSPLRSGQG VVNKGSSNSP
     KMVEDKKIVI MPCKCAPSRQ LVQVWLQAKE QYERSKKLPK TKPTGVVKSA ENFSSSVNPD
     DKPVVPPKMD VSPRILPTTA HTKEDVNSRI ALQAPTTGCS QTASESQMLP PVASSSDPEK
     DEDDDNYYIN YSSPDSPVIP PWQQPVSPDS KALNGDDRPS SPVEELPSLG VENFLKPIKD
     GIQKSPCSEP QEPLVISPIN ARARTEKCES LCLHSTPIIQ RKLLERLPEA TGLSPLSTEP
     KTQKLSNKKG SNTDTLRRVL LTQAKNQFAA VNTPQKETSQ IDGPSLNNTY GFKVSIQNLQ
     EAKALHEIQN LTLISVELHA RTRRDLEPDP EFDPICALFY CISSDAPLPD TEKTELTGVI
     VIDKDKTVFS QDIRYQTPLL IRSGITGLEV TYAADEKALF HEIANIIKRY DPDILLGYEI
     QMHSWGYLLQ RAAALSVDLC QMISRVPDDK IENRFAAERD EYGSYTMSEI NIVGRITLNL
     WRIMRNEVAL TNYTFENVSF HVLHQRFPLF TFRVLSDWFD NKTDLYRWKM VDHYVSRVRG
     NLQMLEQLDL IGKTSEMARL FGIQFLHVLT RGSQYRVESM MLRIAKPMNY IPVTPSVQQR
     SQMRAPQCVP LIMEPESRFY SNSVLVLDFQ SLYPSIVIAY NYCFSTCLGH VENLGKYDEF
     KFGCTSLRVP PDLLYQVRHD ITVSPNGVAF VKPSVRKGVL PRMLEEILKT RFMVKQSMKA
     YKQDRALSRM LDARQLGLKL IANVTFGYTA ANFSGRMPCI EVGDSIVHKA RETLERAIKL
     VNDTKKWGAR VVYGDTDSMF VLLKGATKEQ SFKIGQEIAE AVTATNPKPV KLKFEKVYLP
     CVLQTKKRYV GYMYETLDQK DPVFDAKGIE TVRRDSCPAV SKILERSLKL LFETRDISLI
     KQYVQRQCMK LLEGKASIQD FIFAKEYRGS FSYKPGACVP ALELTRKMLT YDRRSEPQVG
     ERVPYVIIYG TPGVPLIQLV RRPVEVLQDP TLRLNATYYI TKQILPPLAR IFSLIGIDVF
     SWYHELPRIH KATNSSRSEP EGRKGTISQY FTTLHCPVCD DLTQHGICSK CRSQPQHVAV
     ILNQEIRELE RKQEQLVKIC KNCTGCFDRH IPCVSLNCPV LFKVSRVNRE LSKAPYLRQL
     LDQF
//
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