ID U1GSN8_ENDPU Unreviewed; 2530 AA.
AC U1GSN8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000256|ARBA:ARBA00021589};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=EPUS_08061 {ECO:0000313|EMBL:ERF75016.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF75016.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755}.
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DR EMBL; KE720844; ERF75016.1; -; Genomic_DNA.
DR RefSeq; XP_007787673.1; XM_007789483.1.
DR GeneID; 19242939; -.
DR eggNOG; KOG0968; Eukaryota.
DR eggNOG; KOG2238; Eukaryota.
DR HOGENOM; CLU_000203_0_0_1; -.
DR OMA; WTKILQG; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
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:0008289; F:lipid 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:0006869; P:lipid transport; IEA:UniProtKB-KW.
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; cd21675; SMP_TEX2; 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; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR031468; SMP_LBD.
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; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
DR PROSITE; PS51847; SMP; 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1913..2106
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 486..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2377..2530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2165..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2251..2267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2488..2521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2530 AA; 283330 MW; D03FCC0297619554 CRC64;
METFRVRLNC IDHYQAAPTG FDPPVPHGIS NVNIKERPKV SVIRVFGATE TGQKVLMHIH
GAFQYLYIEY SGSLIDEEVK VAIRTLQLSI DQALAVSYRK NDGKPAYVAH ISLVKGIPFY
GFHVGYKFFM KIYLLNPLHM TRLADLLREG AVMKRVLQPY ESHMQYLAQW MCDYNLFGCG
YIDCKKVKFR GPVPDFFEMN SSSHRWHDRS IPSEYVSNED TLPKQSHCSL EVDVHVEDIL
NREDVQARAL HHDFVERIHP LPLDAKLVPS MAGLWKDETR RRKARLGLID TSSSPFPPEV
LVTMSANPRA SQAGGWIHEE EYRQKADKLA REEHEQGIGQ KITFDNFVKT IPFESTVNTA
LESVEDLYTK NLPQGDPASL GRDPAAGYAL GPQTELVDEA WVAQIRDEAT SEPENGVPIA
HGPMSNGAKV SSFLDSSNTS AERLATDVTP PISSSEFDHL GIRKAGDLSH VSEDAFEIPD
EFLVSGNTLN GHKRRPLEPL TSSSEPQKKK RKVLVDEEHL LPDIDPEIHP PLRLVHTPAT
VDYRLSSTNV EQSAQNGFKQ KPGSQTTTEQ HGSQTNGTLR DSKLPFPVVK DPSDTNAIMR
LSQQSNPSLK LSQDIQSKPT VSTSISQHTP SKASVSSSQK TPFSAMSSDL LPLLPAIPPD
LSIPGSNVKT LMFGLACPSF SEVQTTMCMQ GLPDVIYQNA YYGDETDVPD RQREYGGREF
RLESNTVPYL PDFDATGSSP ATYGRRNQTL LDEVQEEKAD RKRRRLCKIT RWSIADQPPT
KAEVTAWLER ENSLAMAPSH SDGKMKEDTN LLSQIDVPTQ KNKHGFKYSQ KHESTSVQHE
TQYMSIMSLE VHVNTRGNLA PNPEEDEIAC LFWSVQSDND DFDANGSQAG RHTGVLVNDK
SGRIAKNVSR DVPVEVEAEP TELDVLTRMT DIVRQYDPDI LTGYEVHNNS WGYLIERARV
KYELNLCDEM SRMKSHSHGR FGKEDDKWGF NQTSTIRITG RHTINIWRAM RGELNLLQYT
MENVVFHLLH RRIPHYKFTD LTAWYKSTIP RDLSKVIEYF VSRVQIDLDI LESNELVPRT
SEQARLLGVD WFSVISRGSQ FKVESLMFRI AKPENFILVS PSRRQVGGQN ALECLPLVME
PQSDFYTSPM LVLDFQSLYP SIMIAYNYCY STFLGRVVSW RGTNKMGFTD YRREQRLIEL
LKDHINIAPN GIMYAKTHIR KSLLAKMLGE ILETRVMVKS GMKVDKNDKT LQRLLNNRQL
ALKLIANVTY GYTSASFSGR MPCSEIADSI VQTARETLEK AIAVIHSREK WGAEVVYGDT
DSLFVYLKGR TREQAFDIGE DIAKTITKMN PRPVKLKFEK VYHPCVLLAK KRYVGFKYEH
RDQKEPDFDA KGIETVRRDG TPAEQKIEEK ALKILFKTAD LSQVKSFFQS QCTKIMKGQV
SIQDFCFARE VKLGTYSDKG PPPPGALISA RRMIEDPRLE PQYGERVPYV VITGGPGARL
IDRCVAPEVL LQDAQLELDS EYYISKNLIP PLERIFNLVG ANVRQWYDEM PKFQRIRRVE
GVLAPDGRDA LTRKTLESYM KSSTCIVCRE SLDGDSPICN SCFEQSPQTT LLLRARMTKA
ERKAIQLNRI CRSCSGLGWT EEVKCDSKDC PVFYSRTRHM ANMNNTKAQV GPVLRMLEEK
GGGGFDCTLK RAHDDDAVLK SGADVLAEQF TRKHESDVAA GYFAVCREYV PGGVNGKPPE
RTTPSGEVVA AESPSVYQSM YRSIFDRQQK PTIQPNKADG KPVKRARNVF FVVLRHGHLM
LYDDSEQLEV RHVISLEHHD VSIYGGPEEI PEGELWIKRN AICLTRSKRA ATTTQTTSLP
FFLFCENSSE KEDFYFALLK NQEKIPGAKD SPPVPQEYEI KDIITLVQKL HSSEEQLQTR
WLNALVGRLF LSMYKTPEVE AFIRKKMTKK ISRVKKPNFI TRLALQRIDM GEGAPFLTNP
KLKDLTVNGD CTAEGDFKYS GKFRIEIAAT ARLDLGTRFK AREVELVLAV VVNKLEGHGL
IRFKPPPSNR VWVAFETMPN LDLKIEPIVS SRQITYNVVL RAIESRIREV FAETLVLPFW
DDIPFLDTGE EAFRGGVWKR EVKPAQPVEI KQEMPEDEGE AGESHVDASV DTIKSSHDRT
VSELHLPPSP TNGLKSRAGR STKVSGEDLG RSSSVAADKL HRPEPPRALR SSSFASLADP
MVSPSHADAD GRQRLLDPPQ RKDAAQAMLK ELSSKSITAS PADSPAGSPP NETALAAALI
AASRPSSKAS DESLSIRNPR QQSESSSIQT NSQSSTLTSP IAGSEDSKAP SLNEGPSRTS
TLGSIRSLAS SAEKRQGINL SSATAAAKNW GWGVLARNQQ REKEAAAQHN KLGTPELPMG
RGRPLPPPGT PLPHPERSIL SALPLPKRRP VPAPAPSDRT TITDSSRLST PKPNQTTRRK
RQSPAQKDEQ PDEVLVVEAP VDSNPPTPAA DDEHHDEFFG HGEDSNGSAS QKIDDRPELQ
SRSDSGGTPA
//
